ryanodine receptor 3 isoform X13 [Homo sapiens]
Protein Classification
ryanodine receptor( domain architecture ID 11696383)
ryanodine receptor is a calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction; similar to human ryanodine receptor 2, also called cardiac muscle ryanodine receptor
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| beta-trefoil_MIR_RyR3 | cd23292 | MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ... |
180-369 | 4.07e-132 | |||||
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, also called RYR-3, or brain ryanodine receptor-calcium release channel, or brain-type ryanodine receptor, or type 3 ryanodine receptor, is a calcium channel that plays a role in cellular calcium signaling. It mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. It also mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. RYR-3 forms homotetramer and also forms heterotetramer with RYR-2. RYR-3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. : Pssm-ID: 467763 [Multi-domain] Cd Length: 187 Bit Score: 412.38 E-value: 4.07e-132
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| RR_TM4-6 | pfam06459 | Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ... |
4194-4464 | 5.90e-112 | |||||
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 family. : Pssm-ID: 461918 Cd Length: 282 Bit Score: 358.63 E-value: 5.90e-112
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| SPRY1_RyR | cd12877 | SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ... |
605-756 | 2.83e-85 | |||||
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this first SPRY domain of the RyRs. : Pssm-ID: 240457 Cd Length: 151 Bit Score: 276.50 E-value: 2.83e-85
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| RYDR_ITPR | pfam01365 | RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ... |
406-585 | 2.99e-80 | |||||
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3. : Pssm-ID: 460175 Cd Length: 199 Bit Score: 264.06 E-value: 2.99e-80
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| SPRY2_RyR | cd12878 | SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ... |
1036-1168 | 1.75e-79 | |||||
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1 : Pssm-ID: 240458 Cd Length: 133 Bit Score: 259.15 E-value: 1.75e-79
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| RYDR_ITPR | pfam01365 | RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ... |
1987-2197 | 1.69e-75 | |||||
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3. : Pssm-ID: 460175 Cd Length: 199 Bit Score: 250.58 E-value: 1.69e-75
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| SPRY3_RyR | cd12879 | SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ... |
1288-1426 | 1.87e-72 | |||||
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this third SPRY domain of the RyRs. : Pssm-ID: 293937 Cd Length: 151 Bit Score: 239.90 E-value: 1.87e-72
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| Ins145_P3_rec super family | cl48031 | Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ... |
14-176 | 1.39e-55 | |||||
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity. The actual alignment was detected with superfamily member pfam08709: Pssm-ID: 462572 [Multi-domain] Cd Length: 212 Bit Score: 193.87 E-value: 1.39e-55
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| RyR | pfam02026 | RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ... |
813-901 | 7.68e-46 | |||||
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown. : Pssm-ID: 460419 Cd Length: 90 Bit Score: 161.13 E-value: 7.68e-46
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| RyR | pfam02026 | RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ... |
2562-2651 | 1.93e-45 | |||||
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown. : Pssm-ID: 460419 Cd Length: 90 Bit Score: 159.98 E-value: 1.93e-45
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| RyR | pfam02026 | RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ... |
927-1016 | 7.37e-41 | |||||
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown. : Pssm-ID: 460419 Cd Length: 90 Bit Score: 146.88 E-value: 7.37e-41
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| RIH_assoc | pfam08454 | RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ... |
3687-3804 | 2.71e-35 | |||||
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1,4,5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels. There seems to be no known function for this domain. Also see the IP3-binding domain pfam01365 and pfam02815. : Pssm-ID: 462482 Cd Length: 98 Bit Score: 131.49 E-value: 2.71e-35
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| RyR super family | cl03409 | RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ... |
2680-2759 | 3.88e-25 | |||||
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown. The actual alignment was detected with superfamily member pfam02026: Pssm-ID: 460419 Cd Length: 90 Bit Score: 102.20 E-value: 3.88e-25
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| Ion_trans | pfam00520 | Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
4581-4741 | 4.00e-25 | |||||
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane. : Pssm-ID: 459842 [Multi-domain] Cd Length: 238 Bit Score: 107.35 E-value: 4.00e-25
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| EF-hand_7 | pfam13499 | EF-hand domain pair; |
3888-3943 | 4.80e-04 | |||||
EF-hand domain pair; : Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 41.47 E-value: 4.80e-04
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| Name | Accession | Description | Interval | E-value | |||||
| beta-trefoil_MIR_RyR3 | cd23292 | MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ... |
180-369 | 4.07e-132 | |||||
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, also called RYR-3, or brain ryanodine receptor-calcium release channel, or brain-type ryanodine receptor, or type 3 ryanodine receptor, is a calcium channel that plays a role in cellular calcium signaling. It mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. It also mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. RYR-3 forms homotetramer and also forms heterotetramer with RYR-2. RYR-3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467763 [Multi-domain] Cd Length: 187 Bit Score: 412.38 E-value: 4.07e-132
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| RR_TM4-6 | pfam06459 | Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ... |
4194-4464 | 5.90e-112 | |||||
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 family. Pssm-ID: 461918 Cd Length: 282 Bit Score: 358.63 E-value: 5.90e-112
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| SPRY1_RyR | cd12877 | SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ... |
605-756 | 2.83e-85 | |||||
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this first SPRY domain of the RyRs. Pssm-ID: 240457 Cd Length: 151 Bit Score: 276.50 E-value: 2.83e-85
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| RYDR_ITPR | pfam01365 | RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ... |
406-585 | 2.99e-80 | |||||
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3. Pssm-ID: 460175 Cd Length: 199 Bit Score: 264.06 E-value: 2.99e-80
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| SPRY2_RyR | cd12878 | SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ... |
1036-1168 | 1.75e-79 | |||||
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1 Pssm-ID: 240458 Cd Length: 133 Bit Score: 259.15 E-value: 1.75e-79
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| MIR | pfam02815 | MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ... |
180-361 | 7.97e-77 | |||||
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function. Pssm-ID: 397103 [Multi-domain] Cd Length: 185 Bit Score: 253.83 E-value: 7.97e-77
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| RYDR_ITPR | pfam01365 | RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ... |
1987-2197 | 1.69e-75 | |||||
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3. Pssm-ID: 460175 Cd Length: 199 Bit Score: 250.58 E-value: 1.69e-75
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| SPRY3_RyR | cd12879 | SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ... |
1288-1426 | 1.87e-72 | |||||
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this third SPRY domain of the RyRs. Pssm-ID: 293937 Cd Length: 151 Bit Score: 239.90 E-value: 1.87e-72
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| Ins145_P3_rec | pfam08709 | Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ... |
14-176 | 1.39e-55 | |||||
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity. Pssm-ID: 462572 [Multi-domain] Cd Length: 212 Bit Score: 193.87 E-value: 1.39e-55
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| RyR | pfam02026 | RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ... |
813-901 | 7.68e-46 | |||||
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown. Pssm-ID: 460419 Cd Length: 90 Bit Score: 161.13 E-value: 7.68e-46
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| RyR | pfam02026 | RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ... |
2562-2651 | 1.93e-45 | |||||
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown. Pssm-ID: 460419 Cd Length: 90 Bit Score: 159.98 E-value: 1.93e-45
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| RyR | pfam02026 | RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ... |
927-1016 | 7.37e-41 | |||||
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown. Pssm-ID: 460419 Cd Length: 90 Bit Score: 146.88 E-value: 7.37e-41
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| RIH_assoc | pfam08454 | RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ... |
3687-3804 | 2.71e-35 | |||||
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1,4,5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels. There seems to be no known function for this domain. Also see the IP3-binding domain pfam01365 and pfam02815. Pssm-ID: 462482 Cd Length: 98 Bit Score: 131.49 E-value: 2.71e-35
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| SPRY | smart00449 | Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ... |
1048-1170 | 1.41e-31 | |||||
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues. Pssm-ID: 214669 Cd Length: 122 Bit Score: 121.63 E-value: 1.41e-31
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| SPRY | pfam00622 | SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ... |
623-758 | 3.43e-25 | |||||
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin. Pssm-ID: 459877 Cd Length: 121 Bit Score: 103.58 E-value: 3.43e-25
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| RyR | pfam02026 | RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ... |
2680-2759 | 3.88e-25 | |||||
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown. Pssm-ID: 460419 Cd Length: 90 Bit Score: 102.20 E-value: 3.88e-25
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| Ion_trans | pfam00520 | Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
4581-4741 | 4.00e-25 | |||||
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane. Pssm-ID: 459842 [Multi-domain] Cd Length: 238 Bit Score: 107.35 E-value: 4.00e-25
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| SPRY | pfam00622 | SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ... |
1050-1170 | 1.24e-21 | |||||
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin. Pssm-ID: 459877 Cd Length: 121 Bit Score: 93.18 E-value: 1.24e-21
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| SPRY | pfam00622 | SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ... |
1292-1427 | 6.18e-20 | |||||
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin. Pssm-ID: 459877 Cd Length: 121 Bit Score: 88.55 E-value: 6.18e-20
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| SPRY | smart00449 | Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ... |
1292-1428 | 3.59e-19 | |||||
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues. Pssm-ID: 214669 Cd Length: 122 Bit Score: 86.19 E-value: 3.59e-19
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| SPRY | smart00449 | Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ... |
623-757 | 4.38e-17 | |||||
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues. Pssm-ID: 214669 Cd Length: 122 Bit Score: 80.42 E-value: 4.38e-17
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| MIR | smart00472 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
239-332 | 8.45e-07 | |||||
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 48.88 E-value: 8.45e-07
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| MIR | smart00472 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
64-119 | 1.24e-05 | |||||
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 45.41 E-value: 1.24e-05
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| EF-hand_7 | pfam13499 | EF-hand domain pair; |
3888-3943 | 4.80e-04 | |||||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 41.47 E-value: 4.80e-04
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| Name | Accession | Description | Interval | E-value | |||||
| beta-trefoil_MIR_RyR3 | cd23292 | MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, ... |
180-369 | 4.07e-132 | |||||
MIR domain, beta-trefoil fold, found in ryanodine receptor 3 (RyR3) and similar proteins; RyR3, also called RYR-3, or brain ryanodine receptor-calcium release channel, or brain-type ryanodine receptor, or type 3 ryanodine receptor, is a calcium channel that plays a role in cellular calcium signaling. It mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. It also mediates Ca(2+)-induced Ca(2+) release from the endoplasmic reticulum in non-muscle cells. RYR-3 forms homotetramer and also forms heterotetramer with RYR-2. RYR-3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467763 [Multi-domain] Cd Length: 187 Bit Score: 412.38 E-value: 4.07e-132
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| RR_TM4-6 | pfam06459 | Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 ... |
4194-4464 | 5.90e-112 | |||||
Ryanodine Receptor TM 4-6; This region covers TM regions 4-6 of the ryanodine receptor 1 family. Pssm-ID: 461918 Cd Length: 282 Bit Score: 358.63 E-value: 5.90e-112
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| beta-trefoil_MIR_RyR | cd23278 | MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also ... |
184-365 | 1.04e-102 | |||||
MIR domain, beta-trefoil fold, found in the family of ryanodine receptor (RyR); RyRs (also called RYRs) are intracellular Ca(2+) release channels located on the sarco/endoplasmic reticulum (SR/ER). They release calcium Ca(2+) intracellular stores to activate critical functions including muscle contraction and neurotransmitter release. The family includes three closely homologous proteins, RyR1, RyR2 and RyR3. RyR1 is present in skeletal muscle; RyR2 is in heart muscle; and RyR3 is expressed at low levels in many tissues including brain, smooth muscle, and slow-twitch skeletal muscle. RYR2 is the major cellular mediator of calcium-induced calcium release (CICR) in animal cells. RyR1 and RyR2 release Ca2+ from the ER in response to excitation of muscle membranes to promote muscle contraction. RYR3 is involved in force production and calcium handling in extraocular muscle. RYRs contain an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467749 [Multi-domain] Cd Length: 180 Bit Score: 327.73 E-value: 1.04e-102
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| beta-trefoil_MIR_RyR1 | cd23290 | MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, ... |
175-369 | 1.70e-102 | |||||
MIR domain, beta-trefoil fold, found in ryanodine receptor 1 (RyR1) and similar proteins; RyR1, also called RYR-1, or skeletal muscle calcium release channel, or skeletal muscle ryanodine receptor, or skeletal muscle-type ryanodine receptor, or type 1 ryanodine receptor, is a calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. It can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. It is required for normal embryonic development of muscle fibers and skeletal muscle, as well as for normal heart morphogenesis, skin development and ossification during embryogenesis. RYR-1 forms homotetramer and can also form heterotetramers with RYR-2. RYR-1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467761 [Multi-domain] Cd Length: 192 Bit Score: 327.62 E-value: 1.70e-102
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| SPRY1_RyR | cd12877 | SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ... |
605-756 | 2.83e-85 | |||||
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this first SPRY domain of the RyRs. Pssm-ID: 240457 Cd Length: 151 Bit Score: 276.50 E-value: 2.83e-85
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| RYDR_ITPR | pfam01365 | RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ... |
406-585 | 2.99e-80 | |||||
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3. Pssm-ID: 460175 Cd Length: 199 Bit Score: 264.06 E-value: 2.99e-80
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| SPRY2_RyR | cd12878 | SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ... |
1036-1168 | 1.75e-79 | |||||
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1 Pssm-ID: 240458 Cd Length: 133 Bit Score: 259.15 E-value: 1.75e-79
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| beta-trefoil_MIR_RyR2 | cd23291 | MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, ... |
184-369 | 3.97e-77 | |||||
MIR domain, beta-trefoil fold, found in ryanodine receptor 2 (RyR2) and similar proteins; RyR2, also called RYR-2, or cardiac muscle ryanodine receptor-calcium release channel, or cardiac muscle ryanodine receptor, or type 2 ryanodine receptor, is a calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity of RYR-2 is modulated by formation of heterotetramers with RYR-3. RYR-2 is required for cellular calcium ion homeostasis. it plays an essential role in embryonic heart development. RYR-2 forms homotetramer and also forms heterotetramers with RYR-1 and RYR-3. RYR-2 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467762 [Multi-domain] Cd Length: 184 Bit Score: 254.58 E-value: 3.97e-77
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| MIR | pfam02815 | MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may ... |
180-361 | 7.97e-77 | |||||
MIR domain; The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function. Pssm-ID: 397103 [Multi-domain] Cd Length: 185 Bit Score: 253.83 E-value: 7.97e-77
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| RYDR_ITPR | pfam01365 | RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types ... |
1987-2197 | 1.69e-75 | |||||
RIH domain; The RIH (RyR and IP3R Homology) domain is an extracellular domain from two types of calcium channels. This region is found in the ryanodine receptor and the inositol-1,4,5- trisphosphate receptor. This domain may form a binding site for IP3. Pssm-ID: 460175 Cd Length: 199 Bit Score: 250.58 E-value: 1.69e-75
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| SPRY3_RyR | cd12879 | SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of ... |
1288-1426 | 1.87e-72 | |||||
SPRY domain 3 (SPRY3) of ryanodine receptor (RyR); This SPRY domain (SPRY3) is the third of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this third SPRY domain of the RyRs. Pssm-ID: 293937 Cd Length: 151 Bit Score: 239.90 E-value: 1.87e-72
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| Ins145_P3_rec | pfam08709 | Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding ... |
14-176 | 1.39e-55 | |||||
Inositol 1,4,5-trisphosphate/ryanodine receptor; This domain corresponds to the ligand binding region on inositol 1,4,5-trisphosphate receptor, and the N terminal region of the ryanodine receptor. Both receptors are involved in Ca2+ release. They can couple to the activation of neurotransmitter-gated receptors and voltage-gated Ca2+ channels on the plasma membrane, thus allowing the endoplasmic reticulum discriminate between different types of neuronal activity. Pssm-ID: 462572 [Multi-domain] Cd Length: 212 Bit Score: 193.87 E-value: 1.39e-55
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| RyR | pfam02026 | RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ... |
813-901 | 7.68e-46 | |||||
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown. Pssm-ID: 460419 Cd Length: 90 Bit Score: 161.13 E-value: 7.68e-46
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| RyR | pfam02026 | RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ... |
2562-2651 | 1.93e-45 | |||||
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown. Pssm-ID: 460419 Cd Length: 90 Bit Score: 159.98 E-value: 1.93e-45
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| RyR | pfam02026 | RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ... |
927-1016 | 7.37e-41 | |||||
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown. Pssm-ID: 460419 Cd Length: 90 Bit Score: 146.88 E-value: 7.37e-41
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| RIH_assoc | pfam08454 | RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) ... |
3687-3804 | 2.71e-35 | |||||
RyR and IP3R Homology associated; This eukaryotic domain is found in ryanodine receptors (RyR) and inositol 1,4,5-trisphosphate receptors (IP3R) which together form a superfamily of homotetrameric ligand-gated intracellular Ca2+ channels. There seems to be no known function for this domain. Also see the IP3-binding domain pfam01365 and pfam02815. Pssm-ID: 462482 Cd Length: 98 Bit Score: 131.49 E-value: 2.71e-35
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| SPRY | smart00449 | Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ... |
1048-1170 | 1.41e-31 | |||||
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues. Pssm-ID: 214669 Cd Length: 122 Bit Score: 121.63 E-value: 1.41e-31
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| SPRY | cd11709 | SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ... |
1049-1166 | 7.20e-26 | |||||
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome. Pssm-ID: 293931 Cd Length: 118 Bit Score: 105.21 E-value: 7.20e-26
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| SPRY | pfam00622 | SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ... |
623-758 | 3.43e-25 | |||||
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin. Pssm-ID: 459877 Cd Length: 121 Bit Score: 103.58 E-value: 3.43e-25
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| RyR | pfam02026 | RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four ... |
2680-2759 | 3.88e-25 | |||||
RyR domain; This domain is called RyR for Ryanodine receptor. The domain is found in four copies in the ryanodine receptor. The function of this domain is unknown. Pssm-ID: 460419 Cd Length: 90 Bit Score: 102.20 E-value: 3.88e-25
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| Ion_trans | pfam00520 | Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ... |
4581-4741 | 4.00e-25 | |||||
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane. Pssm-ID: 459842 [Multi-domain] Cd Length: 238 Bit Score: 107.35 E-value: 4.00e-25
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| SPRY | pfam00622 | SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ... |
1050-1170 | 1.24e-21 | |||||
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin. Pssm-ID: 459877 Cd Length: 121 Bit Score: 93.18 E-value: 1.24e-21
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| SPRY | pfam00622 | SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ... |
1292-1427 | 6.18e-20 | |||||
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin. Pssm-ID: 459877 Cd Length: 121 Bit Score: 88.55 E-value: 6.18e-20
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| SPRY | smart00449 | Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ... |
1292-1428 | 3.59e-19 | |||||
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues. Pssm-ID: 214669 Cd Length: 122 Bit Score: 86.19 E-value: 3.59e-19
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| SPRY | cd11709 | SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ... |
623-754 | 6.90e-19 | |||||
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome. Pssm-ID: 293931 Cd Length: 118 Bit Score: 85.18 E-value: 6.90e-19
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| beta-trefoil_MIR_itr-1-like | cd23280 | MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate ... |
179-362 | 1.90e-18 | |||||
MIR domain, beta-trefoil fold, found in Caenorhabditis elegans inositol 1,4,5-trisphosphate receptor Itr-1 and similar proteins; Itr-1, also called IP3 receptor, or IP3R, or InsP3R, or LET-23 fertility effector 1, is a receptor for inositol 1,4,5-trisphosphate, a second messenger that regulates intracellular calcium homeostasis. It binds in vitro to both inositol 1,4,5-trisphosphate (1,4,5-InsP3) and inositol 2,4,5-trisphosphate (2,4,5-InsP3) with high affinity. It can also bind inositol 1,3,4,5-tetrakisphosphate (1,3,4,5-InsP4) and inositol 4,5-bisphosphate (4,5-InsP2), but with lower affinity. Itr-1 acts as a timekeeper/rhythm generator via calcium signaling, affecting the defecation cycle and pharyngeal pumping. It affects normal hermaphrodite and male fertility as a participant in intracellular signaling by acting downstream of let-23/lin-3 which regulates ovulation, spermathecal valve dilation and male mating behavior. It plays an important role in early embryonic development. It controls epidermal cell migration and may also regulate filopodial protrusive activity during epithelial morphogenesis. Itr-1 functions as a component of inositol trisphosphate (IP3)-mediated downstream signaling pathways that controls amphid sensory neuronal (ASH)-mediated response to nose touch and benzaldehyde, but no other ASH-mediated responses. Itr-1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467751 [Multi-domain] Cd Length: 199 Bit Score: 86.67 E-value: 1.90e-18
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| SPRY_RNF123 | cd12882 | SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the ... |
1045-1129 | 3.30e-18 | |||||
SPRY domain at N-terminus of ring finger protein 123; This SPRY domain is found at the N-terminus of RING finger protein 123 domain (also known as E3 ubiquitin-protein ligase RNF123). The ring finger domain motif is present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RNF123 displays E3 ubiquitin ligase activity toward the cyclin-dependent kinase inhibitor p27 (Kip1). Pssm-ID: 293940 Cd Length: 128 Bit Score: 83.53 E-value: 3.30e-18
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| SPRY | smart00449 | Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ... |
623-757 | 4.38e-17 | |||||
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues. Pssm-ID: 214669 Cd Length: 122 Bit Score: 80.42 E-value: 4.38e-17
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| SPRY_Ash2 | cd12872 | SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ... |
1043-1132 | 1.96e-16 | |||||
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or homeotic discs 2) -like proteins, core components of all mixed-lineage leukemia (MLL) family histone methyltransferases. Ash2 is a member of the trithorax group of transcriptional regulators of the Hox genes. Recent studies show that the SPRY domain of Ash2 mediates the interaction with RbBP5 and has an important role in regulating the methyltransferase activity of MLL complexes. In yeast, Ash2 is involved in histone methylation and is required for the earliest stages of embryogenesis. Pssm-ID: 293932 Cd Length: 150 Bit Score: 79.48 E-value: 1.96e-16
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| beta-trefoil_MIR | cd23263 | MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) ... |
185-354 | 6.99e-15 | |||||
MIR domain, beta-trefoil fold, found in the MIR (protein mannosyltransferase, IP3R and RyR) superfamily; The MIR superfamily includes dolichyl-phosphate-mannose-protein mannosyltransferases (PMTs), inositol 1,4,5-trisphosphate receptors (ITPRs/IP3R), ryanodine receptors (RyRs), and stromal cell-derived factor 2 (SDF-2)-like proteins. They all contain a MIR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The MIR domain may have a ligand transferase function. Pssm-ID: 467746 [Multi-domain] Cd Length: 172 Bit Score: 75.50 E-value: 6.99e-15
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| SPRY_RING | cd12883 | SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ... |
1049-1129 | 1.06e-14 | |||||
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development. Pssm-ID: 293941 Cd Length: 121 Bit Score: 73.54 E-value: 1.06e-14
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| SPRY_DDX1 | cd12873 | SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ... |
1048-1132 | 7.84e-12 | |||||
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay. Pssm-ID: 293933 Cd Length: 155 Bit Score: 66.44 E-value: 7.84e-12
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| SPRY_RanBP_like | cd12885 | SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY ... |
1036-1132 | 2.75e-11 | |||||
SPRY domain in Ran binding proteins, SSH4, HECT E3 and SPRYD3; This family includes SPRY domains found in Ran binding proteins (RBP or RanBPM) 9 and 10, SSH4 (suppressor of SHR3 null mutation protein 4), SPRY domain-containing protein 3 (SPRYD3) as well as HECT, a C-terminal catalytic domain of a subclass of ubiquitin-protein ligase (E3). RanBP9 and RanBP10 act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. The SPRY domain in SSH4 may be involved in cargo recognition, either directly or by combination with other adaptors, possibly leading to a higher selectivity. SPRYD3 is highly expressed in most tissues in humans, possibly involved in important cellular processes. HECT E3 mediates the direct transfer of ubiquitin from E2 to substrate. Pssm-ID: 293943 Cd Length: 132 Bit Score: 63.84 E-value: 2.75e-11
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| SPRY | cd11709 | SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ... |
1293-1413 | 7.34e-10 | |||||
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome. Pssm-ID: 293931 Cd Length: 118 Bit Score: 59.37 E-value: 7.34e-10
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| beta-trefoil_MIR_ITPR | cd23277 | MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor ... |
179-328 | 4.32e-09 | |||||
MIR domain, beta-trefoil fold, found in the family of inositol 1,4,5-trisphosphate receptor (ITPR); Inositol 1,4,5 trisphosphate receptors (ITPRs) are a family of endoplasmic reticulum Ca2+ channels essential for the control of intracellular Ca2+ levels in virtually every mammalian cell type. Calcium-mediated signaling through ITPRs is essential for the regulation of numerous physiological processes, including fertilization, muscle contraction, apoptosis, secretion, and synaptic plasticity. The ITPR family includes three isoforms (ITPR1, ITPR2 and ITPR3), which can control different cellular processes due to their unique biophysical properties, subcellular localization, and tissue distribution. ITPRs contain an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467748 [Multi-domain] Cd Length: 204 Bit Score: 59.68 E-value: 4.32e-09
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| SPRY_Ash2 | cd12872 | SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or ... |
613-753 | 5.29e-09 | |||||
SPRY domain in Ash2; This SPRY domain is found at the C-terminus of Ash2 (absent, small, or homeotic discs 2) -like proteins, core components of all mixed-lineage leukemia (MLL) family histone methyltransferases. Ash2 is a member of the trithorax group of transcriptional regulators of the Hox genes. Recent studies show that the SPRY domain of Ash2 mediates the interaction with RbBP5 and has an important role in regulating the methyltransferase activity of MLL complexes. In yeast, Ash2 is involved in histone methylation and is required for the earliest stages of embryogenesis. Pssm-ID: 293932 Cd Length: 150 Bit Score: 57.91 E-value: 5.29e-09
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| beta-trefoil_MIR_ITPR2 | cd23288 | MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) ... |
166-260 | 1.29e-08 | |||||
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 2 (ITPR2) and similar proteins; ITPR2, also called IP3 receptor isoform 2 (IP3R 2), or InsP3R2, or type 2 inositol 1,4,5-trisphosphate receptor, or type 2 InsP3 receptor, is a key regulator for the activity of calcium ion transmembrane transportation, which plays a critical role in cell cycle and proliferation. It is a receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of cAMP-dependent protein kinase (PKA). ITPR2 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467759 [Multi-domain] Cd Length: 222 Bit Score: 58.51 E-value: 1.29e-08
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| SPRY2_RyR | cd12878 | SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of ... |
623-756 | 4.36e-08 | |||||
SPRY domain 2 (SPRY2) of ryanodine receptor (RyR); This SPRY domain (SPRY2) is the second of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, The SPRY2 domain has been shown to bind to the dihydropryidine receptor (DHPR) II-III loop and the ASI region of RyR1 Pssm-ID: 240458 Cd Length: 133 Bit Score: 55.00 E-value: 4.36e-08
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| beta-trefoil_MIR_ITPR1 | cd23287 | MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ... |
175-328 | 1.20e-07 | |||||
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) and similar proteins; ITPR1, also called IP3 receptor isoform 1 (IP3R 1), or InsP3R1, or type 1 inositol 1,4,5-trisphosphate receptor, or type 1 InsP3 receptor, is an intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. It is involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1. It plays a role in endoplasmic reticulum (ER) stress-induced apoptosis. ITPR1 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467758 [Multi-domain] Cd Length: 222 Bit Score: 55.85 E-value: 1.20e-07
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| MIR | smart00472 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
239-332 | 8.45e-07 | |||||
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 48.88 E-value: 8.45e-07
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| SPRY_hnRNP | cd12884 | SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, ... |
1043-1132 | 2.14e-06 | |||||
SPRY domain in heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of heterogeneous nuclear ribonucleoprotein U-like (hnRNP) protein 1 (also known as HNRPUL1 ) which is a major constituent of nuclear matrix or scaffold and binds directly to DNA sequences through the N-terminal acidic region named serum amyloid P (SAP). Its function is specifically modulated by E1B-55kDa in adenovirus-infected cells. HNRPUL1 also participates in ATR protein kinase signaling pathways during adenovirus infection. Two transcript variants encoding different isoforms have been found for this gene. When associated with bromodomain-containing protein 7 (BRD7), it activates transcription of glucocorticoid-responsive promoter in the absence of ligand-stimulation. Pssm-ID: 293942 Cd Length: 177 Bit Score: 51.05 E-value: 2.14e-06
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| SPRY1_RyR | cd12877 | SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three ... |
1050-1157 | 2.66e-06 | |||||
SPRY domain 1 (SPRY1) of ryanodine receptor (RyR); This SPRY domain is the first of three structural repeats in all three isoforms of the ryanodine receptor (RyR), which are the major Ca2+ release channels in the membranes of sarcoplasmic reticulum (SR). There are three RyR genes in mammals; the skeletal RyR1, the cardiac RyR2 and the brain RyR3. The three SPRY domains are located in the N-terminal part of the cytoplasmic region of the RyRs, but no specific function has been found for this first SPRY domain of the RyRs. Pssm-ID: 240457 Cd Length: 151 Bit Score: 50.39 E-value: 2.66e-06
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| beta-trefoil_MIR_ITPR3 | cd23289 | MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) ... |
182-305 | 4.22e-06 | |||||
MIR domain, beta-trefoil fold, found in inositol 1,4,5-trisphosphate receptor type 3 (ITPR3) and similar proteins; ITPR3, also called IP3 receptor isoform 3 (IP3R 3), or InsP3R3, or type 3 inositol 1,4,5-trisphosphate receptor, or type 3 InsP3 receptor, acts as anti-oncogenic channel by propelling pro-apoptotic Ca2+ signals to mitochondria. It is the principal intracellular Ca2+ release channel in cholangiocytes and plays a particularly important role in cancer. ITPR3 contains an N-terminal MIR (protein mannosyltransferase, IP3R and RyR) domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467760 [Multi-domain] Cd Length: 215 Bit Score: 51.20 E-value: 4.22e-06
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| MIR | smart00472 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
64-119 | 1.24e-05 | |||||
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 45.41 E-value: 1.24e-05
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| SPRY_RING | cd12883 | SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY ... |
624-764 | 2.69e-05 | |||||
SPRY domain at N-terminus of Really Interesting New Gene (RING) finger domain; This SPRY domain is found at the N-terminus of RING finger domains which are present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. RING-finger domain is a type of Zn-finger that binds two Zn atoms and is identified in proteins with a wide range of functions such as viral replication, signal transduction, and development. Pssm-ID: 293941 Cd Length: 121 Bit Score: 46.57 E-value: 2.69e-05
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| SPRY_RanBP9_10 | cd12909 | SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding ... |
1045-1132 | 7.38e-05 | |||||
SPRY domain in Ran binding proteins 9 and 10; This family includes SPRY domain in Ran binding protein (RBP or RanBPM) 9 and 10, and similar proteins. RanBP9 (also known as RanBPM), a binding partner of Ran, is a small Ras-like GTPase that exerts multiple functions via interactions with various proteins. RanBP9 and RanBP10 also act as androgen receptor (AR) coactivators. Both consist of the N-terminal proline- and glutamine-rich regions, the SPRY domain, and LisH-CTLH and CRA motifs. SPRY domain of RanBPM forms a complex with CD39, a prototypic member of the NTPDase family, thus down-regulating activity substantially. RanBP10 enhances the transcriptional activity of AR in a ligand-dependent manner and exhibits a protein expression pattern different from RanBPM in various cell lines. RanBP10 is highly expressed in AR-positive prostate cancer LNCaP cells, while RanBPM is abundant in WI-38 and MCF-7 cells. Pssm-ID: 293966 Cd Length: 144 Bit Score: 45.98 E-value: 7.38e-05
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| SPRY_like | cd12886 | SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in ... |
1049-1163 | 2.29e-04 | |||||
SPRY domain-like in bacteria; This family contains SPRY-like domains that are found only in bacterial and are mostly uncharacterized. SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 eukaryotic protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). Pssm-ID: 293944 Cd Length: 129 Bit Score: 44.03 E-value: 2.29e-04
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| EF-hand_7 | pfam13499 | EF-hand domain pair; |
3888-3943 | 4.80e-04 | |||||
EF-hand domain pair; Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 41.47 E-value: 4.80e-04
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| SPRY_DDX1 | cd12873 | SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD ... |
1375-1414 | 7.02e-04 | |||||
SPRY domain associated with DEAD box gene DDX1; This SPRY domain is associated with the DEAD box gene, DDX1, an RNA-dependent ATPase involved in HIV-1 Rev function and virus replication. It is suggested that DDX1 acts as a cellular cofactor by promoting oligomerization of Rev on the Rev response element (RRE). DDX1 RNA is overexpressed in breast cancer, data showing a strong and independent association between poor prognosis and deregulation of the DEAD box protein DDX1, thus potentially serving as an effective prognostic biomarker for early recurrence in primary breast cancer. DDX1 also interacts with RelA and enhances nuclear factor kappaB-mediated transcription. DEAD-box proteins are associated with all levels of RNA metabolism and function, and have been implicated in translation initiation, transcription, RNA splicing, ribosome assembly, RNA transport, and RNA decay. Pssm-ID: 293933 Cd Length: 155 Bit Score: 43.33 E-value: 7.02e-04
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| MIR | smart00472 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
179-232 | 5.73e-03 | |||||
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 38.09 E-value: 5.73e-03
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| MIR | smart00472 | Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; |
126-170 | 7.85e-03 | |||||
Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases; Pssm-ID: 197746 [Multi-domain] Cd Length: 57 Bit Score: 37.71 E-value: 7.85e-03
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