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Conserved domains on  [gi|1995977757|ref|XP_039699059|]
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follistatin-related protein 1 isoform X2 [Pteropus giganteus]

Protein Classification

follistatin-related protein 1( domain architecture ID 12199490)

follistatin-related protein 1 is an extracellular calcium-binding protein belonging to the BM-40/SPARC/osteonectin family and containing Kazal-type serine protease inhibitor/follistatin-like and EF-hand domains, that is involved in various physiological processes, such as angiogenesis, regulation of the immune response, cell proliferation and differentiation

CATH:  3.30.60.30
Gene Symbol:  FSTL1
Gene Ontology:  GO:0005576|GO:0005509
PubMed:  10641790|22249026|19995574|12051857|28707401|2479149
SCOP:  4003413

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_SPARC_FSTL1 cd16233
EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 ...
 146-259 7.87e-76

EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 (FRP-1); FRP-1, also termed follistatin-like protein 1 (fstl-1), TGF-beta-stimulated clone 36 (TSC-36/Flik), or TGF-beta inducible protein, is a secreted glycoprotein that is overexpressed in certain inflammatory diseases and has been implicated in many autoimmune diseases. FRP-1 functions as an important proinflammatory factor in the pathogenesis of osteoarthritis (OA) by activating the canonical NF-kappaB-mediated inflammatory cytokines, including tumor necrosis factor alpha (TNF-alpha), interleukin-1beta (IL-1beta) and interleukin-6 (IL-6), and enhancing fibroblast like synoviocytes proliferation. It also acts as a critical mediator of collagen-induced arthritis (CIA), juvenile rheumatoid arthritis (JRA), as well as Lyme arthritis observed after Borrelia burgdorferi infection. Meanwhile, it enhances nod-like receptor family, pyrin domain containing 3 (NLRP3) inflammasome-mediated IL-1beta secretion from monocytes and macrophages. Moreover, FRP-1 shows critical functions in the nervous system. It differentially regulates transforming growth factor beta (TGF-beta) and bone morphogenetic protein (BMP) signaling, leading to epithelial injury and fibroblast activation. Furthermore, FRP-1 functions as a cardiokine with cardioprotective properties. It may play a potential role in ischemic stroke through decreasing neuronal apoptosis and improving neurological deficits via disco-interacting protein 2 homolog A (DIP2A)/Akt pathway after middle cerebral artery occlusion (MCAO). Plasma FRP-1 is elevated in Kawasaki disease (KD) and thus may play a possible role in the formation of coronary artery aneurysm (CAA). FRP-1 contains a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, and a von Willebrand factor type C (VWC) domain. The EC domain does not undergo characteristic structural changes upon calcium addition or depletion and therefore is not a functional calcium binding domain.


:

Pssm-ID: 320012  Cd Length: 114  Bit Score: 228.50  E-value: 7.87e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995977757 146 CYQSNRDELRRRIIQWLEAEIIPDGWFSKGSNYSEILDKYFKNFDNGDSRLDSSEFLKFVEQNETAINITTYADQENNKL 225
Cdd:cd16233     1 CYQSDRDELRRRVIDWLQTEVIPDGWFTKGSSYSDILDKYFKKYDNGDSQLDSNELLKFVEQNETATNLTLYQDEETNKL 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1995977757 226 LRGLCVDALIELSDENADWKLSFQEFLQCLNPSF 259
Cdd:cd16233    81 LRGLCVDALIELSDENADWKLNFEEFLKCLNPSF 114
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 87-131 2.97e-13

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


:

Pssm-ID: 197624  Cd Length: 46  Bit Score: 63.47  E-value: 2.97e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1995977757   87 CIEQCKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 131
Cdd:smart00280   2 CPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
FOLN smart00274
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ...
 64-86 1.34e-03

Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence


:

Pssm-ID: 128570  Cd Length: 24  Bit Score: 35.72  E-value: 1.34e-03
                           10        20
                   ....*....|....*....|...
gi 1995977757   64 CANVFCGAGRECAVTEKGEPTCL 86
Cdd:smart00274   2 CRNVQCPFGKVCVVDKNGNARCV 24
VWC super family cl17735
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
 266-304 2.40e-03

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


The actual alignment was detected with superfamily member smart00215:

Pssm-ID: 450195  Cd Length: 67  Bit Score: 36.00  E-value: 2.40e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1995977757  266 CALEDETYADGAETEVDCNRCVCACGNWVCTAMTCDGKN 304
Cdd:smart00215   1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKP 39
 
Name Accession Description Interval E-value
EFh_SPARC_FSTL1 cd16233
EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 ...
 146-259 7.87e-76

EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 (FRP-1); FRP-1, also termed follistatin-like protein 1 (fstl-1), TGF-beta-stimulated clone 36 (TSC-36/Flik), or TGF-beta inducible protein, is a secreted glycoprotein that is overexpressed in certain inflammatory diseases and has been implicated in many autoimmune diseases. FRP-1 functions as an important proinflammatory factor in the pathogenesis of osteoarthritis (OA) by activating the canonical NF-kappaB-mediated inflammatory cytokines, including tumor necrosis factor alpha (TNF-alpha), interleukin-1beta (IL-1beta) and interleukin-6 (IL-6), and enhancing fibroblast like synoviocytes proliferation. It also acts as a critical mediator of collagen-induced arthritis (CIA), juvenile rheumatoid arthritis (JRA), as well as Lyme arthritis observed after Borrelia burgdorferi infection. Meanwhile, it enhances nod-like receptor family, pyrin domain containing 3 (NLRP3) inflammasome-mediated IL-1beta secretion from monocytes and macrophages. Moreover, FRP-1 shows critical functions in the nervous system. It differentially regulates transforming growth factor beta (TGF-beta) and bone morphogenetic protein (BMP) signaling, leading to epithelial injury and fibroblast activation. Furthermore, FRP-1 functions as a cardiokine with cardioprotective properties. It may play a potential role in ischemic stroke through decreasing neuronal apoptosis and improving neurological deficits via disco-interacting protein 2 homolog A (DIP2A)/Akt pathway after middle cerebral artery occlusion (MCAO). Plasma FRP-1 is elevated in Kawasaki disease (KD) and thus may play a possible role in the formation of coronary artery aneurysm (CAA). FRP-1 contains a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, and a von Willebrand factor type C (VWC) domain. The EC domain does not undergo characteristic structural changes upon calcium addition or depletion and therefore is not a functional calcium binding domain.


Pssm-ID: 320012  Cd Length: 114  Bit Score: 228.50  E-value: 7.87e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995977757 146 CYQSNRDELRRRIIQWLEAEIIPDGWFSKGSNYSEILDKYFKNFDNGDSRLDSSEFLKFVEQNETAINITTYADQENNKL 225
Cdd:cd16233     1 CYQSDRDELRRRVIDWLQTEVIPDGWFTKGSSYSDILDKYFKKYDNGDSQLDSNELLKFVEQNETATNLTLYQDEETNKL 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1995977757 226 LRGLCVDALIELSDENADWKLSFQEFLQCLNPSF 259
Cdd:cd16233    81 LRGLCVDALIELSDENADWKLNFEEFLKCLNPSF 114
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 87-131 2.97e-13

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 63.47  E-value: 2.97e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1995977757   87 CIEQCKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 131
Cdd:smart00280   2 CPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 64-133 4.47e-13

Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238649 [Multi-domain]  Cd Length: 86  Bit Score: 64.04  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995977757  64 CANVFCGAGRECAVTEKGEPTCLCIEQCKPH---KRPVCGSNGKTYLNHCELHRDACL-----------TGSKIQVDYDG 129
Cdd:cd01328     2 CENHHCGAGKVCEVDDENTPKCVCIDPCPEEvddRRKVCTNDNETFDSDCELYRTRCLckggkkgcrgpKYQHLHLDYYG 81


                  ....
gi 1995977757 130 HCKE 133
Cdd:cd01328    82 ECKE 85
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 87-131 5.75e-09

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 51.34  E-value: 5.75e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1995977757  87 CIEQC-KPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQ---VDYDGHC 131
Cdd:pfam07648   2 CNCQCpKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
EF-hand_7 pfam13499
EF-hand domain pair;
186-253 2.16e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.86  E-value: 2.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1995977757 186 FKNFD-NGDSRLDSSEFLKFVEQNETAINITtyaDQEnnkllrglcVDALIELSDENADWKLSFQEFLQ 253
Cdd:pfam13499   8 FKLLDsDGDGYLDVEELKKLLRKLEEGEPLS---DEE---------VEELFKEFDLDKDGRISFEEFLE 64
FOLN smart00274
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ...
 64-86 1.34e-03

Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence


Pssm-ID: 128570  Cd Length: 24  Bit Score: 35.72  E-value: 1.34e-03
                           10        20
                   ....*....|....*....|...
gi 1995977757   64 CANVFCGAGRECAVTEKGEPTCL 86
Cdd:smart00274   2 CRNVQCPFGKVCVVDKNGNARCV 24
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
266-304 2.40e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 36.00  E-value: 2.40e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1995977757  266 CALEDETYADGAETEVDCNRCVCACGNWVCTAMTCDGKN 304
Cdd:smart00215   1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKP 39
 
Name Accession Description Interval E-value
EFh_SPARC_FSTL1 cd16233
EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 ...
 146-259 7.87e-76

EF-hand, extracellular calcium-binding (EC) motif, found in follistatin-related protein 1 (FRP-1); FRP-1, also termed follistatin-like protein 1 (fstl-1), TGF-beta-stimulated clone 36 (TSC-36/Flik), or TGF-beta inducible protein, is a secreted glycoprotein that is overexpressed in certain inflammatory diseases and has been implicated in many autoimmune diseases. FRP-1 functions as an important proinflammatory factor in the pathogenesis of osteoarthritis (OA) by activating the canonical NF-kappaB-mediated inflammatory cytokines, including tumor necrosis factor alpha (TNF-alpha), interleukin-1beta (IL-1beta) and interleukin-6 (IL-6), and enhancing fibroblast like synoviocytes proliferation. It also acts as a critical mediator of collagen-induced arthritis (CIA), juvenile rheumatoid arthritis (JRA), as well as Lyme arthritis observed after Borrelia burgdorferi infection. Meanwhile, it enhances nod-like receptor family, pyrin domain containing 3 (NLRP3) inflammasome-mediated IL-1beta secretion from monocytes and macrophages. Moreover, FRP-1 shows critical functions in the nervous system. It differentially regulates transforming growth factor beta (TGF-beta) and bone morphogenetic protein (BMP) signaling, leading to epithelial injury and fibroblast activation. Furthermore, FRP-1 functions as a cardiokine with cardioprotective properties. It may play a potential role in ischemic stroke through decreasing neuronal apoptosis and improving neurological deficits via disco-interacting protein 2 homolog A (DIP2A)/Akt pathway after middle cerebral artery occlusion (MCAO). Plasma FRP-1 is elevated in Kawasaki disease (KD) and thus may play a possible role in the formation of coronary artery aneurysm (CAA). FRP-1 contains a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, and a von Willebrand factor type C (VWC) domain. The EC domain does not undergo characteristic structural changes upon calcium addition or depletion and therefore is not a functional calcium binding domain.


Pssm-ID: 320012  Cd Length: 114  Bit Score: 228.50  E-value: 7.87e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995977757 146 CYQSNRDELRRRIIQWLEAEIIPDGWFSKGSNYSEILDKYFKNFDNGDSRLDSSEFLKFVEQNETAINITTYADQENNKL 225
Cdd:cd16233     1 CYQSDRDELRRRVIDWLQTEVIPDGWFTKGSSYSDILDKYFKKYDNGDSQLDSNELLKFVEQNETATNLTLYQDEETNKL 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1995977757 226 LRGLCVDALIELSDENADWKLSFQEFLQCLNPSF 259
Cdd:cd16233    81 LRGLCVDALIELSDENADWKLNFEEFLKCLNPSF 114
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 146-257 1.79e-27

EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC)-like proteins; The SPARC protein family represents a diverse group of proteins that share a follistatin-like (FS) domain and an extracellular calcium-binding (EC) domain with two EF-hand motifs. It includes SPARC (for secreted protein acidic and rich in cysteine, also termed osteonectin/ON, or basement-membrane protein 40/BM-40), SPARC-like protein 1 (for secreted protein, acidic and rich in cysteines-like 1/ SPARCL1, also termed high endothelial venule protein/Hevi, or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2), testicans 1, 2, and 3 (also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycans, or SPOCK), secreted modular calcium-binding protein SMOC-1 (also termed SPARC-related modular calcium-binding protein 1) and SMOC-2 (also termed SPARC-related modular calcium-binding protein 2, or smooth muscle-associated protein 2/SMAP-2), follistatin-related protein 1 (FRP-1, also termed follistatin-like protein 1/fstl-1, TSC-36/Flik, TGF-beta inducible protein). The SPARC proteins have been implicated in modulating cell interaction with the extracellular milieu, including regulation of extracellular matrix assembly and deposition, counter-adhesion, effects on extracellular protease activity, and modulation of growth factor/cytokine signaling pathways, as well as in development and disease.


Pssm-ID: 320009  Cd Length: 107  Bit Score: 103.61  E-value: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995977757 146 CYQSNRDELRRRIIQWLEAEIIPDGWFSK----------GSNYSEILDKYFKNFD-NGDSRLDSSEFLKFVEQNEtaini 214
Cdd:cd00252     1 CPGSELMQFPDRLLDWLLLLKEQDENRSYdnnkrghdlsGTMRKEIAQWEFDNLDnNKDGKLDKRELAPFRAPLM----- 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1995977757 215 ttyadqennklLRGLCVDALIELSDENADWKLSFQEFLQCLNP 257
Cdd:cd00252    76 -----------PLEHCARGFFESCDLNKDKKISLQEWLGCFGV 107
KAZAL smart00280
Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and ...
 87-131 2.97e-13

Kazal type serine protease inhibitors; Kazal type serine protease inhibitors and follistatin-like domains.


Pssm-ID: 197624  Cd Length: 46  Bit Score: 63.47  E-value: 2.97e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1995977757   87 CIEQCKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 131
Cdd:smart00280   2 CPEACPREYDPVCGSDGVTYSNECHLCKAACESGKSIEVKHDGPC 46
FSL_SPARC cd01328
Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40 ...
 64-133 4.47e-13

Follistatin-like SPARC (secreted protein, acidic, and rich in cysteines) domain; SPARC/BM-40/osteonectin is a multifunctional glycoprotein which modulates cellular interaction with the extracellular matrix by its binding to structural matrix proteins such as collagen and vitronectin. The protein it composed of an N-terminal acidic region, a follistatin (FS) domain and an EF-hand calcium binding domain. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a small hydrophobic core of alpha/beta structure (Kazal domain) and has five disulfide bonds and a conserved N-glycosylation site. The FSL_SPARC domain is a member of the superfamily of kazal-like proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238649 [Multi-domain]  Cd Length: 86  Bit Score: 64.04  E-value: 4.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995977757  64 CANVFCGAGRECAVTEKGEPTCLCIEQCKPH---KRPVCGSNGKTYLNHCELHRDACL-----------TGSKIQVDYDG 129
Cdd:cd01328     2 CENHHCGAGKVCEVDDENTPKCVCIDPCPEEvddRRKVCTNDNETFDSDCELYRTRCLckggkkgcrgpKYQHLHLDYYG 81


                  ....
gi 1995977757 130 HCKE 133
Cdd:cd01328    82 ECKE 85
KAZAL_FS cd00104
Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit ...
 91-131 5.46e-13

Kazal type serine protease inhibitors and follistatin-like domains. Kazal inhibitors inhibit serine proteases, such as, trypsin, chyomotrypsin, avian ovomucoids, and elastases. The inhibitory domain has one reactive site peptide bond, which serves the cognate enzyme as substrate. The reactive site peptide bond is a combining loop which has an identical conformation in all Kazal inhibitors and in all enzyme/inhibitor complexes. These Kazal domains (small hydrophobic core of alpha/beta structure with 3 to 4 disulfide bonds) often occur in tandem arrays. Similar domains are also present in follistatin (FS) and follistatin-like family members, which play an important role in tissue specific regulation. The FS domain consists of an N-terminal beta hairpin (FOLN/EGF-like domain) and a Kazal-like domain and has five disulfide bonds. Although the Kazal-like FS substructure is similar to Kazal proteinase inhibitors, no FS domain has yet been shown to be a proteinase inhibitor. Follistatin-like family members include SPARC, also known as, BM-40 or osteonectin, the Gallus gallus Flik protein, as well as, agrin which has a long array of FS domains. The kazal-type inhibitor domain has also been detected in an extracellular loop region of solute carrier 21 (SLC21) family members (organic anion transporters) , which may regulate the specificity of anion uptake. The distant homolog, Ascidian trypsin inhibitor, is included in this CD.


Pssm-ID: 238052 [Multi-domain]  Cd Length: 41  Bit Score: 62.29  E-value: 5.46e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1995977757  91 CKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 131
Cdd:cd00104     1 CPKEYDPVCGSDGKTYSNECHLGCAACRSGRSITVAHNGPC 41
Kazal_2 pfam07648
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 87-131 5.75e-09

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides.


Pssm-ID: 400135  Cd Length: 50  Bit Score: 51.34  E-value: 5.75e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1995977757  87 CIEQC-KPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQ---VDYDGHC 131
Cdd:pfam07648   2 CNCQCpKTEYEPVCGSDGVTYPSPCALCAAGCKLGKEVKeekVKYDGSC 50
EF-hand_7 pfam13499
EF-hand domain pair;
186-253 2.16e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.86  E-value: 2.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1995977757 186 FKNFD-NGDSRLDSSEFLKFVEQNETAINITtyaDQEnnkllrglcVDALIELSDENADWKLSFQEFLQ 253
Cdd:pfam13499   8 FKLLDsDGDGYLDVEELKKLLRKLEEGEPLS---DEE---------VEELFKEFDLDKDGRISFEEFLE 64
Kazal_1 pfam00050
Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. ...
 91-131 4.47e-04

Kazal-type serine protease inhibitor domain; Usually indicative of serine protease inhibitors. However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. Kazal domains often occur in tandem arrays. Small alpha+beta fold containing three disulphides. Alignment also includes a single domain from transporters in the OATP/PGT family.


Pssm-ID: 395004  Cd Length: 49  Bit Score: 37.65  E-value: 4.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1995977757  91 CKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 131
Cdd:pfam00050   9 CPRIYDPVCGTDGKTYSNECLFCAENGKRGTNLHKVHDGEC 49
KAZAL_PSTI cd01327
Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the ...
 91-131 6.00e-04

Kazal-type pancreatic secretory trypsin inhibitors (PSTI) and related proteins, including the second domain of the ovomucoid turkey inhibitor and the C-terminal domain of the esophagus cancer-related gene-2 protein (ECRG-2), are members of the superfamily of kazal-type proteinase inhibitors and follistatin-like proteins.


Pssm-ID: 238648  Cd Length: 45  Bit Score: 37.26  E-value: 6.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1995977757  91 CKPHKRPVCGSNGKTYLNHCELHRDACLTGSKIQVDYDGHC 131
Cdd:cd01327     5 CPKDYDPVCGTDGVTYSNECLLCAENLKRQTNIRIKHDGEC 45
FOLN smart00274
Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region ...
 64-86 1.34e-03

Follistatin-N-terminal domain-like; Follistatin-N-terminal domain-like, EGF-like. Region distinct from the kazal-like sequence


Pssm-ID: 128570  Cd Length: 24  Bit Score: 35.72  E-value: 1.34e-03
                           10        20
                   ....*....|....*....|...
gi 1995977757   64 CANVFCGAGRECAVTEKGEPTCL 86
Cdd:smart00274   2 CRNVQCPFGKVCVVDKNGNARCV 24
VWC_out smart00215
von Willebrand factor (vWF) type C domain;
266-304 2.40e-03

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214565  Cd Length: 67  Bit Score: 36.00  E-value: 2.40e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1995977757  266 CALEDETYADGAETEVDCNRCVCACGNWVCTAMTCDGKN 304
Cdd:smart00215   1 CWNNGSYYPPGAKWDDDCNRCTCLNGRVSCTKVWCGPKP 39
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 183-252 3.75e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 38.45  E-value: 3.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1995977757 183 DKYFKNFD-NGDSRLDSSEFLKFVEQNETAInittyADQEnnkllrglcVDALIELSDENADWKLSFQEFL 252
Cdd:cd16227   199 DRFDEDYDkDGDGKLDGEEILSWLVPDNEEI-----AEEE---------VDHLFASADDDHDDRLSFDEIL 255
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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