C2 domain-containing protein 2 isoform X5 [Mus musculus]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
SMP_C2CD2 | cd21682 | synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ... |
53-230 | 5.55e-92 | ||||
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 domain-containing protein 2 (C2CD2); C2CD2, also called transmembrane protein 24-like (TMEM24L), may be a lipid-binding protein that shows high sequence similarity with C2 domain-containing protein 2-like (C2CD2L; also transmembrane protein 24 or TMEM24). C2CD2L is a lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane. It is a Ca2+-regulated component of endoplasmic reticulum (ER)-plasma membrane contacts in mammalian neurons. This model corresponds to the SMP domain of C2CD2, which may be implicated in lipid transport. : Pssm-ID: 439238 Cd Length: 175 Bit Score: 277.21 E-value: 5.55e-92
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C2 super family | cl14603 | C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
261-386 | 1.38e-39 | ||||
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. The actual alignment was detected with superfamily member cd08678: Pssm-ID: 472691 [Multi-domain] Cd Length: 126 Bit Score: 139.42 E-value: 1.38e-39
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Name | Accession | Description | Interval | E-value | ||||
SMP_C2CD2 | cd21682 | synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ... |
53-230 | 5.55e-92 | ||||
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 domain-containing protein 2 (C2CD2); C2CD2, also called transmembrane protein 24-like (TMEM24L), may be a lipid-binding protein that shows high sequence similarity with C2 domain-containing protein 2-like (C2CD2L; also transmembrane protein 24 or TMEM24). C2CD2L is a lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane. It is a Ca2+-regulated component of endoplasmic reticulum (ER)-plasma membrane contacts in mammalian neurons. This model corresponds to the SMP domain of C2CD2, which may be implicated in lipid transport. Pssm-ID: 439238 Cd Length: 175 Bit Score: 277.21 E-value: 5.55e-92
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SMP_C2CD2L | pfam18696 | Synaptotagmin-like, mitochondrial and lipid-binding domain; This is a lipid transport domain ... |
71-223 | 1.39e-72 | ||||
Synaptotagmin-like, mitochondrial and lipid-binding domain; This is a lipid transport domain found in phospholipid transfer proteins such as C2CD2L-like (also known as TMEM24). The TMEM24-SMP domain is shown to bind glycerolipids with a preference for phosphatidylinositol (PI).The bound PI is then transferred to the plasma membrane (PM) where it is converted to phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to replenish pools of this lipid hydrolyzed during glucose-stimulated signaling. PI(4,5)P2 is required for Ca2+-dependent exocytosis hence, the SMP domain of TMEM24 is essential for sustaining the intracellular Ca2+ oscillations that trigger bursts of insulin granule release and hence insulin secretion. The SMP domain belongs to a superfamily of lipid/hydrophobic ligand-binding domains called TULIP for (tubular lipid-binding proteins) it adopts TULIP fold with two alpha helices and a highly curved antiparallel beta sheet forming a cornucopia-like structure. Pssm-ID: 465835 Cd Length: 152 Bit Score: 226.77 E-value: 1.39e-72
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C2_C21orf25-like | cd08678 | C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ... |
261-386 | 1.38e-39 | ||||
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Pssm-ID: 176060 [Multi-domain] Cd Length: 126 Bit Score: 139.42 E-value: 1.38e-39
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C2 | pfam00168 | C2 domain; |
283-359 | 2.27e-05 | ||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 43.46 E-value: 2.27e-05
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C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
260-342 | 4.96e-03 | ||||
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles. Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 36.70 E-value: 4.96e-03
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Name | Accession | Description | Interval | E-value | ||||
SMP_C2CD2 | cd21682 | synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ... |
53-230 | 5.55e-92 | ||||
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 domain-containing protein 2 (C2CD2); C2CD2, also called transmembrane protein 24-like (TMEM24L), may be a lipid-binding protein that shows high sequence similarity with C2 domain-containing protein 2-like (C2CD2L; also transmembrane protein 24 or TMEM24). C2CD2L is a lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane. It is a Ca2+-regulated component of endoplasmic reticulum (ER)-plasma membrane contacts in mammalian neurons. This model corresponds to the SMP domain of C2CD2, which may be implicated in lipid transport. Pssm-ID: 439238 Cd Length: 175 Bit Score: 277.21 E-value: 5.55e-92
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SMP_C2CD2L | pfam18696 | Synaptotagmin-like, mitochondrial and lipid-binding domain; This is a lipid transport domain ... |
71-223 | 1.39e-72 | ||||
Synaptotagmin-like, mitochondrial and lipid-binding domain; This is a lipid transport domain found in phospholipid transfer proteins such as C2CD2L-like (also known as TMEM24). The TMEM24-SMP domain is shown to bind glycerolipids with a preference for phosphatidylinositol (PI).The bound PI is then transferred to the plasma membrane (PM) where it is converted to phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to replenish pools of this lipid hydrolyzed during glucose-stimulated signaling. PI(4,5)P2 is required for Ca2+-dependent exocytosis hence, the SMP domain of TMEM24 is essential for sustaining the intracellular Ca2+ oscillations that trigger bursts of insulin granule release and hence insulin secretion. The SMP domain belongs to a superfamily of lipid/hydrophobic ligand-binding domains called TULIP for (tubular lipid-binding proteins) it adopts TULIP fold with two alpha helices and a highly curved antiparallel beta sheet forming a cornucopia-like structure. Pssm-ID: 465835 Cd Length: 152 Bit Score: 226.77 E-value: 1.39e-72
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SMP_C2CD2-like | cd21664 | synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ... |
54-230 | 1.24e-45 | ||||
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 domain-containing protein 2-like (C2CD2L) and similar proteins; This family includes C2 domain-containing protein 2 (C2CD2) and C2CD2-like (C2CD2L). C2CD2 (also called transmembrane protein 24-like or TMEM24L), may be a lipid-binding protein that shows high sequence similarity with C2 domain-containing protein 2-like (C2CD2L; also called transmembrane protein 24 or TMEM24). C2CD2L is a lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum (ER) to the cell membrane. It is a Ca2+-regulated component of ER-plasma membrane contacts in mammalian neurons. This model corresponds to the SMP domain of C2CD2 and C2CD2L which binds glycerolipids with a preference for phosphatidylinositol (PI). The bound PI is then transferred to the plasma membrane (PM) where it is converted to phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to replenish pools of this lipid hydrolyzed during glucose-stimulated signaling. PI(4,5)P2 is required for Ca2+-dependent exocytosis; hence, the SMP domain of TMEM24 is essential for sustaining the intracellular Ca2+ oscillations that trigger bursts of insulin granule release and subsequent insulin secretion. Pssm-ID: 439224 Cd Length: 175 Bit Score: 157.13 E-value: 1.24e-45
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C2_C21orf25-like | cd08678 | C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ... |
261-386 | 1.38e-39 | ||||
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Pssm-ID: 176060 [Multi-domain] Cd Length: 126 Bit Score: 139.42 E-value: 1.38e-39
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SMP_C2CD2L | cd21683 | synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ... |
57-210 | 1.02e-15 | ||||
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 domain-containing protein 2-like (C2CD2L); C2CD2L, also called phospholipid transfer protein C2CD2L, or C2CD2-like, or transmembrane protein 24 (TMEM24), is a lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane. It is a Ca2+-regulated component of endoplasmic reticulum (ER)-plasma membrane contacts in mammalian neurons. This model corresponds to the SMP domain of C2CD2L, which may be implicated in lipid transport. Pssm-ID: 439239 Cd Length: 177 Bit Score: 75.13 E-value: 1.02e-15
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C2 | cd00030 | C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
261-359 | 3.09e-06 | ||||
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 45.91 E-value: 3.09e-06
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C2 | pfam00168 | C2 domain; |
283-359 | 2.27e-05 | ||||
C2 domain; Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 43.46 E-value: 2.27e-05
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C2 | smart00239 | Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
260-342 | 4.96e-03 | ||||
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles. Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 36.70 E-value: 4.96e-03
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Blast search parameters | ||||
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