copine-4 isoform X5 [Homo sapiens]
Protein Classification
C2 and vWA_copine_like domain-containing protein( domain architecture ID 10971227)
C2 and vWA_copine_like domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| Copine | pfam07002 | Copine; This family represents a conserved region approximately 220 residues long within ... |
186-399 | 2.29e-128 | ||||
Copine; This family represents a conserved region approximately 220 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking, and may also be involved in cell division and growth. : Pssm-ID: 462064 Cd Length: 214 Bit Score: 368.97 E-value: 2.29e-128
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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 ... |
90-127 | 1.68e-11 | ||||
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 cd04047: Pssm-ID: 472691 [Multi-domain] Cd Length: 110 Bit Score: 60.66 E-value: 1.68e-11
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| Name | Accession | Description | Interval | E-value | |||||
| Copine | pfam07002 | Copine; This family represents a conserved region approximately 220 residues long within ... |
186-399 | 2.29e-128 | |||||
Copine; This family represents a conserved region approximately 220 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking, and may also be involved in cell division and growth. Pssm-ID: 462064 Cd Length: 214 Bit Score: 368.97 E-value: 2.29e-128
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| vWA_copine_like | cd01459 | VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ... |
140-390 | 4.91e-112 | |||||
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However, the MIDAS motif is not totally conserved, in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding. Pssm-ID: 238736 Cd Length: 254 Bit Score: 328.95 E-value: 4.91e-112
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| C2B_Copine | cd04047 | C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ... |
90-127 | 1.68e-11 | |||||
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. 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. This cd contains the second C2 repeat, C2B, and has a type-I topology. Pssm-ID: 176012 [Multi-domain] Cd Length: 110 Bit Score: 60.66 E-value: 1.68e-11
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
264-348 | 1.81e-08 | |||||
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods. Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 53.61 E-value: 1.81e-08
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| Name | Accession | Description | Interval | E-value | |||||
| Copine | pfam07002 | Copine; This family represents a conserved region approximately 220 residues long within ... |
186-399 | 2.29e-128 | |||||
Copine; This family represents a conserved region approximately 220 residues long within eukaryotic copines. Copines are Ca(2+)-dependent phospholipid-binding proteins that are thought to be involved in membrane-trafficking, and may also be involved in cell division and growth. Pssm-ID: 462064 Cd Length: 214 Bit Score: 368.97 E-value: 2.29e-128
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| vWA_copine_like | cd01459 | VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. ... |
140-390 | 4.91e-112 | |||||
VWA Copine: Copines are phospholipid-binding proteins originally identified in paramecium. They are found in human and orthologues have been found in C. elegans and Arabidopsis Thaliana. None have been found in D. Melanogaster or S. Cereviciae. Phylogenetic distribution suggests that copines have been lost in some eukaryotes. No functional properties have been assigned to the VWA domains present in copines. The members of this subgroup contain a functional MIDAS motif based on their preferential binding to magnesium and manganese. However, the MIDAS motif is not totally conserved, in most cases the MIDAS consists of the sequence DxTxS instead of the motif DxSxS that is found in most cases. The C2 domains present in copines mediate phospholipid binding. Pssm-ID: 238736 Cd Length: 254 Bit Score: 328.95 E-value: 4.91e-112
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| C2B_Copine | cd04047 | C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a ... |
90-127 | 1.68e-11 | |||||
C2 domain second repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. 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. This cd contains the second C2 repeat, C2B, and has a type-I topology. Pssm-ID: 176012 [Multi-domain] Cd Length: 110 Bit Score: 60.66 E-value: 1.68e-11
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| VWA | smart00327 | von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
264-348 | 1.81e-08 | |||||
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods. Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 53.61 E-value: 1.81e-08
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