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Conserved domains on  [gi|1720422895|ref|XP_030098506|]
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C2 domain-containing protein 3 isoform X3 [Mus musculus]

Protein Classification

C2 domain-containing protein 3( domain architecture ID 10171496)

C2 domain-containing protein 3 (C2CD3) is a putative calcium-dependent lipid-binding protein, a component of the centrioles that acts as a positive regulator of centriole elongation

Gene Symbol:  C2CD3
Gene Ontology:  GO:0060271|GO:0061511
PubMed:  8976547|9632630

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2_C2cd3 cd08683
C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins; C2cd3 is a novel ...
 720-862 4.48e-80

C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins; C2cd3 is a novel C2 domain-containing protein specific to vertebrates. C2cd3 functions in regulator of cilia formation, Hedgehog signaling, and mouse embryonic development. Mutations in C2cd3 mice resulted in lethality in some cases and exencephaly, a twisted body axis, and pericardial edema in others. The presence of calcium-dependent lipid-binding domains in C2cd3 suggests a potential role in vesicular transport. C2cd3 is also an interesting candidate for ciliopathy because of its orthology to certain cilia-related genetic disease loci on chromosome. 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: 176065 [Multi-domain]  Cd Length: 143  Bit Score: 260.05  E-value: 4.48e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422895  720 ISVHIIRACGLQAAAKALAEQEPALQFSATVGVNASVTAHLSFLPKGEQRQTRPVACSFCPEFSHHIEFPCNLVTQHCSG 799
Cdd:cd08683      1 LSVQIHRASGLQAAARALAEQDPSLQYSATVGVNSYVTIHLSFLPEKELRRTRTVARSFCPEFNHHVEFPCNLVVQRNSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720422895  800 EACFLAELLEFAEIIFAIYHENTKSVSDITSIQSCKDYLLGIVKVPTKDLLVKRSGITGWYPV 862
Cdd:cd08683     81 EAISLAELLESAEIILEVWHRNPKSAGDTIKIETSGDILLGTVKIPLRDLLTKRSGITGWYPI 143
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 1197-1265 8.80e-05

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: 43.21  E-value: 8.80e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422895 1197 THVVENTDSPIWGFHqqarLSKELLLDPHQTLVFKVWHK--GDEERVVGFASVDLSPLLSGFQFICGWYNI 1265
Cdd:cd00030     36 TKVVKNTLNPVWNET----FEFPVLDPESDTLTVEVWDKdrFSKDDFLGEVEIPLSELLDSGKEGELWLPL 102
 
Name Accession Description Interval E-value
C2_C2cd3 cd08683
C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins; C2cd3 is a novel ...
 720-862 4.48e-80

C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins; C2cd3 is a novel C2 domain-containing protein specific to vertebrates. C2cd3 functions in regulator of cilia formation, Hedgehog signaling, and mouse embryonic development. Mutations in C2cd3 mice resulted in lethality in some cases and exencephaly, a twisted body axis, and pericardial edema in others. The presence of calcium-dependent lipid-binding domains in C2cd3 suggests a potential role in vesicular transport. C2cd3 is also an interesting candidate for ciliopathy because of its orthology to certain cilia-related genetic disease loci on chromosome. 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: 176065 [Multi-domain]  Cd Length: 143  Bit Score: 260.05  E-value: 4.48e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422895  720 ISVHIIRACGLQAAAKALAEQEPALQFSATVGVNASVTAHLSFLPKGEQRQTRPVACSFCPEFSHHIEFPCNLVTQHCSG 799
Cdd:cd08683      1 LSVQIHRASGLQAAARALAEQDPSLQYSATVGVNSYVTIHLSFLPEKELRRTRTVARSFCPEFNHHVEFPCNLVVQRNSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720422895  800 EACFLAELLEFAEIIFAIYHENTKSVSDITSIQSCKDYLLGIVKVPTKDLLVKRSGITGWYPV 862
Cdd:cd08683     81 EAISLAELLESAEIILEVWHRNPKSAGDTIKIETSGDILLGTVKIPLRDLLTKRSGITGWYPI 143
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 1197-1265 8.80e-05

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: 43.21  E-value: 8.80e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422895 1197 THVVENTDSPIWGFHqqarLSKELLLDPHQTLVFKVWHK--GDEERVVGFASVDLSPLLSGFQFICGWYNI 1265
Cdd:cd00030     36 TKVVKNTLNPVWNET----FEFPVLDPESDTLTVEVWDKdrFSKDDFLGEVEIPLSELLDSGKEGELWLPL 102
C2 pfam00168
C2 domain;
1197-1265 2.38e-04

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 42.31  E-value: 2.38e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422895 1197 THVVENTDSPIWgfHQQARLskELLLDPHQTLVFKVWHKG--DEERVVGFASVDLSPLLSGfQFICGWYNI 1265
Cdd:pfam00168   39 TKVVKNTLNPVW--NETFTF--SVPDPENAVLEIEVYDYDrfGRDDFIGEVRIPLSELDSG-EGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 1155-1256 1.36e-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: 39.78  E-value: 1.36e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422895  1155 VSILVERAMHLSLKGSPLTdrkvSVPSCCVSFATATELSpVYTHVVENTDSPIWGFHqqarLSKELLLDPHQTLVFKVWH 1234
Cdd:smart00239    2 LTVKIISARNLPPKDKGGK----SDPYVKVSLDGDPKEK-KKTKVVKNTLNPVWNET----FEFEVPPPELAELEIEVYD 72

                            90       100
                    ....*....|....*....|....
gi 1720422895  1235 K--GDEERVVGFASVDLSPLLSGF 1256
Cdd:smart00239   73 KdrFGRDDFIGQVTIPLSDLLLGG 96
 
Name Accession Description Interval E-value
C2_C2cd3 cd08683
C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins; C2cd3 is a novel ...
 720-862 4.48e-80

C2 domain found in C2 calcium-dependent domain containing 3 (C2cd3) proteins; C2cd3 is a novel C2 domain-containing protein specific to vertebrates. C2cd3 functions in regulator of cilia formation, Hedgehog signaling, and mouse embryonic development. Mutations in C2cd3 mice resulted in lethality in some cases and exencephaly, a twisted body axis, and pericardial edema in others. The presence of calcium-dependent lipid-binding domains in C2cd3 suggests a potential role in vesicular transport. C2cd3 is also an interesting candidate for ciliopathy because of its orthology to certain cilia-related genetic disease loci on chromosome. 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: 176065 [Multi-domain]  Cd Length: 143  Bit Score: 260.05  E-value: 4.48e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422895  720 ISVHIIRACGLQAAAKALAEQEPALQFSATVGVNASVTAHLSFLPKGEQRQTRPVACSFCPEFSHHIEFPCNLVTQHCSG 799
Cdd:cd08683      1 LSVQIHRASGLQAAARALAEQDPSLQYSATVGVNSYVTIHLSFLPEKELRRTRTVARSFCPEFNHHVEFPCNLVVQRNSG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720422895  800 EACFLAELLEFAEIIFAIYHENTKSVSDITSIQSCKDYLLGIVKVPTKDLLVKRSGITGWYPV 862
Cdd:cd08683     81 EAISLAELLESAEIILEVWHRNPKSAGDTIKIETSGDILLGTVKIPLRDLLTKRSGITGWYPI 143
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 1197-1265 8.80e-05

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: 43.21  E-value: 8.80e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422895 1197 THVVENTDSPIWGFHqqarLSKELLLDPHQTLVFKVWHK--GDEERVVGFASVDLSPLLSGFQFICGWYNI 1265
Cdd:cd00030     36 TKVVKNTLNPVWNET----FEFPVLDPESDTLTVEVWDKdrFSKDDFLGEVEIPLSELLDSGKEGELWLPL 102
C2 pfam00168
C2 domain;
1197-1265 2.38e-04

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 42.31  E-value: 2.38e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422895 1197 THVVENTDSPIWgfHQQARLskELLLDPHQTLVFKVWHKG--DEERVVGFASVDLSPLLSGfQFICGWYNI 1265
Cdd:pfam00168   39 TKVVKNTLNPVW--NETFTF--SVPDPENAVLEIEVYDYDrfGRDDFIGEVRIPLSELDSG-EGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 1155-1256 1.36e-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: 39.78  E-value: 1.36e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422895  1155 VSILVERAMHLSLKGSPLTdrkvSVPSCCVSFATATELSpVYTHVVENTDSPIWGFHqqarLSKELLLDPHQTLVFKVWH 1234
Cdd:smart00239    2 LTVKIISARNLPPKDKGGK----SDPYVKVSLDGDPKEK-KKTKVVKNTLNPVWNET----FEFEVPPPELAELEIEVYD 72

                            90       100
                    ....*....|....*....|....
gi 1720422895  1235 K--GDEERVVGFASVDLSPLLSGF 1256
Cdd:smart00239   73 KdrFGRDDFIGQVTIPLSDLLLGG 96
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 720-861 3.58e-03

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: 38.59  E-value: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422895  720 ISVHIIRACGLqaaakalaeqePALQFSATVgvNASVTAHLSflpKGEQRQTRPVACSFCPEFSHHIEFPCNLVTQHcsg 799
Cdd:cd00030      1 LRVTVIEARNL-----------PAKDLNGKS--DPYVKVSLG---GKQKFKTKVVKNTLNPVWNETFEFPVLDPESD--- 61

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720422895  800 eacflaellefaEIIFAIYHENTKSvsditsiqscKDYLLGIVKVPTKDLLVKRSGITGWYP 861
Cdd:cd00030     62 ------------TLTVEVWDKDRFS----------KDDFLGEVEIPLSELLDSGKEGELWLP 101
 
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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