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Conserved domains on  [gi|530419214|ref|XP_005261166|]
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C2 domain-containing protein 2 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 110-236 9.45e-55

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: 180.64  E-value: 9.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419214 110 LLVRNIHVLLLSEpgASGHINAVCVVQLNDPVQRFSSTLTKNTPDLMWEEEFTFELNAKSKELHLQISEAGRSSE-GLLA 188
Cdd:cd08678    1 LLVKNIKANGLSE--AAGSSNPYCVLEMDEPPQKYQSSTQKNTSNPFWDEHFLFELSPNSKELLFEVYDNGKKSDsKFLG 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 530419214 189 TATVPLDLFKKQPSGPQSFTLTSGSACGSSVLGSVTAEFSYMEPGELK 236
Cdd:cd08678   79 LAIVPFDELRKNPSGRQIFPLQGRPYEGDSVSGSITVEFLFMEPAELP 126
SMP_SF super family cl45903
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP ...
 1-79 7.57e-34

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP domain is a lipid transport domain found in phospholipid transfer proteins such as synaptotagmin family proteins, tricalbin (TCB) family proteins, maintenance of mitochondrial morphology protein 1 (MMM1), mitochondrial distribution and morphology protein 12 (MDM12), mitochondrial distribution and morphology protein 34 (MDM34), PDZ domain-containing protein 8 (PDZD8), testis-expressed protein 2 (TEX2), meiotically up-regulated gene 190 protein (Mug190), C2 domain-containing protein 2 (C2CD2) and C2 domain-containing protein 2-like (C2CD2L). The SMP domain belongs to a superfamily of lipid/hydrophobic ligand-binding domains called TULIP (tubular lipid-binding proteins). It adopts a TULIP fold with two alpha helices and a highly curved antiparallel beta sheet forming a cornucopia-like structure.


The actual alignment was detected with superfamily member cd21682:

Pssm-ID: 459248  Cd Length: 175  Bit Score: 126.21  E-value: 7.57e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530419214   1 MRLSPFHLQLEFHMKEKREDLQISWSFISVPEMAVNIQPKALGEdqVAETSAMSDVLKDILKHLAGSASPSVVLITKPT 79
Cdd:cd21682   99 VKLSPLHLQLELHMKEKREDIQVSWSFSHLDETNLQVQPKATQE--VDETSASSEALKDILKQLLCSASPSVVLSTRPA 175
 
Name Accession Description Interval E-value
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 110-236 9.45e-55

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: 180.64  E-value: 9.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419214 110 LLVRNIHVLLLSEpgASGHINAVCVVQLNDPVQRFSSTLTKNTPDLMWEEEFTFELNAKSKELHLQISEAGRSSE-GLLA 188
Cdd:cd08678    1 LLVKNIKANGLSE--AAGSSNPYCVLEMDEPPQKYQSSTQKNTSNPFWDEHFLFELSPNSKELLFEVYDNGKKSDsKFLG 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 530419214 189 TATVPLDLFKKQPSGPQSFTLTSGSACGSSVLGSVTAEFSYMEPGELK 236
Cdd:cd08678   79 LAIVPFDELRKNPSGRQIFPLQGRPYEGDSVSGSITVEFLFMEPAELP 126
SMP_C2CD2 cd21682
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ...
 1-79 7.57e-34

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: 126.21  E-value: 7.57e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530419214   1 MRLSPFHLQLEFHMKEKREDLQISWSFISVPEMAVNIQPKALGEdqVAETSAMSDVLKDILKHLAGSASPSVVLITKPT 79
Cdd:cd21682   99 VKLSPLHLQLELHMKEKREDIQVSWSFSHLDETNLQVQPKATQE--VDETSASSEALKDILKQLLCSASPSVVLSTRPA 175
SMP_C2CD2L pfam18696
Synaptotagmin-like, mitochondrial and lipid-binding domain; This is a lipid transport domain ...
 2-72 1.32e-28

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: 110.82  E-value: 1.32e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530419214    2 RLSPFHLQLEFHMKEKREDLQISWSFISVPEMAVNIQPKALGEdQVAETSAMSDVLKDILKHLAGSASPSV 72
Cdd:pfam18696  83 TLSPLHLQLELHMEEKEEDIQISWSFSHLPELSLQVTPKAQQE-QVNETAAVSETLKDLLKDLLSSASPSV 152
C2 pfam00168
C2 domain;
120-209 1.11e-07

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 50.01  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419214  120 LSEPGASGHINAVCVVQLNDPVQRFSSTLTKNTPDLMWEEEFTFEL-NAKSKELHLQISEAGR-SSEGLLATATVPLDLF 197
Cdd:pfam00168  13 LPPKDGNGTSDPYVKVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVpDPENAVLEIEVYDYDRfGRDDFIGEVRIPLSEL 92

                          90
                  ....*....|..
gi 530419214  198 KKQPSGPQSFTL 209
Cdd:pfam00168  93 DSGEGLDGWYPL 104
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 109-201 4.63e-04

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: 4.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419214   109 KLLVRNIHVLLLSEPGASGHINAVCVVQLN-DPVQRFSSTLTKNTPDLMWEEEFTFELN-AKSKELHLQISEAGR-SSEG 185
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDgDPKEKKKTKVVKNTLNPVWNETFEFEVPpPELAELEIEVYDKDRfGRDD 80

                           90
                   ....*....|....*.
gi 530419214   186 LLATATVPLDLFKKQP 201
Cdd:smart00239  81 FIGQVTIPLSDLLLGG 96
 
Name Accession Description Interval E-value
C2_C21orf25-like cd08678
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ...
 110-236 9.45e-55

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: 180.64  E-value: 9.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419214 110 LLVRNIHVLLLSEpgASGHINAVCVVQLNDPVQRFSSTLTKNTPDLMWEEEFTFELNAKSKELHLQISEAGRSSE-GLLA 188
Cdd:cd08678    1 LLVKNIKANGLSE--AAGSSNPYCVLEMDEPPQKYQSSTQKNTSNPFWDEHFLFELSPNSKELLFEVYDNGKKSDsKFLG 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 530419214 189 TATVPLDLFKKQPSGPQSFTLTSGSACGSSVLGSVTAEFSYMEPGELK 236
Cdd:cd08678   79 LAIVPFDELRKNPSGRQIFPLQGRPYEGDSVSGSITVEFLFMEPAELP 126
SMP_C2CD2 cd21682
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ...
 1-79 7.57e-34

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: 126.21  E-value: 7.57e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530419214   1 MRLSPFHLQLEFHMKEKREDLQISWSFISVPEMAVNIQPKALGEdqVAETSAMSDVLKDILKHLAGSASPSVVLITKPT 79
Cdd:cd21682   99 VKLSPLHLQLELHMKEKREDIQVSWSFSHLDETNLQVQPKATQE--VDETSASSEALKDILKQLLCSASPSVVLSTRPA 175
SMP_C2CD2L pfam18696
Synaptotagmin-like, mitochondrial and lipid-binding domain; This is a lipid transport domain ...
 2-72 1.32e-28

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: 110.82  E-value: 1.32e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530419214    2 RLSPFHLQLEFHMKEKREDLQISWSFISVPEMAVNIQPKALGEdQVAETSAMSDVLKDILKHLAGSASPSV 72
Cdd:pfam18696  83 TLSPLHLQLELHMEEKEEDIQISWSFSHLPELSLQVTPKAQQE-QVNETAAVSETLKDLLKDLLSSASPSV 152
SMP_C2CD2-like cd21664
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in C2 ...
 1-79 4.86e-22

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: 93.19  E-value: 4.86e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530419214   1 MRLSPFHLQLEFHMKEKREDLQISWSFISVPEMAVNIQPKALGedQVAETSAMSDVLKDILKHLAGSASPSVVLITKPT 79
Cdd:cd21664   99 VSVTKLSGKLRCHGRTLGEELQISVSFEDRPDLKLNIKPKNGS--PTAEDSVDLDVVEEIVRNAIASATTTFVLPTQAT 175
C2 pfam00168
C2 domain;
120-209 1.11e-07

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 50.01  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419214  120 LSEPGASGHINAVCVVQLNDPVQRFSSTLTKNTPDLMWEEEFTFEL-NAKSKELHLQISEAGR-SSEGLLATATVPLDLF 197
Cdd:pfam00168  13 LPPKDGNGTSDPYVKVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVpDPENAVLEIEVYDYDRfGRDDFIGEVRIPLSEL 92

                          90
                  ....*....|..
gi 530419214  198 KKQPSGPQSFTL 209
Cdd:pfam00168  93 DSGEGLDGWYPL 104
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 110-209 5.50e-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: 45.14  E-value: 5.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419214 110 LLVRNIHVLLLSEPGASGHINAVCVVQLnDPVQRFSSTLTKNTPDLMWEEEFTFEL-NAKSKELHLQI-SEAGRSSEGLL 187
Cdd:cd00030    1 LRVTVIEARNLPAKDLNGKSDPYVKVSL-GGKQKFKTKVVKNTLNPVWNETFEFPVlDPESDTLTVEVwDKDRFSKDDFL 79

                         90       100
                 ....*....|....*....|...
gi 530419214 188 ATATVPL-DLFKKQPSGPQSFTL 209
Cdd:cd00030   80 GEVEIPLsELLDSGKEGELWLPL 102
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
 109-201 4.63e-04

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: 4.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419214   109 KLLVRNIHVLLLSEPGASGHINAVCVVQLN-DPVQRFSSTLTKNTPDLMWEEEFTFELN-AKSKELHLQISEAGR-SSEG 185
Cdd:smart00239   1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDgDPKEKKKTKVVKNTLNPVWNETFEFEVPpPELAELEIEVYDKDRfGRDD 80

                           90
                   ....*....|....*.
gi 530419214   186 LLATATVPLDLFKKQP 201
Cdd:smart00239  81 FIGQVTIPLSDLLLGG 96
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
 130-229 3.59e-03

C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating protein 1), a Ras-specific GAP member, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA1 contains a C2 domain, a Ras-GAP domain, a pleckstrin homology (PH)-like domain, a SH3 domain, and 2 SH2 domains. 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. Members here have a type-I topology.


Pssm-ID: 176045 [Multi-domain]  Cd Length: 126  Bit Score: 37.73  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419214 130 NAVCVVQLNDpVQrFSSTLTKNTPDLMWEEEFTFE-LNAKSKELHLQISEAG-RSSEGLLATATVPLDLFKKQPSGPQSF 207
Cdd:cd08400   23 HPYCVISLNE-VK-VARTKVREGPNPVWSEEFVFDdLPPDVNSFTISLSNKAkRSKDSEIAEVTVQLSKLQNGQETDEWY 100

                         90       100
                 ....*....|....*....|..
gi 530419214 208 TLTSGSACGSSVLGSVTAEFSY 229
Cdd:cd08400  101 PLSSASPLKGGEWGSLRIRARY 122
 
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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