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cl14603: C2 Superfamily 
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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.
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Taxonomy: root
PubMed: 54 links
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Protein: Related Protein
Related Structure
Statistics
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Accession: cl14603
PSSM Id: 265430
Name: C2
Created: 20-May-2010
Updated: 16-Jan-2014
Superfamily
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Curated CD Hierarchy
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cd00030:C2cd00275:C2_PLC_likecd00276:C2B_Synaptotagmincd04009:C2B_Munc13-likecd04010:C2B_RasA3cd04011:C2B_Ferlincd04012:C2A_PI3K_class_IIcd04013:C2_SynGAP_likecd04014:C2_PKC_epsiloncd04015:C2_plant_PLDcd04016:C2_Tollipcd04017:C2D_Ferlincd04018:C2C_Ferlincd04019:C2C_MCTP_PRT_plantcd04020:C2B_SLP_1-2-3-4cd04021:C2_E3_ubiquitin_ligasecd04022:C2A_MCTP_PRT_plantcd04024:C2A_Synaptotagmin-likecd04025:C2B_RasA1_RasA4cd04026:C2_PKC_alpha_gammacd04027:C2B_Munc13cd04028:C2B_RIM1alphacd04029:C2A_SLP-4_5cd04030:C2C_KIAA1228cd04031:C2A_RIM1alphacd04032:C2_Perforincd04033:C2_NEDD4_NEDD4Lcd04035:C2A_Rabphilin_Doc2cd04036:C2_cPLA2cd04037:C2E_Ferlincd04038:C2_ArfGAPcd04039:C2_PSDcd04040:C2D_Tricalbin-likecd04041:C2A_fungalcd04042:C2A_MCTP_PRTcd04043:C2_Munc13_fungalcd04044:C2A_Tricalbin-likecd04045:C2C_Tricalbin-likecd04046:C2_Calpaincd04047:C2B_Copinecd04048:C2A_Copinecd04049:C2_putative_Elicitor-responsive_genecd04050:C2B_Synaptotagmin-likecd04051:C2_SRC2_likecd04052:C2B_Tricalbin-likecd04054:C2A_Rasal1_RasA4cd08373:C2A_Ferlincd08374:C2F_Ferlincd08375:C2_Intersectincd08376:C2B_MCTP_PRTcd08377:C2C_MCTP_PRTcd08378:C2B_MCTP_PRT_plantcd08379:C2D_MCTP_PRT_plantcd08380:C2_PI3K_likecd08381:C2B_PI3K_class_IIcd08382:C2_Smurf-likecd08383:C2A_RasGAPcd08384:C2B_Rabphilin_Doc2cd08385:C2A_Synaptotagmin-1-5-6-9-10cd08386:C2A_Synaptotagmin-7cd08387:C2A_Synaptotagmin-8cd08388:C2A_Synaptotagmin-4-11cd08389:C2A_Synaptotagmin-14_16cd08390:C2A_Synaptotagmin-15-17cd08391:C2A_C2C_Synaptotagmin_likecd08392:C2A_SLP-3cd08393:C2A_SLP-1_2cd08394:C2A_Munc13cd08395:C2C_Munc13cd08397:C2_PI3K_class_IIIcd08398:C2_PI3K_class_I_alphacd08399:C2_PI3K_class_I_gammacd08400:C2_Ras_p21A1cd08401:C2A_RasA2_RasA3cd08402:C2B_Synaptotagmin-1cd08403:C2B_Synaptotagmin-3-5-6-9-10cd08404:C2B_Synaptotagmin-4cd08405:C2B_Synaptotagmin-7cd08406:C2B_Synaptotagmin-12cd08407:C2B_Synaptotagmin-13cd08408:C2B_Synaptotagmin-14_16cd08409:C2B_Synaptotagmin-15cd08410:C2B_Synaptotagmin-17cd08521:C2A_SLPcd08675:C2B_RasGAPcd08676:C2A_Munc13-likecd08677:C2A_Synaptotagmin-13cd08678:C2_C21orf25-likecd08679:C2_DOCK180_relatedcd08680:C2_Kibracd08681:C2_fungal_Inn1p-likecd08682:C2_Rab11-FIP_classIcd08683:C2_C2cd3cd08684:C2A_Tac2-Ncd08685:C2_RGS-likecd08686:C2_ABRcd08687:C2_PKN-likecd08688:C2_KIAA0528-likecd08689:C2_fungal_Pkc1pcd08690:C2_Freud-1cd08691:C2_NEDL1-likecd08692:C2B_Tac2-Ncd08693:C2_PI3K_class_I_beta_deltacd08694:C2_Dock-Acd08695:C2_Dock-Bcd08696:C2_Dock-Ccd08697:C2_Dock-D
CD Hierarchy
Imported CD
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Citing CDD
Marchler-Bauer A et al. (2013), "CDD: conserved domains and protein three-dimensional structure.", Nucleic Acids Res. 41(D1):D384-52.
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