ID DID5_CERCE Reviewed; 65 AA. AC P83041; P83042; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2001, sequence version 1. DT 02-SEP-2026, entry version 73. DE RecName: Full=Disintegrin CC5; DE Contains: DE RecName: Full=Disintegrin CC5B; OS Cerastes cerastes (Horned desert viper). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Viperidae; Viperinae; Cerastes. OX NCBI_TaxID=8697; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Venom; RX PubMed=11827548; DOI=10.1021/bi015627o; RA Calvete J.J., Fox J.W., Agelan A., Niewiarowski S., Marcinkiewicz C.; RT "The presence of the WGD motif in CC8 heterodimeric disintegrin increases RT its inhibitory effect on alphaII(b)beta3, alpha(v)beta3, and alpha5beta1 RT integrins."; RL Biochemistry 41:2014-2021(2002). CC -!- FUNCTION: Binds and inhibits integrins alpha-IIb/beta-3 (ITGA2B/ITGB3), CC alpha-V/beta-3 (ITGAV/ITGB3) and alpha-5/beta-1 (ITGA5/ITGB1). CC -!- SUBUNIT: Homodimer; disulfide-linked. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; P83041; -. DR SMR; P83041; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR Gene3D; 4.10.70.10; Disintegrin domain; 1. DR InterPro; IPR018358; Disintegrin_CS. DR InterPro; IPR001762; Disintegrin_dom. DR InterPro; IPR036436; Disintegrin_dom_sf. DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1. DR PANTHER; PTHR11905:SF159; ADAM METALLOPROTEASE; 1. DR Pfam; PF00200; Disintegrin; 1. DR PRINTS; PR00289; DISINTEGRIN. DR SMART; SM00050; DISIN; 1. DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1. DR PROSITE; PS00427; DISINTEGRIN_1; 1. DR PROSITE; PS50214; DISINTEGRIN_2; 1. PE 1: Evidence at protein level; KW Cell adhesion; Cell adhesion impairing toxin; Direct protein sequencing; KW Disulfide bond; Secreted; Toxin. FT CHAIN 1..65 FT /note="Disintegrin CC5" FT /id="PRO_0000045876" FT CHAIN 2..65 FT /note="Disintegrin CC5B" FT /id="PRO_0000045877" FT DOMAIN 1..65 FT /note="Disintegrin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068" FT MOTIF 43..45 FT /note="Cell attachment site" FT DISULFID 7..30 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068" FT DISULFID 8 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068" FT DISULFID 13 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068" FT DISULFID 21..27 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068" FT DISULFID 26..51 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068" FT DISULFID 39..58 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068" SQ SEQUENCE 65 AA; 7158 MW; 558BDF91EDA596E8 CRC64; MNSAHPCCDP VTCKPKRGEH CISGPCCRNC KFLSPGTICK KARGDDMNDY CTGISSDCPR NRYKS //