ID VSP1_AGKBI Reviewed; 20 AA. AC P33588; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 16-JUN-2009, entry version 47. DE RecName: Full=Ancrod; DE EC=3.4.21.74; DE AltName: Full=Venombin-A; DE AltName: Full=Protein C activator; DE AltName: Full=ACC-C; DE Flags: Fragment; OS Agkistrodon bilineatus (Cantil) (Tropical moccasin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea; OC Viperidae; Crotalinae; Agkistrodon. OX NCBI_TaxID=8718; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Venom; RX MEDLINE=90350102; PubMed=2385829; DOI=10.1016/0049-3848(90)90305-V; RA Nakagaki T., Kazim A.L., Kisiel W.; RT "Isolation and characterization of a protein C activator from tropical RT moccasin venom."; RL Thromb. Res. 58:593-602(1990). CC -!- FUNCTION: Thrombin-like snake venom serine protease. Activates CC protein C. CC -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Xaa bond in CC fibrinogen, to form fibrin, and release fibrinopeptide A. The CC specificity of further degradation of fibrinogen varies with CC species origin of the enzyme. CC -!- SUBCELLULAR LOCATION: Secreted (Potential). CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Snake venom CC subfamily. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A60489; A60489. DR MEROPS; S01.178; -. DR HOVERGEN; P33588; -. DR BRENDA; 3.4.21.74; 279476. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW. DR InterPro; IPR018114; Peptidase_S1/S6_AS. DR PROSITE; PS50240; TRYPSIN_DOM; PARTIAL. DR PROSITE; PS00134; TRYPSIN_HIS; PARTIAL. DR PROSITE; PS00135; TRYPSIN_SER; PARTIAL. PE 1: Evidence at protein level; KW Direct protein sequencing; Hydrolase; Protease; Secreted; KW Serine protease; Toxin. FT CHAIN 1 >20 Ancrod. FT /FTId=PRO_0000088724. FT DOMAIN 1 >20 Peptidase S1. FT NON_TER 20 20 SQ SEQUENCE 20 AA; 2191 MW; 6E99F8B4CC53EFE1 CRC64; VVGGDECNIN EHRSLALMYA //