VM1K_CALRH
ID VM1K_CALRH Reviewed; 417 AA.
AC P0CB14;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Snake venom metalloproteinase kistomin;
DE Short=SVMP;
DE EC=3.4.24.-;
DE Flags: Precursor;
OS Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Calloselasma.
OX NCBI_TaxID=8717;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 277-296; 210-221 AND
RP 356-370, FUNCTION, AND ACTIVITY REGULATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=17609416; DOI=10.1124/mol.107.038018;
RA Hsu C.C., Wu W.B., Chang Y.H., Kuo H.L., Huang T.F.;
RT "Antithrombotic effect of a protein-type I class snake venom
RT metalloproteinase, kistomin, is mediated by affecting glycoprotein Ib-von
RT Willebrand factor interaction.";
RL Mol. Pharmacol. 72:984-992(2007).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Venom;
RX PubMed=18624975; DOI=10.1111/j.1538-7836.2008.03071.x;
RA Hsu C.C., Wu W.B., Huang T.F.;
RT "A snake venom metalloproteinase, kistomin, cleaves platelet glycoprotein
RT VI and impairs platelet functions.";
RL J. Thromb. Haemost. 6:1578-1585(2008).
RN [3]
RP FUNCTION.
RX PubMed=8251530; DOI=10.1016/0304-4165(93)90028-7;
RA Huang T.F., Chang M.C., Teng C.M.;
RT "Antiplatelet protease, kistomin, selectively cleaves human platelet
RT glycoprotein Ib.";
RL Biochim. Biophys. Acta 1158:293-299(1993).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=1477097; DOI=10.1016/0167-4838(92)90086-s;
RA Huang T.F., Chang M.C., Peng H.C., Teng C.M.;
RT "A novel alpha-type fibrinogenase from Agkistrodon rhodostoma snake
RT venom.";
RL Biochim. Biophys. Acta 1160:262-268(1992).
CC -!- FUNCTION: Snake venom zinc metalloprotease that inhibits platelet
CC aggregation by binding specifically to platelet glycoprotein VI (GP6)
CC and platelet glycoprotein Ib alpha (GP1BA). It inhibits the interaction
CC between collagen and platelet GP6 by cleaving GP6 (at '225-Glu-|-Ala-
CC 226' and '238-Val-|-Phe-239' bonds), and inhibits vWF-induced platelet
CC aggregation by cleaving GP1BA and vWF. Cleavage of GP1BA occurs at two
CC distinct sites to generate two soluble fragments. It also cleaves
CC alpha- (FGA) and subsequently the gamma-chain (FGG) of fibrinogen,
CC leaving the beta-chain unaffected. It also inhibits collagen-,
CC convulxin- and ristocetin-induced platelet aggregation. It blocks the
CC adhesion of platelet to immobilized collagen, but only exerts a slight
CC inhibition to fibrinogen. In vivo, it exerts potent antithrombotic
CC effect. {ECO:0000269|PubMed:1477097, ECO:0000269|PubMed:17609416,
CC ECO:0000269|PubMed:18624975, ECO:0000269|PubMed:8251530}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, and O-phenanthrolene.
CC {ECO:0000269|PubMed:1477097, ECO:0000269|PubMed:17609416}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
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; P0CB14; -.
DR SMR; P0CB14; -.
DR PRIDE; P0CB14; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IDA:CACAO.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0035893; P:negative regulation of platelet aggregation in another organism; IDA:CACAO.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Signal; Toxin;
KW Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..189
FT /evidence="ECO:0000250"
FT /id="PRO_0000380630"
FT CHAIN 190..391
FT /note="Snake venom metalloproteinase kistomin"
FT /id="PRO_0000380631"
FT PROPEP 392..417
FT /evidence="ECO:0000250"
FT /id="PRO_0000380632"
FT DOMAIN 197..391
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 308..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 348..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 350..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 417 AA; 47446 MW; EFD47D4A93B17A45 CRC64;
MIEVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKIT ALSEGAAQQK YEDTMQYEFK
VNGEPVVLHL EKNKELFAKD YSETHYSPDG TRITTYPSVE DHCYYQGRIH NDADSTASIS
TCNGLKGHFK FHGERYFIEP LKLPGSEAHA VYKYENIEKE DETPKMCGVI QKWKSDELIK
KPFRLNLTPQ QQESPQAKVY LVIVADKSMV DKHNGNIKKI EEQGHQMVNT MNECYRPMGI
IIIMAGIECW TTNDFFEVKS SAKETLYSFA KWRVEDLSKR KPHNDAQFLT NKDFDGNTVG
LAFVGGICNE KYCAGVVQDH TKVPLLMAIT MGHEIGHNLG MEHDEANCKC KACVMAPEVN
NNPTKKFSDC SRNYYQKFLK DRKPECLFKK PLRTDTVSTP VSGNEPLEVI TMDDFYA
