VM3_MICIK
ID VM3_MICIK Reviewed; 169 AA.
AC P0DJ43;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like mikarin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Fragments;
OS Micropechis ikaheca (New Guinean small-eyed snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Notechinae; Micropechis.
OX NCBI_TaxID=66188;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=12485606; DOI=10.1016/s0003-9861(02)00447-2;
RA Gao R., Kini R.M., Gopalakrishnakone P.;
RT "A novel prothrombin activator from the venom of Micropechis ikaheka:
RT isolation and characterization.";
RL Arch. Biochem. Biophys. 408:87-92(2002).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that calcium-independently
CC catalyzes the conversion of prothrombin (F2) to alpha-thrombin through
CC the formation of a thrombin intermediate.
CC {ECO:0000269|PubMed:12485606}.
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, but not by PMSF.
CC {ECO:0000269|PubMed:12485606}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12485606}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not have an affect on factor X (F10) and
CC fibrinogen. {ECO:0000305|PubMed:12485606}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-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; P0DJ43; -.
DR PRIDE; P0DJ43; -.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0043655; C:host extracellular space; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0016504; F:peptidase activator activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044469; P:envenomation resulting in positive regulation of blood coagulation in another organism; IDA:UniProtKB.
DR GO; GO:0044481; P:envenomation resulting in proteolysis in another organism; IDA:UniProtKB.
DR GO; GO:0010952; P:positive regulation of peptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Prothrombin activator; Secreted; Toxin; Zinc.
FT CHAIN 1..169
FT /note="Zinc metalloproteinase-disintegrin-like mikarin"
FT /id="PRO_0000418035"
FT DOMAIN 14..57
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 65..>129
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 116..118
FT /note="D/ECD-tripeptide"
FT DISULFID 68..97
FT /evidence="ECO:0000250"
FT DISULFID 79..92
FT /evidence="ECO:0000250"
FT DISULFID 81..87
FT /evidence="ECO:0000250"
FT DISULFID 105..111
FT /evidence="ECO:0000250"
FT DISULFID 110..123
FT /evidence="ECO:0000250"
FT DISULFID 150..161
FT /evidence="ECO:0000250"
FT NON_CONS 30..31
FT /evidence="ECO:0000305"
FT NON_CONS 57..58
FT /evidence="ECO:0000305"
FT NON_CONS 113..114
FT /evidence="ECO:0000305"
FT NON_CONS 129..130
FT /evidence="ECO:0000305"
SQ SEQUENCE 169 AA; 18439 MW; 29E83FDA889EEE40 CRC64;
TNTPEQDRYL QVKKYLEYVV VDNNMYRNYG NAGPCVMSAE ISFEPLQEFS SCDIQEPLSQ
DIVQPAVCGN YYVEVGGECD CGSPKPCRSA CCNAATCKLQ REHQCDSGEC CEKKDDCDLP
EICTGRSAKC SCVISQGDLG YGMVEPGTKC TDGMVCSNEQ CVDVQTAAK
