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VM1H2_CRORU
ID   VM1H2_CRORU             Reviewed;         202 AA.
AC   P20897;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Snake venom metalloproteinase HT-2;
DE            Short=SVMP;
DE            EC=3.4.24.48;
DE   AltName: Full=Hemorrhagic metalloproteinase HT-2;
DE   AltName: Full=Hemorrhagic toxin II;
DE   AltName: Full=Ruberlysin;
OS   Crotalus ruber ruber (Red diamond rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8736;
RN   [1]
RP   PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, AND DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=2081731; DOI=10.1093/oxfordjournals.jbchem.a123270;
RA   Takeya H., Onikura T., Sugihara H., Iwanaga S.;
RT   "Primary structure of a hemorrhagic metalloproteinase, HT-2, isolated from
RT   the venom of Crotalus ruber ruber.";
RL   J. Biochem. 108:711-719(1990).
CC   -!- FUNCTION: This protein is a zinc protease from snake venom that induces
CC       hemorrhage.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17
CC         and 23-Gly-|-Phe-24 bonds of the B chain of insulin, His-|-Pro,
CC         Pro-|-Phe, and Trp-|-Ser of angiotensin I, and Gly-|-Phe of Met
CC         enkephalin.; EC=3.4.24.48;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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}.
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DR   PIR; JX0139; HYRSR.
DR   AlphaFoldDB; P20897; -.
DR   SMR; P20897; -.
DR   MEROPS; M12.150; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
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; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Hemorrhagic toxin;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Pyrrolidone carboxylic acid; Secreted; Toxin; Zinc.
FT   CHAIN           1..202
FT                   /note="Snake venom metalloproteinase HT-2"
FT                   /id="PRO_0000078191"
FT   DOMAIN          6..202
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         9
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:2081731"
FT   DISULFID        117..197
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000269|PubMed:2081731"
FT   DISULFID        157..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000269|PubMed:2081731"
SQ   SEQUENCE   202 AA;  23321 MW;  5AF5D29318A61A9B CRC64;
     QNLPQSYIEL VVVADHRMFM KYNSDLNTIR TRVHEIVNFI NEFYRSLNIR VSLTDLEIWS
     DQDFITVQSS AKNTLHSFGE WRKSVLLNRK RHDNAQLLTA IVLDDYTLGL AYLNSMCHPR
     NSVGLIQDHS PINLLMGVTM AHELGHNLGM EHDGKDCLRG ASLCIMRPGL TPGRSYEFSD
     ASMRYYQKFL DQYKPQCILN KP
 
 
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