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VM31_CRODC
ID   VM31_CRODC              Reviewed;         418 AA.
AC   C5H5D1;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Zinc metalloproteinase-disintegrin-like crotastatin;
DE            EC=3.4.24.-;
DE   AltName: Full=Crotastatin-1;
DE   AltName: Full=Snake venom metalloprotease;
DE            Short=SVMP;
DE   AltName: Full=Vascular apoptosis-inducing protein-like;
DE            Short=VAP-like;
DE   Flags: Fragment;
OS   Crotalus durissus cascavella (Northeastern Brazilian rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=184540;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=18926840; DOI=10.1016/j.toxicon.2008.08.022;
RA   Tavares N.A.C., Correia J.M., Guarnieri M.C., Lima-Filho J.L.,
RA   Prieto-da-Silva A.R.B., Radis-Baptista G.;
RT   "Expression of mRNAs coding for VAP1/crotastatin-like metalloproteases in
RT   the venom glands of three South American pit vipers assessed by
RT   quantitative real-time PCR.";
RL   Toxicon 52:897-907(2008).
CC   -!- FUNCTION: Snake venom zinc metalloprotease that induces apoptosis in
CC       vascular endothelial cells (VEC), without degrading the extracellular
CC       matrix (it cannot cleave collagen) or inhibiting adhesion of VEC. Has
CC       also fibrinogenolytic and hemorrhagic activities (By similarity).
CC       {ECO:0000250}.
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: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. P-IIIc sub-subfamily. {ECO:0000305}.
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DR   EMBL; EU733638; ACI02286.1; -; mRNA.
DR   AlphaFoldDB; C5H5D1; -.
DR   SMR; C5H5D1; -.
DR   MEROPS; M12.186; -.
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:0006915; P:apoptotic process; 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   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Calcium; Cell adhesion impairing toxin; Disulfide bond;
KW   Fibrinogenolytic toxin; Glycoprotein; Hemorrhagic toxin;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Toxin; Zinc.
FT   CHAIN           1..>418
FT                   /note="Zinc metalloproteinase-disintegrin-like crotastatin"
FT                   /id="PRO_0000418201"
FT   DOMAIN          10..206
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          214..299
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           278..280
FT                   /note="D/ECD-tripeptide"
FT   ACT_SITE        147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        121..201
FT                   /evidence="ECO:0000250"
FT   DISULFID        161..185
FT                   /evidence="ECO:0000250"
FT   DISULFID        163..168
FT                   /evidence="ECO:0000250"
FT   DISULFID        176
FT                   /note="Interchain (with C-365)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DISULFID        217..246
FT                   /evidence="ECO:0000250"
FT   DISULFID        228..241
FT                   /evidence="ECO:0000250"
FT   DISULFID        230..236
FT                   /evidence="ECO:0000250"
FT   DISULFID        240..263
FT                   /evidence="ECO:0000250"
FT   DISULFID        254..260
FT                   /evidence="ECO:0000250"
FT   DISULFID        259..285
FT                   /evidence="ECO:0000250"
FT   DISULFID        272..292
FT                   /evidence="ECO:0000250"
FT   DISULFID        279..310
FT                   /evidence="ECO:0000250"
FT   DISULFID        303..315
FT                   /evidence="ECO:0000250"
FT   DISULFID        322..372
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..383
FT                   /evidence="ECO:0000250"
FT   DISULFID        350..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        367..409
FT                   /evidence="ECO:0000250"
FT   DISULFID        403..414
FT                   /evidence="ECO:0000250"
FT   NON_TER         418
SQ   SEQUENCE   418 AA;  46165 MW;  CFBB8B8BCF4A2869 CRC64;
     EQQKYLNAKK YVKLFLVADY IMYLKYGRNL TAVRTRMYDI VNVITPIYHR MNIHVALVGL
     EIWSNTDKII VQSSADVTLD LFAKWRATDL LSRKSHDNAQ LLTGINFNGP TAGLGYLGGI
     CNTMYSAGIV QDHSKIHDLV AIAIAHEMGH NLGMDHDKDT CTCGTRPCIM AGVLSCEASF
     LFSDCSQKDH QEFLIKNMPQ CILKKPLKTD VVSPAVCGNY FVEVGEECDC GSPRTCRDPC
     CDAATCKLRQ GAQCAEGLCC DQCRFKGAGT ECRAAKDECD MADVCTGRST ECTDRFQRNG
     QPCKNNNGYC YNGKCPIMAD QCIALFGPGA TVSQDACFQF NREGNHYGYC RKEQNTKIAC
     EPQDVKCGRL YCFPNSPENK NPCNIYYSPN DEDKGMVLPG TKCADGKACS NGQCVDVT
 
 
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