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VM3BP_BOTJA
ID   VM3BP_BOTJA             Reviewed;         610 AA.
AC   O93523;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Zinc metalloproteinase-disintegrin-like bothropasin {ECO:0000303|PubMed:6819660};
DE            EC=3.4.24.49;
DE   AltName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE   Contains:
DE     RecName: Full=Disintegrin-like bothropasin;
DE   Flags: Precursor;
OS   Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 248-253; 257-268; 273-276;
RP   296-303 AND 395-420, AND FUNCTION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=12565741; DOI=10.1016/s0041-0101(02)00279-9;
RA   Assakura M.T., Silva C.A., Mentele R., Camargo A.C.M., Serrano S.M.T.;
RT   "Molecular cloning and expression of structural domains of bothropasin, a
RT   P-III metalloproteinase from the venom of Bothrops jararaca.";
RL   Toxicon 41:217-227(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=6819660; DOI=10.1016/0041-0101(82)90098-8;
RA   Mandelbaum F.R., Reichel A.P., Assakura M.T.;
RT   "Isolation and characterization of a proteolytic enzyme from the venom of
RT   the snake Bothrops jararaca (Jararaca).";
RL   Toxicon 20:955-972(1982).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 192-610 IN COMPLEX WITH ZINC AND
RP   CALCIUM IONS, COFACTOR, METAL-BINDING SITES, GLYCOSYLATION AT ASN-372,
RP   PYROGLUTAMATE FORMATION AT GLN-192, AND DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=18831982; DOI=10.1016/j.toxicon.2008.08.021;
RA   Muniz J.R.C., Ambrosio A.L.B., Selistre-de-Araujo H.S., Cominetti M.R.,
RA   Moura-da-Silva A.M., Oliva G., Garratt R.C., Souza D.H.F.;
RT   "The three-dimensional structure of bothropasin, the main hemorrhagic
RT   factor from Bothrops jararaca venom: insights for a new classification of
RT   snake venom metalloprotease subgroups.";
RL   Toxicon 52:807-816(2008).
CC   -!- FUNCTION: [Zinc metalloproteinase-disintegrin-like bothropasin]: Has
CC       caseinolytic activity. Causes hemorrhage on rabbit skin and causes
CC       myonecrosis in mouse tibialis anterior muscle.
CC   -!- FUNCTION: [Disintegrin-like bothropasin]: Inhibits platelet
CC       aggregation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15,
CC         16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 in insulin B chain.;
CC         EC=3.4.24.49; Evidence={ECO:0000269|PubMed:6819660};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:18831982};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18831982};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA and EGTA.
CC       {ECO:0000269|PubMed:6819660}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18831982,
CC       ECO:0000269|PubMed:6819660}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: The metalloproteinase domain which is released from the
CC       cleavage of the disintegrin bothropasin may be unstable.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. P-IIIb sub-subfamily. {ECO:0000305}.
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DR   EMBL; AF056025; AAC61986.2; -; mRNA.
DR   PDB; 3DSL; X-ray; 2.70 A; A/B=192-610.
DR   PDBsum; 3DSL; -.
DR   AlphaFoldDB; O93523; -.
DR   SMR; O93523; -.
DR   MEROPS; M12.140; -.
DR   iPTMnet; O93523; -.
DR   KEGG; ag:AAC61986; -.
DR   BRENDA; 3.4.24.49; 911.
DR   EvolutionaryTrace; O93523; -.
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   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; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 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   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell adhesion impairing toxin;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hemorrhagic toxin;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Platelet aggregation inhibiting toxin; Protease;
KW   Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Zinc; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..191
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000326418"
FT   CHAIN           192..610
FT                   /note="Zinc metalloproteinase-disintegrin-like bothropasin"
FT                   /evidence="ECO:0000269|PubMed:18831982"
FT                   /id="PRO_0000326419"
FT   CHAIN           399..610
FT                   /note="Disintegrin-like bothropasin"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000326420"
FT   DOMAIN          198..394
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          402..488
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           466..468
FT                   /note="D/ECD-tripeptide"
FT   ACT_SITE        335
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         201
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         285
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         334
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         338
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         344
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         389
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         392
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         404
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         407
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         409
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         411
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         414
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         417
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         468
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         469
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         471
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         483
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   BINDING         484
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   SITE            378
FT                   /note="Necessary, but not sufficient, for proteolytic
FT                   processing"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         192
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:18831982"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:18831982"
FT   DISULFID        309..389
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        349..373
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        351..356
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        405..434
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin; alternate"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        405..424
FT                   /note="In disintegrin-like bothropasin; alternate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        416..434
FT                   /note="In disintegrin-like bothropasin; alternate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        416..429
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin; alternate"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        418..424
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin; alternate"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        428..451
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        442..448
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        447..473
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        460..480
FT                   /note="In both disintegrin-like bothropasin and zinc
FT                   metalloproteinase-disintegrin-like bothropasin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000269|PubMed:18831982, ECO:0000312|PDB:3DSL"
FT   DISULFID        467..499
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin; alternate"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        467..492
FT                   /note="In disintegrin-like bothropasin; alternate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        492..504
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin; alternate"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        499..504
FT                   /note="In disintegrin-like bothropasin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        511..561
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin; alternate"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        511..526
FT                   /note="In disintegrin-like bothropasin; alternate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        526..572
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin; alternate"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        539..549
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin; alternate"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        549..556
FT                   /note="In disintegrin-like bothropasin; alternate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        556..598
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin; alternate"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        561..572
FT                   /note="In disintegrin-like bothropasin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        592..603
FT                   /note="In zinc metalloproteinase-disintegrin-like
FT                   bothropasin; alternate"
FT                   /evidence="ECO:0000269|PubMed:18831982,
FT                   ECO:0000312|PDB:3DSL"
FT   DISULFID        598..603
FT                   /note="In disintegrin-like bothropasin"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   610 AA;  68213 MW;  014C8AE6B86F25DD CRC64;
     MIEVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQPK YEDAMQYEFK
     VNGEPVVLHL EKNKGLFSKD YSETHYSPDG REITTYPAVE DHCYYHGRIE NDADSTASIS
     ACNGLKGHFK LQRETYFIEP LKLSNSEAHA VFKYENVEKE DEAPKMCGVT QNWKSYEPIK
     KASQLVVTAE QQKYNPFRYV ELFIVVDQGM VTKNNGDLDK IKARMYELAN IVNEILRYLY
     MHAALVGLEI WSNGDKITVK PDVDYTLNSF AEWRKTDLLT RKKHDNAQLL TAIDFNGPTI
     GYAYIGSMCH PKRSVAIVED YSPINLVVAV IMAHEMGHNL GIHHDTDFCS CGDYPCIMGP
     TISNEPSKFF SNCSYIQCWD FIMKENPQCI LNEPLGTDIV SPPVCGNELL EVGEECDCGT
     PENCQNECCD AATCKLKSGS QCGHGDCCEQ CKFSKSGTEC RASMSECDPA EHCTGQSSEC
     PADVFHKNGQ PCLDNYGYCY NGNCPIMYHQ CYALFGADVY EAEDSCFKDN QKGNYYGYCR
     KENGKKIPCA PEDVKCGRLY CKDNSPGQNN PCKMFYSNDD EHKGMVLPGT KCADGKVCSN
     GHCVDVATAY
 
 
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