VM3_BUNMU
ID VM3_BUNMU Reviewed; 614 AA.
AC A8QL49;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like BmMP;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Bungarus multicinctus (Many-banded krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=8616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=17337026; DOI=10.1016/j.toxicon.2007.01.003;
RA Guo X.-X., Zeng L., Lee W.-H., Zhang Y., Jin Y.;
RT "Isolation and cloning of a metalloproteinase from king cobra snake
RT venom.";
RL Toxicon 49:954-965(2007).
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 inhibits platelet
CC aggregation and degrades fibrinogen. {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: Monomer. {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-IIIa sub-subfamily. {ECO:0000305}.
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DR EMBL; EF080830; ABN72537.1; -; mRNA.
DR AlphaFoldDB; A8QL49; -.
DR SMR; A8QL49; -.
DR MEROPS; M12.159; -.
DR PRIDE; A8QL49; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043655; C:host extracellular space; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044485; P:envenomation resulting in fibrinogenolysis in another organism; ISS:UniProtKB.
DR GO; GO:0044358; P:envenomation resulting in hemorrhagic damage in another organism; ISS:UniProtKB.
DR GO; GO:0044477; P:envenomation resulting in negative regulation of platelet aggregation in another organism; ISS:UniProtKB.
DR GO; GO:0044481; P:envenomation resulting in proteolysis in another organism; ISS:UniProtKB.
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 Cell adhesion impairing toxin; Disulfide bond; Fibrinogenolytic toxin;
KW Glycoprotein; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Platelet aggregation inhibiting toxin; Protease; Secreted;
KW Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..188
FT /evidence="ECO:0000250"
FT /id="PRO_0000417637"
FT CHAIN 189..614
FT /note="Zinc metalloproteinase-disintegrin-like BmMP"
FT /id="PRO_0000417638"
FT DOMAIN 205..401
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 409..495
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 473..475
FT /note="D/ECD-tripeptide"
FT ACT_SITE 342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 316..396
FT /evidence="ECO:0000250"
FT DISULFID 356..380
FT /evidence="ECO:0000250"
FT DISULFID 359..364
FT /evidence="ECO:0000250"
FT DISULFID 412..441
FT /evidence="ECO:0000250"
FT DISULFID 423..436
FT /evidence="ECO:0000250"
FT DISULFID 425..431
FT /evidence="ECO:0000250"
FT DISULFID 435..458
FT /evidence="ECO:0000250"
FT DISULFID 449..455
FT /evidence="ECO:0000250"
FT DISULFID 454..480
FT /evidence="ECO:0000250"
FT DISULFID 467..487
FT /evidence="ECO:0000250"
FT DISULFID 474..506
FT /evidence="ECO:0000250"
FT DISULFID 499..511
FT /evidence="ECO:0000250"
FT DISULFID 518..568
FT /evidence="ECO:0000250"
FT DISULFID 533..576
FT /evidence="ECO:0000250"
FT DISULFID 546..556
FT /evidence="ECO:0000250"
FT DISULFID 563..602
FT /evidence="ECO:0000250"
FT DISULFID 596..607
FT /evidence="ECO:0000250"
SQ SEQUENCE 614 AA; 68988 MW; 4A8BF9BF446E7C23 CRC64;
MIQALLVTIC LAVFPYQGSS IILESGNVND YEVVYPQKVP LLPKGGVQNP QPKTKYEDTV
QYEFEVNGEP VVLHLERNKG LFSEDYTEAH YAPDGREITT RPPVQDHCYY HGYIQNEADS
SAAISACDGL KGHFKHQGET YFIEPLKLSD SEAHAIYKDE NVEEENETPK ICGLTETTWE
SDEPIRNASL LIYTPEQNRY LKVKKYIEFY VAVDNRMYRH YKRNKPIIKR RVYELVNILN
TILRRLNFHI ALIGLEIWSK RDKINVQSDV KATLKSFGKW REKKLLPRKR NDNAQLLTRI
DFNGNTVGLA ALGSLCSVKY SVAVIQDYSK RTSMVASTMA HEMGHNLGIN HDRASCTSCG
SNKCIMATKR TKPASRFSSC SVREHQRYLL RDRPQCILNK PLITDIVAPA ICGNYFVEVG
EECDCGSPRD CRSACCNAAT CKLKHEAQCD SGECCGKCKF KKVGAKCRAA KDDCDLPERC
TGRSAECPTD IFRRNGLPCQ NKQGYCYNGK CPTLTNQCIA LMGPNVKVSR DSCFTLNQRG
KGCGYCRMQN GAKIPCAAKD IKCGKLFCKK RNSGVCNCLI LPDDPNYGMV ETGTKCGDGM
VCSDRKCVKL QTVY
