VM3_OPHHA
ID VM3_OPHHA Reviewed; 611 AA.
AC A3R0T9;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like ohanin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 188-212, FUNCTION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and 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 has hemorrhagic
CC activity. Inhibits ADP-, TMVA- and stejnulxin-induced platelet
CC aggregation in a dose-dependent manner (on washed platelet, but not on
CC platelet rich plasm). Also specifically degrades alpha-chain of
CC fibrinogen (FGA). {ECO:0000269|PubMed:17337026}.
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 -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not affect beta- (FGB) and gamma-chain (FGG) of
CC fibrinogen. Does not interfere with ristocetin-, thrombin-, and
CC collagen-induced platelet aggregation.
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; EF065674; ABM87941.1; -; mRNA.
DR AlphaFoldDB; A3R0T9; -.
DR SMR; A3R0T9; -.
DR MEROPS; M12.331; -.
DR TopDownProteomics; A3R0T9; -.
DR BRENDA; 3.4.24.51; 4419.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043655; C:host extracellular space; NAS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
DR GO; GO:0044485; P:envenomation resulting in fibrinogenolysis in another organism; IDA:UniProtKB.
DR GO; GO:0044358; P:envenomation resulting in hemorrhagic damage in another organism; IDA:UniProtKB.
DR GO; GO:0044477; P:envenomation resulting in negative regulation of platelet aggregation in another organism; IDA:UniProtKB.
DR GO; GO:0044481; P:envenomation resulting in proteolysis in another organism; IDA: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; Direct protein sequencing; Disulfide bond;
KW Fibrinogenolytic toxin; Glycoprotein; Hemorrhagic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease; Secreted; Signal; Toxin;
KW Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..187
FT /evidence="ECO:0000269|PubMed:17337026"
FT /id="PRO_0000417635"
FT CHAIN 188..611
FT /note="Zinc metalloproteinase-disintegrin-like ohanin"
FT /id="PRO_0000417636"
FT DOMAIN 198..393
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 401..487
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 465..467
FT /note="D/ECD-tripeptide"
FT ACT_SITE 333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 307..388
FT /evidence="ECO:0000250"
FT DISULFID 347..372
FT /evidence="ECO:0000250"
FT DISULFID 349..354
FT /evidence="ECO:0000250"
FT DISULFID 404..433
FT /evidence="ECO:0000250"
FT DISULFID 415..428
FT /evidence="ECO:0000250"
FT DISULFID 417..423
FT /evidence="ECO:0000250"
FT DISULFID 427..450
FT /evidence="ECO:0000250"
FT DISULFID 441..447
FT /evidence="ECO:0000250"
FT DISULFID 446..472
FT /evidence="ECO:0000250"
FT DISULFID 459..479
FT /evidence="ECO:0000250"
FT DISULFID 466..498
FT /evidence="ECO:0000250"
FT DISULFID 491..503
FT /evidence="ECO:0000250"
FT DISULFID 510..560
FT /evidence="ECO:0000250"
FT DISULFID 525..578
FT /evidence="ECO:0000250"
FT DISULFID 538..548
FT /evidence="ECO:0000250"
FT DISULFID 555..603
FT /evidence="ECO:0000250"
FT DISULFID 597..608
FT /evidence="ECO:0000250"
SQ SEQUENCE 611 AA; 69049 MW; 4B91BAE3457FCCA4 CRC64;
MIQVLLVTIC LVVFPYQGSS IILESGKVND YEVVYPQKIP VLPKSKIQRR EQKMYEDTMK
YEFKVNGEPV VLHLERNKEL FSKDYTETHY SPDGREITTS PPVEDHCYYH GYIQSDIDST
AILNACNGLK GYFRHHGEAY HIEPLKFSDS EAHAVYKYEN IEKEDETPKI CGVKHSTWES
DEPIEKISQK KDFLEEKKYL ELYIVADYVM FRKYGRNVTT IRMRVFDMVN YITVVYKALN
IHVALIGFEI WSLKDKFVIN ASTKNNLLHF SIWRSTVLRK RNDNAQLLTG VDLNGYTLGS
AYLKAMCDVL QSVGIVQDYS KSPYLVGAAM AHEIGHNLGM EHDTKTCSCM RGNCIMSPEE
EGSDFPMEFS SCSLYDFQNY MLTDTPQCLI NKPSNTSIIK NAVCGNYVEE EGEECDCGSP
EQCENNCCEA ATCKLKPGAK CAKGACCKKC QFKKAGAECR AARNECDLPE FCIGQSAECP
MDRFHKNGHS CQNDQGYCFR GYCPTLAKQC ITLWGSDAKV APDECFQNNT NGNEYDYCKK
TNNVIIPCKP TDVKCGRLYC TGGTENPSEG EKISSDPCKA SYSEIEDIGM VDHRTKCGEK
MVCSDGKCIP L
