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Zinc metalloproteinase/disintegrin [Cleaved into: Snake venom metalloproteinase HR2a (SVMP) (EC 3.4.24.53) (Snake venom metalloproteinase HR2b) (Trimerelysin II); Disintegrin flavostatin (Platelet aggregation activation inhibitor)]

 VM2HA_PROFL             Reviewed;         478 AA.
P14530; P80949; Q90W25;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 3.
25-APR-2018, entry version 124.
RecName: Full=Zinc metalloproteinase/disintegrin;
Contains:
RecName: Full=Snake venom metalloproteinase HR2a {ECO:0000303|PubMed:10371209, ECO:0000303|PubMed:2753880};
Short=SVMP;
EC=3.4.24.53;
AltName: Full=Snake venom metalloproteinase HR2b {ECO:0000303|PubMed:7597726};
AltName: Full=Trimerelysin II;
Contains:
RecName: Full=Disintegrin flavostatin {ECO:0000303|PubMed:10371209, ECO:0000303|PubMed:9114455};
AltName: Full=Platelet aggregation activation inhibitor;
Flags: Precursor;
Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
Protobothrops.
NCBI_TaxID=88087;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=10371209; DOI=10.1016/S0014-5793(99)00604-3;
Yamada D., Shin Y., Morita T.;
"Nucleotide sequence of a cDNA encoding a common precursor of
disintegrin flavostatin and hemorrhagic factor HR2a from the venom of
Trimeresurus flavoviridis.";
FEBS Lett. 451:299-302(1999).
[2]
PROTEIN SEQUENCE OF 191-392, DISULFIDE BONDS, PYROGLUTAMATE FORMATION
AT GLN-191, AND VARIANTS OKINAWA HABU 189-GLU--PHE-192 AND ASN-271.
STRAIN=Okinawa habu; TISSUE=Venom;
PubMed=7597726; DOI=10.1016/0041-0101(94)00147-Z;
Iha M., Qi Z.Q., Kannki T., Tomihara Y., Yonaha K.;
"The primary structure of a hemorrhagic factor, HR2b, from the venom
of Okinawa habu (Trimeresurus flavoviridis).";
Toxicon 33:229-239(1995).
[3]
PROTEIN SEQUENCE OF 191-392, DISULFIDE BONDS, PYROGLUTAMATE FORMATION
AT GLN-191, AND ABSENCE OF GLYCOSYLATION.
STRAIN=Amami habu; TISSUE=Venom;
PubMed=2753880;
Miyata T., Takeya H., Ozeki Y., Arakawa M., Tokunaga F., Iwanaga S.,
Omori-Satoh T.;
"Primary structure of hemorrhagic protein, HR2a, isolated from the
venom of Trimeresurus flavoviridis.";
J. Biochem. 105:847-853(1989).
[4]
PROTEIN SEQUENCE OF 411-478, AND FUNCTION OF FLAVOSTATIN.
TISSUE=Venom;
PubMed=9114455; DOI=10.1016/S0196-9781(96)00259-8;
Maruyama K., Kawasaki T., Sakai Y., Taniuchi Y., Shimizu M.,
Kawashima H., Takenaka T.;
"Isolation and amino acid sequence of flavostatin, a novel disintegrin
from the venom of Trimeresurus flavoviridis.";
Peptides 18:73-78(1997).
-!- FUNCTION: Snake venom metalloproteinase HR2a: zinc protease that
induces hemorrhage. {ECO:0000269|PubMed:9114455}.
-!- FUNCTION: Disintegrin flavostatin: inhibits platelet aggregation
induced by ADP, thrombin, and collagen. Acts by inhibiting
fibrinogen interaction with platelet receptors GPIIb/GPIIIa
(ITGA2B/ITGB3). {ECO:0000269|PubMed:9114455}.
-!- CATALYTIC ACTIVITY: Cleavage of 3-Asn-|-Gln-4, 10-His-|-Leu-11 and
14-Ala-|-Leu-15 in the insulin B chain, and the bond Z-Gly-Pro-|-
Leu-Gly-Pro in a small molecule substrate of microbial
collagenase.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- PTM: Not N-glycosylated. {ECO:0000269|PubMed:2753880}.
-!- MISCELLANEOUS: The disintegrin belongs to the medium disintegrin
subfamily.
-!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
P-II subfamily. P-IIa sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY037808; AAK68850.1; -; mRNA.
PIR; JX0074; HYTVH2.
ProteinModelPortal; P14530; -.
SMR; P14530; -.
MEROPS; M12.156; -.
HOVERGEN; HBG006978; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
CDD; cd04269; ZnMc_adamalysin_II_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR018358; Disintegrin_CS.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR034027; Reprolysin_adamalysin.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
PRINTS; PR00289; DISINTEGRIN.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS00427; DISINTEGRIN_1; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hemorrhagic toxin;
Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
Platelet aggregation inhibiting toxin; Protease;
Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Zinc; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 190 {ECO:0000305}.
/FTId=PRO_0000029013.
CHAIN 191 392 Snake venom metalloproteinase HR2a.
{ECO:0000269|PubMed:2753880}.
/FTId=PRO_0000029014.
PROPEP 393 410 {ECO:0000305}.
/FTId=PRO_0000029015.
CHAIN 411 478 Disintegrin flavostatin.
{ECO:0000269|PubMed:9114455}.
/FTId=PRO_0000029016.
DOMAIN 197 392 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 400 478 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
MOTIF 459 461 Cell attachment site.
ACT_SITE 334 334
METAL 200 200 Calcium. {ECO:0000250}.
METAL 284 284 Calcium. {ECO:0000250}.
METAL 333 333 Zinc; catalytic.
METAL 337 337 Zinc; catalytic.
METAL 343 343 Zinc; catalytic.
METAL 387 387 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 390 390 Calcium. {ECO:0000250}.
SITE 293 293 Not glycosylated.
{ECO:0000269|PubMed:2753880}.
MOD_RES 191 191 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:2753880,
ECO:0000269|PubMed:7597726}.
DISULFID 308 387 {ECO:0000269|PubMed:2753880,
ECO:0000269|PubMed:7597726}.
DISULFID 349 371 {ECO:0000269|PubMed:2753880,
ECO:0000269|PubMed:7597726}.
DISULFID 351 354 {ECO:0000269|PubMed:2753880,
ECO:0000269|PubMed:7597726}.
DISULFID 414 423 {ECO:0000250}.
DISULFID 416 424 {ECO:0000250}.
DISULFID 429 443 {ECO:0000250}.
DISULFID 437 467 {ECO:0000250}.
DISULFID 442 446 {ECO:0000250}.
DISULFID 455 474 {ECO:0000250}.
VARIANT 189 192 PEQQ -> EQRF (in Okinawa habu).
{ECO:0000269|PubMed:7597726}.
VARIANT 192 192 Missing (in 50% of the chains).
VARIANT 271 271 D -> N (in Okinawa habu).
{ECO:0000269|PubMed:7597726}.
SEQUENCE 478 AA; 53646 MW; 6C8FF7F184F1B85F CRC64;
MIEVLLVTIC LAVFPYPGSS IILESGNVDD YEVVYPQKLT ALPKGAVQPK YEDAMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTYPSVE DHCYYHGRIQ NDADSTASIS
ACDGLKGYFK LQGETYLIEP LELSDSEAHA VFKYENVEKE DEAPKMCGVT QNWESDESIK
KASQLYLTPE QQRFPQRYIE LAIVVDHGMY TKYSSNFKKI RKRVHQMVNN INEMYRPLNI
AITLSLLDVW SEKDLITMQA VAPTTARLFG DWRETVLLKQ KDHDHAQLLT DINFTGNTIG
WAYMGGMCNA KNSVGIVKDH SSNVFMVAVT MTHEIGHNLG MEHDDKDKCK CEACIMSAVI
SDKPSKLFSD CSKDYYQTFL TNSKPQCIIN APLRTDTVST PVSGNEFLEA GEECDCGSPS
NPCCDAATCK LRPGAQCADG LCCDQCRFKK KRTICRRARG DNPDDRCTGQ SADCPRNS


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