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Zinc metalloproteinase/disintegrin [Cleaved into: Snake venom metalloproteinase rhodostoxin (SVMP) (EC 3.4.24.-) (Hemorrhagic protein); Disintegrin rhodostomin (RHO) (RHOD) (Disintegrin kistrin) (Platelet aggregation activation inhibitor)]

 VM2RH_CALRH             Reviewed;         478 AA.
P30403; P17494;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
22-NOV-2017, entry version 132.
RecName: Full=Zinc metalloproteinase/disintegrin;
Contains:
RecName: Full=Snake venom metalloproteinase rhodostoxin;
Short=SVMP;
EC=3.4.24.-;
AltName: Full=Hemorrhagic protein;
Contains:
RecName: Full=Disintegrin rhodostomin;
Short=RHO;
Short=RHOD;
AltName: Full=Disintegrin kistrin;
AltName: Full=Platelet aggregation activation inhibitor;
Flags: Precursor;
Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae;
Calloselasma.
NCBI_TaxID=8717;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom gland;
PubMed=7916635; DOI=10.1016/0167-4781(93)90190-O;
Au L.-C.;
"Nucleotide sequence of a full-length cDNA encoding a common precursor
of platelet aggregation inhibitor and hemorrhagic protein from
Calloselasma rhodostoma venom.";
Biochim. Biophys. Acta 1173:243-245(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 77-478.
TISSUE=Venom gland;
PubMed=1755841; DOI=10.1016/0006-291X(91)91230-A;
Au L.-C., Huang Y.-B., Huang T.-F., Teh G.-W., Lin H.-H., Choo K.-B.;
"A common precursor for a putative hemorrhagic protein and
rhodostomin, a platelet aggregation inhibitor of the venom of
Calloselasma rhodostoma: molecular cloning and sequence analysis.";
Biochem. Biophys. Res. Commun. 181:585-593(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 408-475.
TISSUE=Venom gland;
PubMed=7916592; DOI=10.1006/bbrc.1993.1037;
Chang H.H., Hu S.T., Huang T.-F., Chen S.H., Lee Y.H., Lo S.J.;
"Rhodostomin, an RGD-containing peptide expressed from a synthetic
gene in Escherichia coli, facilitates the attachment of human hepatoma
cells.";
Biochem. Biophys. Res. Commun. 190:242-249(1993).
[4]
PROTEIN SEQUENCE OF 189-391, DISULFIDE BONDS, GLYCOSYLATION AT ASN-279
AND ASN-369, GLYCAN STRUCTURE, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Venom;
PubMed=8561498; DOI=10.1006/abbi.1996.0025;
Chung M.C., Ponnudurai G., Kataoka M., Shimizu S., Tan N.H.;
"Structural studies of a major hemorrhagin (rhodostoxin) from the
venom of Calloselasma rhodostoma (Malayan pit viper).";
Arch. Biochem. Biophys. 325:199-208(1996).
[5]
PROTEIN SEQUENCE OF 408-475.
TISSUE=Venom;
PubMed=2236100; DOI=10.3181/00379727-195-43129B;
Gould R.J., Polokoff M.A., Friedman P.A., Huang T.-F., Holt J.C.,
Cook J.J., Niecviarowski S.;
"Disintegrins: a family of integrin inhibitory proteins from viper
venoms.";
Proc. Soc. Exp. Biol. Med. 195:168-171(1990).
[6]
PROTEIN SEQUENCE OF 408-475.
TISSUE=Venom;
PubMed=2320569; DOI=10.1073/pnas.87.7.2471;
Dennis M.S., Henzel W.J., Pitti R.M., Lipari M.T., Napier M.A.,
Deisher T.A., Bunting S., Lazarus R.A.;
"Platelet glycoprotein IIb-IIIa protein antagonists from snake venoms:
evidence for a family of platelet-aggregation inhibitors.";
Proc. Natl. Acad. Sci. U.S.A. 87:2471-2475(1990).
[7]
STRUCTURE BY NMR OF 408-475, AND DISULFIDE BONDS.
PubMed=8418848; DOI=10.1021/bi00052a036;
Adler M., Carter P., Lazarus R.A., Wagner G.;
"Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using
NMR, chemical analysis, and structure calculations.";
Biochemistry 32:282-289(1993).
[8]
STRUCTURE BY NMR OF 408-475.
PubMed=1862345; DOI=10.1126/science.1862345;
Adler M., Lazarus R.A., Dennis M.S., Wagner G.;
"Solution structure of kistrin, a potent platelet aggregation
inhibitor and GP IIb-IIIa antagonist.";
Science 253:445-448(1991).
[9]
STRUCTURE BY NMR OF 408-475.
PubMed=1734953; DOI=10.1021/bi00119a011;
Adler M., Wagner G.;
"Sequential 1H NMR assignments of kistrin, a potent platelet
aggregation inhibitor and glycoprotein IIb-IIIa antagonist.";
Biochemistry 31:1031-1039(1992).
-!- FUNCTION: Snake venom metalloproteinase rhodostoxin: impairs
hemostasis in the envenomed animal. {ECO:0000250}.
-!- FUNCTION: Disintegrin rhodostomin: inhibit platelet aggregation
induced by ADP, thrombin, platelet-activating factor and collagen.
Acts by inhibiting fibrinogen interaction with platelet receptors
alpha-IIb/beta-3 (ITGA2B/ITGB3).
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Monomeric (disintegrin). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- PTM: Glycans are composed of 4 GlcNAc, 3 Man, 2 Gal, 2 NeuAC and 1
Fuc residue.
-!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
P-II subfamily. P-IIa sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L08780; AAA49196.1; -; mRNA.
PIR; S33792; JQ1301.
PDB; 1N4Y; NMR; -; A=408-475.
PDB; 1Q7I; NMR; -; A=408-475.
PDB; 1Q7J; NMR; -; A=408-475.
PDB; 2LJV; NMR; -; A=408-475.
PDB; 2M75; NMR; -; A=408-475.
PDB; 2M7F; NMR; -; A=408-478.
PDB; 2M7H; NMR; -; A=408-478.
PDB; 2PJF; NMR; -; A=408-475.
PDB; 2PJG; NMR; -; A=408-475.
PDB; 2PJI; NMR; -; A=408-475.
PDB; 3UCI; X-ray; 1.35 A; A=408-475.
PDB; 4M4C; X-ray; 1.80 A; A/B/C/D=408-475.
PDB; 4R5R; X-ray; 0.96 A; A/B=408-475.
PDB; 4R5U; X-ray; 1.81 A; A/B=408-475.
PDB; 4RQG; X-ray; 1.66 A; A/B=408-475.
PDBsum; 1N4Y; -.
PDBsum; 1Q7I; -.
PDBsum; 1Q7J; -.
PDBsum; 2LJV; -.
PDBsum; 2M75; -.
PDBsum; 2M7F; -.
PDBsum; 2M7H; -.
PDBsum; 2PJF; -.
PDBsum; 2PJG; -.
PDBsum; 2PJI; -.
PDBsum; 3UCI; -.
PDBsum; 4M4C; -.
PDBsum; 4R5R; -.
PDBsum; 4R5U; -.
PDBsum; 4RQG; -.
ProteinModelPortal; P30403; -.
SMR; P30403; -.
MEROPS; M12.161; -.
iPTMnet; P30403; -.
HOVERGEN; HBG006978; -.
EvolutionaryTrace; P30403; -.
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;
3D-structure; Cell adhesion impairing toxin;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
Platelet aggregation inhibiting toxin; Protease; Secreted; Signal;
Toxin; Zinc; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 188 {ECO:0000269|PubMed:8561498}.
/FTId=PRO_0000028956.
CHAIN 189 391 Snake venom metalloproteinase
rhodostoxin.
/FTId=PRO_0000028957.
PROPEP 392 407
/FTId=PRO_0000028958.
CHAIN 408 475 Disintegrin rhodostomin.
/FTId=PRO_0000028959.
PROPEP 476 478
/FTId=PRO_0000028960.
DOMAIN 194 391 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 397 478 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
MOTIF 456 458 Cell attachment site.
ACT_SITE 331 331 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 330 330 Zinc; catalytic. {ECO:0000305}.
METAL 334 334 Zinc; catalytic. {ECO:0000305}.
METAL 340 340 Zinc; catalytic. {ECO:0000305}.
CARBOHYD 279 279 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:8561498}.
CARBOHYD 369 369 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:8561498}.
DISULFID 207 248
DISULFID 305 386
DISULFID 345 370 {ECO:0000305}.
DISULFID 347 353 {ECO:0000305}.
DISULFID 411 426
DISULFID 413 421
DISULFID 420 443
DISULFID 434 440
DISULFID 439 464
DISULFID 452 471
CONFLICT 287 287 M -> T (in Ref. 4; AA sequence).
{ECO:0000305}.
HELIX 408 410 {ECO:0000244|PDB:3UCI}.
STRAND 412 414 {ECO:0000244|PDB:4RQG}.
STRAND 419 421 {ECO:0000244|PDB:1N4Y}.
TURN 423 425 {ECO:0000244|PDB:4R5R}.
STRAND 426 428 {ECO:0000244|PDB:4R5R}.
STRAND 429 431 {ECO:0000244|PDB:2PJI}.
STRAND 435 437 {ECO:0000244|PDB:4R5R}.
STRAND 438 441 {ECO:0000244|PDB:1Q7I}.
STRAND 451 453 {ECO:0000244|PDB:4R5R}.
STRAND 456 458 {ECO:0000244|PDB:4R5R}.
STRAND 461 463 {ECO:0000244|PDB:4M4C}.
SEQUENCE 478 AA; 54006 MW; 6490A2B171D3A830 CRC64;
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKVI ALSEGAAQQK YEDTMQYEFK
VNGEPVVLHL EKNKGLFAKD YSETHYSPDG TRITTYPSVE DHCYYQGRIH NDADSTASIS
ACNGLKGHFK LQGETYFIEP MKLPDSEAHA VFKYENIEKE DESPKMCGVT ETNWESDEPI
KKVSQLNLNH EIKRHVDIVV VVDSRFCTKH SNDLEVIRKF VHEVVNAIIE SYKYMHFGIS
LVNLETWCNG DLINVQEDSY ETLKAFGKWR ESDLIKHVNH SNAQFLMDMK FIKNIIGKAY
LDSICDPERS VGIVQNYHGI TLNVAAIMAH EMGHNLGVRH DGEYCTCYGS SECIMSSHIS
DPPSKYFSNC SYYQFWKYIE NQNPQCILNK PLRTVSIPVS GNEHLEAGKE CDCSSPENPC
CDAATCKLRP GAQCGEGLCC EQCKFSRAGK ICRIPRGDMP DDRCTGQSAD CPRYHSHA


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