VM2RH_CALRH
ID VM2RH_CALRH Reviewed; 478 AA.
AC P30403; P17494;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Zinc metalloproteinase/disintegrin;
DE Contains:
DE RecName: Full=Snake venom metalloproteinase rhodostoxin {ECO:0000303|PubMed:8561498};
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=Hemorrhagic protein {ECO:0000303|PubMed:8561498};
DE Contains:
DE RecName: Full=Disintegrin rhodostomin {ECO:0000303|PubMed:1755841, ECO:0000303|PubMed:7916592};
DE Short=RHO;
DE Short=RHOD;
DE AltName: Full=Disintegrin kistrin {ECO:0000303|PubMed:1734953};
DE AltName: Full=Platelet aggregation activation inhibitor;
DE Flags: Precursor;
OS Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Calloselasma.
OX NCBI_TaxID=8717;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=7916635; DOI=10.1016/0167-4781(93)90190-o;
RA Au L.-C.;
RT "Nucleotide sequence of a full-length cDNA encoding a common precursor of
RT platelet aggregation inhibitor and hemorrhagic protein from Calloselasma
RT rhodostoma venom.";
RL Biochim. Biophys. Acta 1173:243-245(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 77-478.
RC TISSUE=Venom gland;
RX PubMed=1755841; DOI=10.1016/0006-291x(91)91230-a;
RA Au L.-C., Huang Y.-B., Huang T.-F., Teh G.-W., Lin H.-H., Choo K.-B.;
RT "A common precursor for a putative hemorrhagic protein and rhodostomin, a
RT platelet aggregation inhibitor of the venom of Calloselasma rhodostoma:
RT molecular cloning and sequence analysis.";
RL Biochem. Biophys. Res. Commun. 181:585-593(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 408-475.
RC TISSUE=Venom gland;
RX PubMed=7916592; DOI=10.1006/bbrc.1993.1037;
RA Chang H.H., Hu S.T., Huang T.-F., Chen S.H., Lee Y.H., Lo S.J.;
RT "Rhodostomin, an RGD-containing peptide expressed from a synthetic gene in
RT Escherichia coli, facilitates the attachment of human hepatoma cells.";
RL Biochem. Biophys. Res. Commun. 190:242-249(1993).
RN [4]
RP PROTEIN SEQUENCE OF 189-391, DISULFIDE BONDS, GLYCOSYLATION AT ASN-279 AND
RP ASN-369, GLYCAN STRUCTURE, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8561498; DOI=10.1006/abbi.1996.0025;
RA Chung M.C., Ponnudurai G., Kataoka M., Shimizu S., Tan N.H.;
RT "Structural studies of a major hemorrhagin (rhodostoxin) from the venom of
RT Calloselasma rhodostoma (Malayan pit viper).";
RL Arch. Biochem. Biophys. 325:199-208(1996).
RN [5]
RP PROTEIN SEQUENCE OF 408-475, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=2236100; DOI=10.3181/00379727-195-43129b;
RA Gould R.J., Polokoff M.A., Friedman P.A., Huang T.-F., Holt J.C.,
RA Cook J.J., Niecviarowski S.;
RT "Disintegrins: a family of integrin inhibitory proteins from viper
RT venoms.";
RL Proc. Soc. Exp. Biol. Med. 195:168-171(1990).
RN [6]
RP PROTEIN SEQUENCE OF 408-475, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=2320569; DOI=10.1073/pnas.87.7.2471;
RA Dennis M.S., Henzel W.J., Pitti R.M., Lipari M.T., Napier M.A.,
RA Deisher T.A., Bunting S., Lazarus R.A.;
RT "Platelet glycoprotein IIb-IIIa protein antagonists from snake venoms:
RT evidence for a family of platelet-aggregation inhibitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2471-2475(1990).
RN [7]
RP STRUCTURE BY NMR OF 408-475.
RX PubMed=8418848; DOI=10.1021/bi00052a036;
RA Adler M., Carter P., Lazarus R.A., Wagner G.;
RT "Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR,
RT chemical analysis, and structure calculations.";
RL Biochemistry 32:282-289(1993).
RN [8] {ECO:0000312|PDB:1N4Y}
RP STRUCTURE BY NMR OF 408-475, AND DISULFIDE BONDS.
RX PubMed=1862345; DOI=10.1126/science.1862345;
RA Adler M., Lazarus R.A., Dennis M.S., Wagner G.;
RT "Solution structure of kistrin, a potent platelet aggregation inhibitor and
RT GP IIb-IIIa antagonist.";
RL Science 253:445-448(1991).
RN [9]
RP STRUCTURE BY NMR OF 408-475.
RX PubMed=1734953; DOI=10.1021/bi00119a011;
RA Adler M., Wagner G.;
RT "Sequential 1H NMR assignments of kistrin, a potent platelet aggregation
RT inhibitor and glycoprotein IIb-IIIa antagonist.";
RL Biochemistry 31:1031-1039(1992).
CC -!- FUNCTION: [Snake venom metalloproteinase rhodostoxin]: Impairs
CC hemostasis in the envenomed animal. {ECO:0000250}.
CC -!- FUNCTION: [Disintegrin rhodostomin]: Inhibits platelet aggregation
CC induced by ADP, thrombin, platelet-activating factor and collagen. Acts
CC by inhibiting fibrinogen interaction with platelet receptors alpha-
CC IIb/beta-3 (ITGA2B/ITGB3).
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: Monomeric (disintegrin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Snake venom metalloproteinase rhodostoxin]:
CC Secreted {ECO:0000269|PubMed:2236100, ECO:0000269|PubMed:2320569,
CC ECO:0000269|PubMed:8561498}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:2236100, ECO:0000305|PubMed:2320569,
CC ECO:0000305|PubMed:8561498}.
CC -!- PTM: Glycans are composed of 4 GlcNAc, 3 Man, 2 Gal, 2 NeuAC and 1 Fuc
CC residue. {ECO:0000269|PubMed:8561498}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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DR EMBL; L08780; AAA49196.1; -; mRNA.
DR PIR; S33792; JQ1301.
DR PDB; 1N4Y; NMR; -; A=408-475.
DR PDB; 1Q7I; NMR; -; A=408-475.
DR PDB; 1Q7J; NMR; -; A=408-475.
DR PDB; 2LJV; NMR; -; A=408-475.
DR PDB; 2M75; NMR; -; A=408-475.
DR PDB; 2M7F; NMR; -; A=408-478.
DR PDB; 2M7H; NMR; -; A=408-478.
DR PDB; 2PJF; NMR; -; A=408-475.
DR PDB; 2PJG; NMR; -; A=408-475.
DR PDB; 2PJI; NMR; -; A=408-475.
DR PDB; 3UCI; X-ray; 1.35 A; A=408-475.
DR PDB; 4M4C; X-ray; 1.80 A; A/B/C/D=408-475.
DR PDB; 4R5R; X-ray; 0.96 A; A/B=408-475.
DR PDB; 4R5U; X-ray; 1.81 A; A/B=408-475.
DR PDB; 4RQG; X-ray; 1.66 A; A/B=408-475.
DR PDBsum; 1N4Y; -.
DR PDBsum; 1Q7I; -.
DR PDBsum; 1Q7J; -.
DR PDBsum; 2LJV; -.
DR PDBsum; 2M75; -.
DR PDBsum; 2M7F; -.
DR PDBsum; 2M7H; -.
DR PDBsum; 2PJF; -.
DR PDBsum; 2PJG; -.
DR PDBsum; 2PJI; -.
DR PDBsum; 3UCI; -.
DR PDBsum; 4M4C; -.
DR PDBsum; 4R5R; -.
DR PDBsum; 4R5U; -.
DR PDBsum; 4RQG; -.
DR AlphaFoldDB; P30403; -.
DR BMRB; P30403; -.
DR SMR; P30403; -.
DR MEROPS; M12.161; -.
DR iPTMnet; P30403; -.
DR EvolutionaryTrace; P30403; -.
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; 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; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
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; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Platelet aggregation inhibiting toxin;
KW Protease; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..188
FT /evidence="ECO:0000305|PubMed:8561498"
FT /id="PRO_0000028956"
FT CHAIN 189..391
FT /note="Snake venom metalloproteinase rhodostoxin"
FT /evidence="ECO:0000269|PubMed:8561498"
FT /id="PRO_0000028957"
FT PROPEP 392..407
FT /id="PRO_0000028958"
FT CHAIN 408..475
FT /note="Disintegrin rhodostomin"
FT /evidence="ECO:0000269|PubMed:2236100,
FT ECO:0000269|PubMed:2320569"
FT /id="PRO_0000028959"
FT PROPEP 476..478
FT /id="PRO_0000028960"
FT DOMAIN 194..391
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 397..478
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 456..458
FT /note="Cell attachment site"
FT ACT_SITE 331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:8561498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:8561498"
FT DISULFID 207..248
FT DISULFID 305..386
FT DISULFID 345..370
FT /evidence="ECO:0000305"
FT DISULFID 347..353
FT /evidence="ECO:0000305"
FT DISULFID 411..426
FT /evidence="ECO:0000269|PubMed:1862345,
FT ECO:0007744|PDB:1N4Y"
FT DISULFID 413..421
FT /evidence="ECO:0000269|PubMed:1862345,
FT ECO:0007744|PDB:1N4Y"
FT DISULFID 420..443
FT /evidence="ECO:0000269|PubMed:1862345,
FT ECO:0007744|PDB:1N4Y"
FT DISULFID 434..440
FT /evidence="ECO:0000269|PubMed:1862345,
FT ECO:0007744|PDB:1N4Y"
FT DISULFID 439..464
FT /evidence="ECO:0000269|PubMed:1862345,
FT ECO:0007744|PDB:1N4Y"
FT DISULFID 452..471
FT /evidence="ECO:0000269|PubMed:1862345,
FT ECO:0007744|PDB:1N4Y"
FT CONFLICT 287
FT /note="M -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:3UCI"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:4RQG"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:1N4Y"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:4R5R"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:4R5R"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:2PJI"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:4R5R"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:1Q7I"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:4R5R"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:4R5R"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:4M4C"
SQ 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
