VM2I2_GLOUS
ID VM2I2_GLOUS Reviewed; 71 AA.
AC Q7LZT4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Disintegrin ussuristatin-2;
DE Short=US-2;
OS Gloydius ussuriensis (Ussuri mamushi) (Gloydius blomhoffii ussuriensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=35671 {ECO:0000312|PIR:A59412};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC TISSUE=Venom {ECO:0000269|PubMed:9880793};
RX PubMed=9880793; DOI=10.1093/oxfordjournals.jbchem.a022264;
RA Oshikawa K., Terada S.;
RT "Ussuristatin 2, a novel KGD-bearing disintegrin from Agkistrodon
RT ussuriensis venom.";
RL J. Biochem. 125:31-35(1999).
CC -!- FUNCTION: Suppress platelet aggregation induced by ADP, collagen,
CC thrombin, and epinephrine (IC(50)=170-330 nM). Also dose-dependently
CC inhibits the adhesion of human melanoma cells to fibrinogen but not to
CC fibronectin. {ECO:0000269|PubMed:9880793}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9880793}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: The disintegrin belongs to the dimeric disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IId sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A59412; A59412.
DR AlphaFoldDB; Q7LZT4; -.
DR SMR; Q7LZT4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR Pfam; PF00200; Disintegrin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW Secreted; Toxin.
FT CHAIN 1..71
FT /note="Disintegrin ussuristatin-2"
FT /id="PRO_0000101781"
FT DOMAIN 1..71
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 51..53
FT /note="Cell attachment site; atypical (KGD)"
FT DISULFID 6..15
FT /evidence="ECO:0000250|UniProtKB:P22828,
FT ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 8..16
FT /evidence="ECO:0000250|UniProtKB:P22828,
FT ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 21..35
FT /evidence="ECO:0000250|UniProtKB:P22828,
FT ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 29..59
FT /evidence="ECO:0000250|UniProtKB:P22828,
FT ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 34..38
FT /evidence="ECO:0000250|UniProtKB:P22828,
FT ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 47..66
FT /evidence="ECO:0000250|UniProtKB:P22828,
FT ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 71 AA; 7455 MW; B62E06326442504A CRC64;
EAGEECDCGA PANPCCDAAT CKLRPGAQCA EGDCCEQCRF VKEGTVCREA KGDWNDDSCT
GQSADCPRNG F
