VM3H_GLOHA
ID VM3H_GLOHA Reviewed; 212 AA.
AC Q90Y44;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Disintegrin-like halysetin;
OS Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX NCBI_TaxID=8714;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-10 AND 207-212, FUNCTION,
RP AND MASS SPECTROMETRY.
RC TISSUE=Venom gland;
RX PubMed=11185525; DOI=10.1006/bbrc.2000.3724;
RA Liu J.W., Du X.Y., Liu P., Chen X., Xu J.M., Wu X.F., Zhou Y.C.;
RT "Purification, characterization, and cDNA sequence of halysetin, a
RT disintegrin-like/cysteine-rich protein from the venom of Agkistrodon halys
RT Pallas.";
RL Biochem. Biophys. Res. Commun. 278:112-118(2000).
CC -!- FUNCTION: Inhibits human platelet aggregation stimulated by collagen
CC with an IC(50) of 420 nM. {ECO:0000269|PubMed:11185525}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=23168; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:11185525};
CC -!- MISCELLANEOUS: Does not inhibit platelet aggregation stimulated by ADP.
CC {ECO:0000305|PubMed:11185525}.
CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIb sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: The complete sequence contains a signal peptide, a propeptide
CC domain, and a proteinase domain at the N-terminus. {ECO:0000305}.
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DR EMBL; AF284093; AAK82974.1; -; mRNA.
DR AlphaFoldDB; Q90Y44; -.
DR SMR; Q90Y44; -.
DR MEROPS; M12.022; -.
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; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
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..212
FT /note="Disintegrin-like halysetin"
FT /id="PRO_0000424625"
FT DOMAIN 4..90
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 68..70
FT /note="D/ECD-tripeptide"
FT DISULFID 7..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 18..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 62..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 69..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 101..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 113..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 151..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 163..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 200..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 212 AA; 23102 MW; 4D5D738AC862CC07 CRC64;
IVSPPVCGNE LLEVGEECDC GTPENCQNEC CDAATCKLKS GSQCGHGDCC EQCKFSKSGT
ECRESMSECD PAEHCTGQSS ECPADVFHKN GQPCLDNYGY CYNGNCPIMY HQCYALWGAD
VYEAEDSCFE SNTKGNYYGY CRKENGIKIP CAPEDVKCGR LYCKDNSPGQ NNPCKMFYSN
EDEHKGMVLP GTKCGDGKVC SNGHCVDVAT AY
