SLRB_BITRH
ID SLRB_BITRH Reviewed; 150 AA.
AC I7ICN3;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Snaclec rhinocetin subunit beta;
DE AltName: Full=C-type lectin like protein 2;
DE Flags: Precursor;
OS Bitis rhinoceros (West African gaboon viper) (Vipera rhinoceros).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Bitis.
OX NCBI_TaxID=715877;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-33, FUNCTION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=22689571; DOI=10.1074/jbc.m112.381483;
RA Vaiyapuri S., Hutchinson E.G., Ali M.S., Dannoura A., Stanley R.G.,
RA Harrison R.A., Bicknell A.B., Gibbins J.M.;
RT "Rhinocetin, a venom-derived integrin-specific antagonist inhibits
RT collagen-induced platelet and endothelial cell functions.";
RL J. Biol. Chem. 287:26235-26244(2012).
CC -!- FUNCTION: Antagonist of the alpha-2 subunit of the integrin alpha-
CC 2/beta-1 (ITGA2/ITGB1) on human platelets and endothelial cells. This
CC protein inhibits collagen-stimulated activation of human platelets in a
CC dose-dependent manner. In addition, it antagonizes the binding of
CC monoclonal antibodies against the alpha-2 subunit of integrin alpha-
CC 2/beta-1 to platelets and it coimmunoprecipitates with this integrin.
CC {ECO:0000269|PubMed:22689571}.
CC -!- SUBUNIT: Heterodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not block the glycoprotein VI (GP6) and does not
CC inhibit platelet activation induced by ADP-, and thrombin.
CC {ECO:0000305|PubMed:22689571}.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; HE800430; CCH15162.1; -; mRNA.
DR AlphaFoldDB; I7ICN3; -.
DR SMR; I7ICN3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:22689571"
FT CHAIN 24..150
FT /note="Snaclec rhinocetin subunit beta"
FT /id="PRO_0000422546"
FT DOMAIN 34..145
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 27..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 55..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 100
FT /note="Interchain (with C-104 in alpha chain)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 121..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 150 AA; 17726 MW; 9F4469292028136F CRC64;
MGRFIFLSSG LLVVFLSLSG TGADQGCLPD WTLYEGYCYK VFKEKKTWAD AEKFCKEQAN
GGHLVSLQSS EEVDFMVHQT FPILRYDFVW IGLSDFSRDC QWKWSDYSKL FYKAWNNEPN
CFVCKTTDNQ WLRRDCNRQQ YFVCKSRVPR
