ID   SLB1_DEIAC              Reviewed;         146 AA.
AC   Q8AYA4;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Snaclec agglucetin subunit beta-1;
DE   Flags: Precursor;
OS   Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX   NCBI_TaxID=36307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=12958616; DOI=10.1160/th03-02-0072;
RA   Wang W.J., Ling Q.D., Liau M.Y., Huang T.F.;
RT   "A tetrameric glycoprotein Ib-binding protein, agglucetin, from Formosan
RT   pit viper: structure and interaction with human platelets.";
RL   Thromb. Haemost. 90:465-475(2003).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=11686327;
RA   Wang W.J., Huang T.F.;
RT   "A novel tetrameric venom protein, agglucetin from Agkistrodon acutus, acts
RT   as a glycoprotein Ib agonist.";
RL   Thromb. Haemost. 86:1077-1086(2001).
RN   [3]
RP   FUNCTION.
RX   PubMed=18312855; DOI=10.1016/j.bbrc.2008.02.091;
RA   Wang W.J.;
RT   "Agglucetin, a tetrameric C-type lectin-like venom protein, regulates
RT   endothelial cell survival and promotes angiogenesis by activating integrin
RT   alphavbeta3 signaling.";
RL   Biochem. Biophys. Res. Commun. 369:753-760(2008).
CC   -!- FUNCTION: Agglucetin specifically causes platelet aggregation and
CC       surface exposure of integrin alpha-IIb/beta-3 with a GPIb-(GP1BA-)
CC       dependent manner in washed platelets. It binds to human platelets in a
CC       saturable manner, and its binding is specifically blocked by anti-GP Ib
CC       mAb. It regulates endothelial cell survival and promotes angiogenesis
CC       by activating integrin alpha-v/beta-3 signaling through
CC       FAK/phosphatidylinositol 3-kinase (PI3K)/Akt pathway.
CC       {ECO:0000269|PubMed:11686327, ECO:0000269|PubMed:18312855}.
CC   -!- SUBUNIT: Heterotetramer of the subunits alpha-1, alpha-2, beta-1 and
CC       beta-2; disulfide-linked. {ECO:0000269|PubMed:11686327}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the snaclec family. {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   EMBL; AF540647; AAN23126.1; -; mRNA.
DR   AlphaFoldDB; Q8AYA4; -.
DR   SMR; Q8AYA4; -.
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 activating toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT   CHAIN           24..146
FT                   /note="Snaclec agglucetin subunit beta-1"
FT                   /id="PRO_5000064017"
FT   DOMAIN          32..143
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        25..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        53..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        98
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        119..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   146 AA;  16728 MW;  2342BAE38EB0CCB9 CRC64;
     MGRVIFVSFG LLVVFLSLSG TAADCPSEWS SYEGHCYKAF KQSKTWADAE KFCTQQHKGS
     HLASFHSSEE ADFVVTLTTP SLKTDLVWIG LKNIWNGCYW KWSDGTKLDY KDWREQFECL
     VSRTVNNEWL SMDCGTTYSF VCKFQA