ID   SLA1_DEIAC              Reviewed;         154 AA.
AC   Q8JIV9;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Snaclec agglucetin subunit alpha-1;
DE   AltName: Full=Agkisacucetin subunit alpha;
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;
RA   Yu H., Xiang K., Wang Y., Liu J.;
RT   "Member of C-type lectin family from Deinagkistrodon acutus.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
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   [4]
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).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 24-154, AND DISULFIDE BONDS.
RX   PubMed=22447656; DOI=10.1002/prot.24060;
RA   Gao Y., Ge H., Chen H., Li H., Liu Y., Chen L., Li X., Liu J., Niu L.,
RA   Teng M.;
RT   "Crystal structure of agkisacucetin, a Gpib-binding snake C-type lectin
RT   that inhibits platelet adhesion and aggregation.";
RL   Proteins 80:1707-1711(2012).
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       ECO:0000269|PubMed:22447656}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
CC   -!- CAUTION: PubMed:22447656 describes a heterodimeric snaclec (named
CC       agkisacucetin) that is presented as being another protein than
CC       agglucetin, despite the very high sequence similarity. Agkisacucetin is
CC       described as an inhibitor of platelet aggregation, but no experimental
CC       data or cited references support this description. In addition,
CC       according to PubMed:22447656, agkisacucetin cannot be tetrameric,
CC       because cysteine residues are missing. However, non-covalently linked
CC       tetramers are found in snaclecs, as exemplified by rhodocetin.
CC       {ECO:0000305}.
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DR   EMBL; AY091759; AAM22787.1; -; mRNA.
DR   EMBL; AF540645; AAN23124.1; -; mRNA.
DR   PDB; 3UBU; X-ray; 1.91 A; A=24-154.
DR   PDB; 6XFQ; X-ray; 3.30 A; A=1-154.
DR   PDBsum; 3UBU; -.
DR   PDBsum; 6XFQ; -.
DR   AlphaFoldDB; Q8JIV9; -.
DR   SMR; Q8JIV9; -.
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   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hemostasis impairing toxin; Platelet aggregation activating toxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT   CHAIN           24..154
FT                   /note="Snaclec agglucetin subunit alpha-1"
FT                   /id="PRO_0000355233"
FT   DOMAIN          34..151
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:22447656"
FT   DISULFID        55..150
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:22447656"
FT   DISULFID        102
FT                   /note="Interchain (with C-100 in subunit beta-2)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:22447656"
FT   DISULFID        125..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT                   ECO:0000269|PubMed:22447656"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:3UBU"
FT   STRAND          37..46
FT                   /evidence="ECO:0007829|PDB:3UBU"
FT   HELIX           48..56
FT                   /evidence="ECO:0007829|PDB:3UBU"
FT   HELIX           70..82
FT                   /evidence="ECO:0007829|PDB:3UBU"
FT   TURN            83..85
FT                   /evidence="ECO:0007829|PDB:6XFQ"
FT   STRAND          89..96
FT                   /evidence="ECO:0007829|PDB:3UBU"
FT   STRAND          98..102
FT                   /evidence="ECO:0007829|PDB:3UBU"
FT   TURN            119..121
FT                   /evidence="ECO:0007829|PDB:3UBU"
FT   STRAND          125..128
FT                   /evidence="ECO:0007829|PDB:3UBU"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:3UBU"
FT   STRAND          136..140
FT                   /evidence="ECO:0007829|PDB:3UBU"
FT   STRAND          146..152
FT                   /evidence="ECO:0007829|PDB:3UBU"
SQ   SEQUENCE   154 AA;  17318 MW;  AA08E518501BECC7 CRC64;
     MGRFIFVSFG LLVVFLSLSG TGADVDCLPG WSAYDQSCYR VFKLLKTWDD AEKFCTERPK
     GGHLVSIESA GERDFVAQLV SENKQTDNVW LGLKIQSKGQ QCSTEWTDGS SVSYENFSEY
     QSKKCFVLEK NTGFRTWLNL NCGSEYAFVC KSPP