SLA2_DEIAC
ID SLA2_DEIAC Reviewed; 158 AA.
AC Q8AYA5; Q8UVC6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Snaclec agglucetin subunit alpha-2;
DE AltName: Full=Antithrombin 1 chain A;
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., Liu J.;
RL Submitted (DEC-2001) 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).
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}.
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DR EMBL; AF463522; AAL66391.1; -; mRNA.
DR EMBL; AF540646; AAN23125.1; -; mRNA.
DR AlphaFoldDB; Q8AYA5; -.
DR SMR; Q8AYA5; -.
DR PRIDE; Q8AYA5; -.
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..158
FT /note="Snaclec agglucetin subunit alpha-2"
FT /id="PRO_5000064016"
FT DOMAIN 34..153
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..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 104
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 127..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 83
FT /note="N -> S (in Ref. 2; AAL66391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 17977 MW; 9D0A9C936ABEA5E4 CRC64;
MGRFIFVSFG LLVVFLSLSG TGADFNCPPG WSAYDQYCYQ VIKEPKNWDD AERFCTEQAD
GGHLVSIESK GERDFVAQLV SQNIESVEDH VWTGLRVQNK EKQCSTEWSD GSSVSYENLL
ELYMRKCGAL ERETGFHKWI NLGCIQLNPF VCKFPPQC
