SLB2_DEIAC
ID SLB2_DEIAC Reviewed; 149 AA.
AC Q8AYA3; Q8JIW2; Q8UVC7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Snaclec agglucetin subunit beta-2;
DE AltName: Full=Antithrombin 1 chain B;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM22783.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF463521; AAL66390.1; -; mRNA.
DR EMBL; AY091754; AAM22783.1; ALT_FRAME; mRNA.
DR EMBL; AF540648; AAN23127.1; -; mRNA.
DR PDB; 3UBU; X-ray; 1.91 A; B=24-149.
DR PDB; 6XFQ; X-ray; 3.30 A; B=1-149.
DR PDBsum; 3UBU; -.
DR PDBsum; 6XFQ; -.
DR AlphaFoldDB; Q8AYA3; -.
DR SMR; Q8AYA3; -.
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;
KW Hemostasis impairing toxin; Platelet aggregation activating toxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT CHAIN 24..149
FT /note="Snaclec agglucetin subunit beta-2"
FT /id="PRO_5000064018"
FT DOMAIN 34..146
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 27..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:22447656"
FT DISULFID 55..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:22447656"
FT DISULFID 100
FT /note="Interchain (with C-102 in subunit alpha-1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:22447656"
FT DISULFID 121..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:22447656"
FT CONFLICT 114
FT /note="A -> S (in Ref. 1; AAL66390/AAM22783)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="T -> I (in Ref. 1; AAM22783)"
FT /evidence="ECO:0000305"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:3UBU"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:3UBU"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:3UBU"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:3UBU"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:3UBU"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:3UBU"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:3UBU"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:3UBU"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:3UBU"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6XFQ"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:3UBU"
SQ SEQUENCE 149 AA; 17234 MW; 620C9D59AE92965A CRC64;
MGRFIFVSFG LLVVFLSLRG TGAGFCCPLR WSSYEGHCYL VVKEKKTWDD AEKFCTEQRK
GGHLVSVHSR EEADFLVHLA YPILDLSLIW MGLSNMWNDC KREWSDGTKL DFKAWAKTSD
CLIGKTDGDN QWLNMDCSKK HYFVCKFKL
