ID   SLCB_DEIAC              Reviewed;         146 AA.
AC   Q9DEA1;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Snaclec agkicetin-C subunit beta;
DE   AltName: Full=Antithrombin A subunit 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;
RX   PubMed=10669165;
RA   Chen Y.L., Tsai K.W., Chang T., Hong T.M., Tsai I.H.;
RT   "Glycoprotein Ib-binding protein from the venom of Deinagkistrodon acutus
RT   -- cDNA sequence, functional characterization, and three-dimensional
RT   modeling.";
RL   Thromb. Haemost. 83:119-126(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Yu H., Xiang K., Wang Y., Liu J.;
RT   "B chain of antithrombin A from Deinagkistrodon acutus.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 24-32, AND FUNCTION.
RX   PubMed=15777951; DOI=10.1016/j.toxicon.2004.11.017;
RA   Xu G., Ulrichts H., Vauterin S., De Meyer S.F., Deckmyn H., Teng M.,
RA   Niu L.;
RT   "How does agkicetin-C bind on platelet glycoprotein Ibalpha and achieve its
RT   platelet effects?";
RL   Toxicon 45:561-570(2005).
RN   [4]
RP   CRYSTALLIZATION.
RX   PubMed=16508096; DOI=10.1107/s1744309104027241;
RA   Xu G., Huang Q., Teng M., Liu P., Dong Y., Niu L.;
RT   "Crystallization and preliminary X-ray crystallographic analysis of
RT   agkicetin-C from Deinagkistrodon acutus venom.";
RL   Acta Crystallogr. F 61:75-78(2005).
CC   -!- FUNCTION: Is a potent glycoprotein Ibalpha (GP1BA) antagonist.
CC       Concentration-dependently inhibits botrocetin-, ristocetin- and low
CC       dose thrombin-induced platelet aggregation. Inhibits platelet adhesion
CC       only through inhibiting the vWF interaction with GP1BA, but has minimal
CC       effect on other platelet receptors, such as alpha-IIb/beta-3
CC       (ITGA2B/ITGB3) or alpha-2/beta-1 (ITGA2/ITGB1). Causes an instant
CC       severe thrombocytopenia in rats and is not lethal to mice.
CC       {ECO:0000269|PubMed:15777951}.
CC   -!- SUBUNIT: Heterodimer of subunits alpha and beta; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Lacks hemorrhagic activity in rabbits. Has no inhibitory
CC       effect on the coagulation cascade of humans. Does not agglutinate human
CC       erythrocytes of four groups (AC, BC, OC, ABK) and rabbit erythrocytes
CC       as well, which indicates it is not really a lectin (PubMed:15777951).
CC       {ECO:0000305|PubMed:15777951}.
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   EMBL; AF102902; AAG42041.1; -; mRNA.
DR   EMBL; AY091755; AAM22784.1; -; mRNA.
DR   AlphaFoldDB; Q9DEA1; -.
DR   SMR; Q9DEA1; -.
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:15777951"
FT   CHAIN           24..146
FT                   /note="Snaclec agkicetin-C subunit beta"
FT                   /id="PRO_5000055287"
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 (with C-101 in subunit alpha)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        119..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   146 AA;  16688 MW;  E5E32A734887793B CRC64;
     MGRFIFVSFG LLVVFLSLSG TGADCPPDWS SYEGNCYLVV KEKKTWAEAQ KFCTEQRKEC
     HLVSFHSAEE VDFVVSKTFP ILSYDLVWIG LNNIWNDCML EWSDGTKLTY KAWSGIPECI
     ISKTSDNQWL SRACSRTQPF VCKFQA