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SLCA_DEIAC
ID   SLCA_DEIAC              Reviewed;         155 AA.
AC   Q9DEA2; Q8JIV6;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Snaclec agkicetin-C subunit alpha;
DE   AltName: Full=Antithrombin A subunit 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;
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   "A 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.
RC   TISSUE=Venom;
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; AF102901; AAG42040.1; -; mRNA.
DR   EMBL; AY091762; AAM22790.1; -; mRNA.
DR   AlphaFoldDB; Q9DEA2; -.
DR   SMR; Q9DEA2; -.
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..155
FT                   /note="Snaclec agkicetin-C subunit alpha"
FT                   /id="PRO_5000055286"
FT   DOMAIN          32..150
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..149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        101
FT                   /note="Interchain (with C-98 in subunit beta)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        124..141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CONFLICT        31
FT                   /note="S -> C (in Ref. 2; AAM22790)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="R -> G (in Ref. 2; AAM22790)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   155 AA;  17799 MW;  92B40281A797AACD CRC64;
     MGRFIFVSFG LLVVFLSLSG TAADCLPGWS SYIRFCYQPF KLLKTWEDAE RFCTEQANGG
     HLVSFESARE ADFVAGVLSE NIKIKPYVWI GLRVQNEGQQ CSSKWSDSSK VSYENLVEPF
     SKKCFVLKKD TGFRTWENVY CGLKHVFMCK YLKPR
 
 
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