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SLDB_TRIAB
ID   SLDB_TRIAB              Reviewed;         148 AA.
AC   P0DM39;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Snaclec alboaggregin-D subunit beta;
DE   Flags: Precursor;
OS   Trimeresurus albolabris (White-lipped pit viper) (Cryptelytrops
OS   albolabris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=8765;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=22033027; DOI=10.1016/j.toxicon.2011.10.009;
RA   Mekchay P., Rojnuckarin P.;
RT   "Molecular cloning and characterization of alboaggregin D, a novel platelet
RT   activating protein, from Green pit viper (Cryptelytrops albolabris)
RT   venom.";
RL   Toxicon 59:59-67(2012).
CC   -!- FUNCTION: Snaclec that induces human platelet aggregation in the
CC       absence of any cofactor with the EC(50) of 0.25 nM and causes tyrosine
CC       phosphorylation in human platelets. Antibodies against either platelet
CC       GPIbalpha (GP1BA) or GPVI (GP6) inhibit alboaggregin D-induced platelet
CC       aggregation. Only the combination of these two antibodies completely
CC       inhibit aggregation, suggesting that it acts through both GPIbalpha
CC       (GP1BA) and GPVI (GP6). {ECO:0000269|PubMed:22033027}.
CC   -!- SUBUNIT: Tetramer of heterodimers of alpha and beta subunits
CC       (alphabeta)(4); disulfide-linked. {ECO:0000269|PubMed:22033027}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22033027}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:22033027}.
CC   -!- MASS SPECTROMETRY: Mass=16963.1; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:22033027};
CC   -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DM39; -.
DR   SMR; P0DM39; -.
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   Disulfide bond; Glycoprotein; Hemostasis impairing toxin;
KW   Platelet aggregation activating toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..148
FT                   /note="Snaclec alboaggregin-D subunit beta"
FT                   /id="PRO_0000422609"
FT   DOMAIN          34..145
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26
FT                   /note="Interchain (with C-158 in subunit alpha)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        27..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        55..144
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        100
FT                   /note="Interchain (with C-104 in subunit alpha)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        121..136
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   148 AA;  17233 MW;  F479F21142AC6F0D CRC64;
     MGRFISVSFG LLVVFLSLSG AGAGLCCPLD WSSYDLYCYK VFKQQMNWTD AEQFCTQQHT
     GSHLVSFHST EEVDFVVQMS YKSLDTTFFW IGVNNIWNGC NWQWSDGTGL DYKEWREQFE
     CLVAKTFDNQ WWSMDCNSTY SFVCKFQA
 
 
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