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