SLDA_TRIAB
ID SLDA_TRIAB Reviewed; 158 AA.
AC P0DM38;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Snaclec alboaggregin-D subunit alpha;
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 IDENTIFICATION BY 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 -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
CC -!- CAUTION: Position 67 and 84 are wrongly translated from the nucleotide
CC sequence, it is why a feature 'unsure' is indicated. AGC (position 67)
CC code for a Ser but a Val is indicated instead, whereas CTA (position
CC 84) code for a Leu but a Iso is indicated instead. {ECO:0000305}.
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DR AlphaFoldDB; P0DM38; -.
DR SMR; P0DM38; -.
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; Hemostasis impairing toxin;
KW Platelet aggregation activating toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..158
FT /note="Snaclec alboaggregin-D subunit alpha"
FT /id="PRO_0000422608"
FT DOMAIN 34..153
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 27..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 55..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 104
FT /note="Interchain (with C-100 in subunit beta of
FT heterodimeric partner)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 127..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 158
FT /note="Interchain (with C-26 in subunit beta of tetrameric
FT partner)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VARIANT 80
FT /note="V -> I"
FT UNSURE 67
FT UNSURE 84
SQ SEQUENCE 158 AA; 18017 MW; 8FAB70FDC678C203 CRC64;
MGRFIFGSFG LLVVFLSLSG TGADFDCPPG WSAYDRYCYQ AFSEPKTWED AESFCMEGVK
DSHLVSVESS GEADFVAQLV NENIKTSFRY VWIGLRIQNK EQQCRSEWSD ASSVSYENLI
KKVSKKCYGL KKGTELRTWF NVYCAELNPF ICKFPPEC