SLEA_PROMU
ID SLEA_PROMU Reviewed; 158 AA.
AC Q8JGT7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Snaclec mucetin subunit alpha;
DE AltName: Full=Trimeresurus mucrosquamatus venom activator subunit alpha;
DE Short=TMVA subunit alpha;
DE Flags: Precursor;
OS Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=103944;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-58, FUNCTION, SUBUNIT,
RP AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=12220719; DOI=10.1016/s0041-0101(02)00144-7;
RA Wei Q., Lu Q.-M., Jin Y., Li R., Wei J.-F., Wang W.-Y., Xiong Y.-L.;
RT "Purification and cloning of a novel C-type lectin-like protein with
RT platelet aggregation activity from Trimeresurus mucrosquamatus venom.";
RL Toxicon 40:1331-1338(2002).
RN [2]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=15175804; DOI=10.1160/th03-12-0747;
RA Lu Q., Navdaev A., Clemetson J.M., Clemetson K.J.;
RT "GPIb is involved in platelet aggregation induced by mucetin, a snake C-
RT type lectin protein from Chinese habu (Trimeresurus mucrosquamatus)
RT venom.";
RL Thromb. Haemost. 91:1168-1176(2004).
RN [3]
RP FUNCTION.
RX PubMed=15501291; DOI=10.1016/j.toxicon.2004.07.022;
RA Tai H., Wei Q., Jin Y., Su M., Song J.X., Zhou X.D., Ouyang H.M.,
RA Wang W.Y., Xiong Y.L., Zhang Y.;
RT "TMVA, a snake C-type lectin-like protein from Trimeresurus mucrosquamatus
RT venom, activates platelet via GPIb.";
RL Toxicon 44:649-656(2004).
RN [4]
RP FUNCTION.
RX PubMed=16102113; DOI=10.1111/j.1538-7836.2005.01481.x;
RA Lu Q., Clemetson J.M., Clemetson K.J.;
RT "Translocation of GPIb and Fc receptor gamma-chain to cytoskeleton in
RT mucetin-activated platelets.";
RL J. Thromb. Haemost. 3:2065-2076(2005).
CC -!- FUNCTION: Potent platelet activator that acts via GPIb (GP1BA/GP1BB)
CC (PubMed:15175804). After activation by the toxin, the receptor is
CC redistributed on platelet surface thanks to cytoskeletal translocation.
CC The indirect activation of integrin alpha-IIb/beta-3 (ITGA2B/ITGB3)
CC also induced by the toxin is downstream the cytoskeletal translocation
CC of GPIb (PubMed:16102113). {ECO:0000269|PubMed:12220719,
CC ECO:0000269|PubMed:15175804, ECO:0000269|PubMed:15501291,
CC ECO:0000269|PubMed:16102113}.
CC -!- SUBUNIT: Dimer and tetramer of heterodimers of alpha and beta subunits
CC ((alphabeta)(2) and (alphabeta)(4)); disulfide-linked. These two
CC multimeric forms are found. {ECO:0000269|PubMed:12220719}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: The complex is glycosylated. {ECO:0000269|PubMed:12220719}.
CC -!- MASS SPECTROMETRY: Mass=15536; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:12220719};
CC -!- MISCELLANEOUS: Does not act by binding GPVI (GP6) and integrin alpha-
CC 2/beta-1 (ITGA2/ITGB1) (PubMed:15175804 and PubMed:15501291). Does not
CC bind to platelet GPIX (GP9), GPIIb (ITGA2B), and GPIIIa (ITGB3)
CC (PubMed:15501291). {ECO:0000305|PubMed:15501291}.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; AY099321; AAM43808.1; -; mRNA.
DR AlphaFoldDB; Q8JGT7; -.
DR SMR; Q8JGT7; -.
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; Glycoprotein;
KW Hemostasis impairing toxin; Platelet aggregation activating toxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:12220719"
FT CHAIN 24..158
FT /note="Snaclec mucetin subunit alpha"
FT /id="PRO_0000355295"
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 multimeric
FT partner)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 158 AA; 18101 MW; CD0B71F02289AA6E CRC64;
MGRFTFVSFG LLVVFLSLSG TGADFDCIPG WSAYDRYCYQ AFSEPKNWED AESFCEEGVK
TSHLVSIESS GEGDFVAQLV AEKIKTSFQY VWIGLRIQNK EQQCRSEWSD ASSVNYENLF
KQSSKKCYAL KKGTELRTWF NVYCGRENPF VCKYTPEC
