SLJA_PROJR
ID SLJA_PROJR Reviewed; 158 AA.
AC E2DQZ6;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Snaclec jerdonuxin subunit alpha;
DE Flags: Precursor;
OS Protobothrops jerdonii (Jerdon's pitviper) (Trimeresurus jerdonii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=242841;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ADK56182.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-45, AND FUNCTION.
RC TISSUE=Venom {ECO:0000269|PubMed:21040740};
RX PubMed=21040740; DOI=10.1016/j.toxicon.2010.10.011;
RA Chen Z.M., Wu J.B., Zhang Y., Yu G.Y., Lee W.H., Lu Q.M., Zhang Y.;
RT "Jerdonuxin, a novel snaclec (snake C-type lectin) with platelet
RT aggregation activity from Trimeresurus jerdonii venom.";
RL Toxicon 57:109-116(2011).
CC -!- FUNCTION: Snaclec that strongly induces platelet aggregation, in a
CC dose-dependent manner. {ECO:0000269|PubMed:21040740}.
CC -!- SUBUNIT: Tetramer of 4 heterodimers of alpha and beta subunits;
CC disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21040740}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:21040740}.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; GU136389; ADK56182.1; -; mRNA.
DR AlphaFoldDB; E2DQZ6; -.
DR SMR; E2DQZ6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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 Lectin; Platelet aggregation activating toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:21040740"
FT CHAIN 24..158
FT /note="Snaclec jerdonuxin subunit alpha"
FT /id="PRO_0000413658"
FT DOMAIN 34..153
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 27..38
FT /evidence="ECO:0000250|UniProtKB:Q6TPH0,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 55..152
FT /evidence="ECO:0000250|UniProtKB:Q6TPH0,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 104
FT /note="Interchain (with C-100 in subunit beta of
FT heterodimeric partner)"
FT /evidence="ECO:0000250|UniProtKB:Q6TPH0,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 127..144
FT /evidence="ECO:0000250|UniProtKB:Q6TPH0,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 158
FT /note="Interchain (with C-26 in subunit beta of tetrameric
FT partner)"
FT /evidence="ECO:0000250|UniProtKB:Q6TPH0,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 44
FT /note="E -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 18102 MW; 10D2C00D968A1FBD CRC64;
MGRFTFVSFG LLVVFLSLSG TGADFDCIPG WSAYDRYCYQ AFSEPKNWED AESFCEEGVK
TSHLVSIESS GEGDFVAQLV SEKIKTSFQY VWIGLRIQNK EQQCRSEWTD ASSVNYENLI
KQFSKKCYAL KKGTELRTWF NVYCGTENPF VCKYTPEC