ID   SLJB_PROJR              Reviewed;         148 AA.
AC   E2DQZ5;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Snaclec jerdonuxin subunit beta;
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:ADK56181.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-49, 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; GU136388; ADK56181.1; -; mRNA.
DR   AlphaFoldDB; E2DQZ5; -.
DR   SMR; E2DQZ5; -.
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..148
FT                   /note="Snaclec jerdonuxin subunit beta"
FT                   /id="PRO_0000413659"
FT   DOMAIN          34..145
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        26
FT                   /note="Interchain (with C-158 in subunit alpha of
FT                   tetrameric partner)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6TPG9,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        27..38
FT                   /evidence="ECO:0000250|UniProtKB:Q6TPG9,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        55..144
FT                   /evidence="ECO:0000250|UniProtKB:Q6TPG9,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        100
FT                   /note="Interchain (with C-104 in subunit alpha of
FT                   heterodimeric partner)"
FT                   /evidence="ECO:0000250|UniProtKB:Q6TPG9,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        121..136
FT                   /evidence="ECO:0000250|UniProtKB:Q6TPG9,
FT                   ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   148 AA;  17153 MW;  D685E161A4C4F623 CRC64;
     MVRFIFVSFG LLVVFLSLSG IGAGFCCPWG WSSYDEHCYQ VFQQKMNWED AEKFCIQQHK
     GSHLVSFHSS EEVDLVTSKT FPILKHDFVW MGLSNVWNEC TREWSDGTKL DYKAWSGQSD
     CIVSKTTDNQ WLSMDCSSKR YIVCKFQA