LECG_TRIST
ID LECG_TRIST Reviewed; 158 AA.
AC Q9YGP1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=C-type lectin TsL;
DE AltName: Full=Galactose-binding lectin;
DE Short=CTL;
DE Flags: Precursor;
OS Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera
OS stejnegeri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=39682;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-53, SUBUNIT, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=10417338; DOI=10.1042/bj3410733;
RA Xu Q., Wu X.-F., Xia Q.-C., Wang K.-Y.;
RT "Cloning of a galactose-binding lectin from the venom of Trimeresurus
RT stejnegeri.";
RL Biochem. J. 341:733-737(1999).
RN [2]
RP PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-28, AND STRUCTURE OF CARBOHYDRATES.
RC TISSUE=Venom;
RX PubMed=10561575; DOI=10.1046/j.1432-1327.1999.00859.x;
RA Zeng R., Xu Q., Shao X.-X., Wang K.-Y., Xia Q.-C.;
RT "Characterization and analysis of a novel glycoprotein from snake venom
RT using liquid chromatography-electrospray mass spectrometry and Edman
RT degradation.";
RL Eur. J. Biochem. 266:352-358(1999).
CC -!- FUNCTION: Galactose-binding protein which recognizes specific
CC carbohydrate structures and agglutinates a variety of animal cells by
CC binding to cell-surface glycoproteins and glycolipids. May be a
CC calcium-dependent lectin.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:10417338}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=17924.2; Mass_error=2.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10417338};
CC -!- MISCELLANEOUS: Met-33 has been shown to be oxidized to methionine
CC sulfoxide but this probably results from sample treatment prior to mass
CC spectrometry. {ECO:0000305|PubMed:10561575}.
CC -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
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DR EMBL; AF119097; AAD17252.1; -; mRNA.
DR AlphaFoldDB; Q9YGP1; -.
DR SMR; Q9YGP1; -.
DR GlyConnect; 169; 5 N-Linked glycans (1 site).
DR PRIDE; Q9YGP1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
KW Metal-binding; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:10417338"
FT CHAIN 24..158
FT /note="C-type lectin TsL"
FT /id="PRO_0000017394"
FT DOMAIN 24..158
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 119..121
FT /note="Galactose-binding"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:10561575"
FT /id="CAR_000165"
FT DISULFID 26..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 54..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 61..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 109
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 129..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 158 AA; 18635 MW; 2077BC62B7A08FF9 CRC64;
MGRFIFVSFG LLVVFLSLSG AKGSCCTNDS LPMNGMCYKI FDEPKTWEDA EMFCRKYKPG
CHLASFHRLA ESLDIAEYIS DYHKRQAEVW IGLLDRKKDF SWEWTDRSCT DYLNWDKNQP
DHYKDKEFCV ELVSLTGYHR WNDQVCESKN SFLCQCKF
