ID LECM2_PSEPL Reviewed; 111 AA.
AC A7X3W6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 22-FEB-2023, entry version 54.
DE RecName: Full=C-type lectin lectoxin-Enh2;
DE Short=CTL;
DE Flags: Precursor;
OS Pseudoferania polylepis (Macleay's water snake) (Enhydris polylepis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Homalopsidae; Pseudoferania.
OX NCBI_TaxID=338839;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=17855442; DOI=10.1074/mcp.m700094-mcp200;
RA Fry B.G., Scheib H., van der Weerd L., Young B., McNaughtan J.,
RA Ramjan S.F.R., Vidal N., Poelmann R.E., Norman J.A.;
RT "Evolution of an arsenal: structural and functional diversification of the
RT venom system in the advanced snakes (Caenophidia).";
RL Mol. Cell. Proteomics 7:215-246(2008).
CC -!- FUNCTION: Mannose-binding lectin which recognizes specific carbohydrate
CC structures and agglutinates a variety of animal cells by binding to
CC cell-surface glycoproteins and glycolipids. May be a calcium-dependent
CC lectin (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
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DR EMBL; EU029690; ABU68490.1; -; mRNA.
DR AlphaFoldDB; A7X3W6; -.
DR SMR; A7X3W6; -.
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 GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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 PANTHER; PTHR22801:SF53; 27 KDA PRIMARY MESENCHYME-SPECIFIC SPICULE PROTEIN; 1.
DR PANTHER; PTHR22801; LITHOSTATHINE; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Hemagglutinin; Lectin; Metal-binding; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..111
FT /note="C-type lectin lectoxin-Enh2"
FT /id="PRO_0000356308"
FT DOMAIN 33..108
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 72..74
FT /note="Mannose-binding"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 26..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 82..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 111 AA; 12747 MW; AC8564819CB1D8B4 CRC64;
MGQFTVVSLG LLAMFLSLSG AKGDNCPASW ISRNGVCNKL FPDRKTWLEA EKRTWKWSDR
TSTNYFSWNQ GEPNNVQDNE NCVHLWAPSG YLKWNDEPCA SLHPFICQYK L
//
