LECM_CERRY
ID LECM_CERRY Reviewed; 158 AA.
AC D8VNS6;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=C-type lectin;
DE Short=CTL;
DE Flags: Precursor;
OS Cerberus rynchops (Dog-faced water snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Homalopsidae; Cerberus.
OX NCBI_TaxID=46267;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP 3D-STRUCTURE MODELING.
RC TISSUE=Venom, and Venom gland;
RX PubMed=20158271; DOI=10.1021/pr901044x;
RA Ompraba G., Chapeaurouge A., Doley R., Devi K.R., Padmanaban P.,
RA Venkatraman C., Velmurugan D., Lin Q., Kini R.M.;
RT "Identification of a novel family of snake venom proteins Veficolins from
RT Cerberus rynchops using a venom gland transcriptomics and proteomics
RT approach.";
RL J. Proteome Res. 9:1882-1893(2010).
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.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the true venom lectin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GU065322; ADJ51061.1; -; mRNA.
DR AlphaFoldDB; D8VNS6; -.
DR SMR; D8VNS6; -.
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; -; 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; Disulfide bond; Lectin; Metal-binding; Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..158
FT /note="C-type lectin"
FT /id="PRO_0000414914"
FT DOMAIN 33..155
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 119..121
FT /note="Mannose-binding"
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 DISULFID 26..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 54..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 129..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 158 AA; 18112 MW; 5B38F1BED9C0D72A CRC64;
MWQFTVVSLG WLAVFLSLSG AKGNSCPASW ISRNGVCNKL FPDRKTWLEA EMYCRALKPG
GHLASLHKDS DSTVLAWYIS DHFKGAGHVW IGLRDTNKKR SWKWSDRTST NYFSWNQGEP
NNVQDNENCV HLWAPSGYLK WNDEPCASLH PFICQYKL
