ID LECM2_PHIOL Reviewed; 156 AA.
AC A7X409;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=C-type lectin lectoxin-Phi2;
DE Short=CTL;
DE Flags: Precursor;
OS Philodryas olfersii (Green snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Dipsadidae; Philodryas.
OX NCBI_TaxID=120305;
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; EU029701; ABU68501.1; -; mRNA.
DR AlphaFoldDB; A7X409; -.
DR SMR; A7X409; -.
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; 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; PTHR22803:SF124; C-TYPE LECTIN DOMAIN FAMILY 19 MEMBER A-RELATED; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR PRINTS; PR01504; PNCREATITSAP.
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; Glycoprotein; Lectin; Metal-binding; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..156
FT /note="C-type lectin lectoxin-Phi2"
FT /id="PRO_0000355286"
FT DOMAIN 34..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 CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 55..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 129..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 156 AA; 18309 MW; 2296791B66F621D7 CRC64;
MGRFIFVSLG LLVLAFSLSG IGADQHCPSG WFSHNVSCYK LINDWKTWDE AQRFCMDEQE
NGQLASINDV GESVKLSDEF SKTWSIIDVW IGLRLSKRKS IWEWIDGSNV TQTRWEEGEP
NNFLKKEFCV VLTSRSRYLK WNDKDCNRRH RFLCKF
//
