CLC2F_MOUSE
ID CLC2F_MOUSE Reviewed; 196 AA.
AC Q8VI21;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=C-type lectin domain family 2 member F;
DE AltName: Full=C-type lectin-related protein C;
DE Short=Clr-c;
GN Name=Clec2f; Synonyms=Clrc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=11398965; DOI=10.1007/s002510100319;
RA Plougastel B., Dubbelde C., Yokoyama W.M.;
RT "Cloning of Clr, a new family of lectin-like genes localized between mouse
RT Nkrp1a and Cd69.";
RL Immunogenetics 53:209-214(2001).
CC -!- FUNCTION: Lectin-type cell surface receptor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
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; AF320596; AAL37197.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8VI21; -.
DR SMR; Q8VI21; -.
DR GlyGen; Q8VI21; 1 site.
DR iPTMnet; Q8VI21; -.
DR PhosphoSitePlus; Q8VI21; -.
DR PRIDE; Q8VI21; -.
DR ProteomicsDB; 279100; -.
DR MGI; MGI:3522133; Clec2f.
DR InParanoid; Q8VI21; -.
DR PRO; PR:Q8VI21; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VI21; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; IBA:GO_Central.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
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; IPR016187; CTDL_fold.
DR InterPro; IPR033992; NKR-like_CTLD.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; Lectin; Membrane;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..196
FT /note="C-type lectin domain family 2 member F"
FT /id="PRO_0000315288"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..196
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 84..187
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 77..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 105..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 196 AA; 22205 MW; 2504DA7A46BF3C6A CRC64;
MNAQCLKKPE EGESSPGTGD KILQRNSLRA ISPESSAKLY CCCGVIMVLT VAVVALSVAL
PATKTEQILI NKTYAACPKN WIGVGNKCFY FSEYTSNWTF AQTFCMAQEA QLARFDNEKE
LNFLKRHMNS SHWIGLHRDS SEHPWRWTDN TEYNNTFLIQ GDGECGFLSD NGISSSRDYI
PRKWICSRSS NYMLQC