C209C_MOUSE
ID C209C_MOUSE Reviewed; 178 AA.
AC Q91ZW9; Q0VB37;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=CD209 antigen-like protein C;
DE AltName: Full=DC-SIGN-related protein 2;
DE Short=DC-SIGNR2;
DE AltName: CD_antigen=CD209;
GN Name=Cd209c;
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 [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=11581173; DOI=10.1093/intimm/13.10.1283;
RA Park C.G., Takahara K., Umemoto E., Yashima Y., Matsubara K., Matsuda Y.,
RA Clausen B.E., Inaba K., Steinman R.M.;
RT "Five mouse homologues of the human dendritic cell C-type lectin, DC-
RT SIGN.";
RL Int. Immunol. 13:1283-1290(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Probable pathogen-recognition receptor. May recognize in a
CC calcium-dependent manner high mannose N-linked oligosaccharides in a
CC variety of pathogen antigens.
CC -!- CAUTION: In mouse, 5 genes homologous to human CD209/DC-SIGN and
CC CD209L/DC-SIGNR have been identified. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=SIGNR2;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_163";
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DR EMBL; AF373410; AAL13236.1; -; mRNA.
DR EMBL; BC120804; AAI20805.1; -; mRNA.
DR EMBL; BC132635; AAI32636.1; -; mRNA.
DR EMBL; BC145088; AAI45089.1; -; mRNA.
DR CCDS; CCDS22078.1; -.
DR RefSeq; NP_570973.1; NM_130903.3.
DR AlphaFoldDB; Q91ZW9; -.
DR SMR; Q91ZW9; -.
DR BioGRID; 228434; 1.
DR STRING; 10090.ENSMUSP00000039861; -.
DR GlyGen; Q91ZW9; 1 site.
DR PaxDb; Q91ZW9; -.
DR PRIDE; Q91ZW9; -.
DR DNASU; 170776; -.
DR Ensembl; ENSMUST00000044060; ENSMUSP00000039861; ENSMUSG00000040165.
DR GeneID; 170776; -.
DR KEGG; mmu:170776; -.
DR UCSC; uc009ksw.1; mouse.
DR CTD; 170776; -.
DR MGI; MGI:2157945; Cd209c.
DR VEuPathDB; HostDB:ENSMUSG00000040165; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155012; -.
DR HOGENOM; CLU_049894_7_0_1; -.
DR InParanoid; Q91ZW9; -.
DR OMA; YWICKKS; -.
DR OrthoDB; 1232767at2759; -.
DR PhylomeDB; Q91ZW9; -.
DR TreeFam; TF333341; -.
DR BioGRID-ORCS; 170776; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q91ZW9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91ZW9; protein.
DR Bgee; ENSMUSG00000040165; Expressed in morula and 58 other tissues.
DR ExpressionAtlas; Q91ZW9; baseline and differential.
DR Genevisible; Q91ZW9; MM.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0005537; F:mannose binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001618; F:virus receptor activity; ISO:MGI.
DR CDD; cd03590; CLECT_DC-SIGN_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; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Lectin; Mannose-binding;
KW Metal-binding; Receptor; Reference proteome.
FT CHAIN 1..178
FT /note="CD209 antigen-like protein C"
FT /id="PRO_0000046606"
FT DOMAIN 54..169
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 76..168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 147..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 178 AA; 21245 MW; 034F94CE02BD9032 CRC64;
MRMHTRLQFL KRVSNVAYSH GQEQAKKEKV YKEMTQLKSQ INRLCRPCPW DWTVFQGNCY
FFSKFQQNWN DSVNACRKLD AQLVVIKSDD EQSFLQQTSK EKGYAWMGLS DLKHEGRWHW
VDGSHLLFSF MKYWNKGEPN NEWEEDCAEF RGDGWNDAPC TIKKYWICKK SAMSCTEK
