C209A_MOUSE
ID C209A_MOUSE Reviewed; 238 AA.
AC Q91ZX1; Q3TAT9; Q91ZW5;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=CD209 antigen-like protein A;
DE AltName: Full=Dendritic cell-specific ICAM-3-grabbing non-integrin;
DE Short=DC-SIGN;
DE AltName: CD_antigen=CD209;
GN Name=Cd209a; Synonyms=Cire;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INDUCTION,
RP AND TISSUE SPECIFICITY.
RX PubMed=11684292; DOI=10.1016/s0161-5890(01)00067-0;
RA Caminschi I., Lucas K.M., O'Keeffe M.A., Hochrein H., Laabi Y.,
RA Brodnicki T.C., Lew A.M., Shortman K., Wright M.D.;
RT "Molecular cloning of a C-type lectin superfamily protein differentially
RT expressed by CD8alpha(-) splenic dendritic cells.";
RL Mol. Immunol. 38:365-373(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Oviduct, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Probable pathogen-recognition receptor. May mediate the
CC endocytosis of pathogens which are subsequently degraded in lysosomal
CC compartments. May recognize in a calcium-dependent manner high mannose
CC N-linked oligosaccharides in a variety of pathogen antigens.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91ZX1-1; Sequence=Displayed;
CC Name=2; Synonyms=neck-less;
CC IsoId=Q91ZX1-2; Sequence=VSP_010067;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in dendritic cells.
CC Detected at very low levels in lung, spleen, lymph nodes and bone
CC marrow. {ECO:0000269|PubMed:11581173, ECO:0000269|PubMed:11684292}.
CC -!- INDUCTION: Down-regulated upon activation of dendritic cells.
CC {ECO:0000269|PubMed:11684292}.
CC -!- CAUTION: In mouse, 5 genes homologous to human CD209/DC-SIGN and
CC CD209L/DC-SIGNR have been identified. Mouse CD209A product was named
CC DC-SIGN by PubMed:11581173 because of its similar expression pattern
CC and chromosomal location in juxtaposition to CD23, but despite of the
CC low sequence similarity. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=SIGNR5;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_00130";
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; AF373408; AAL13234.1; -; mRNA.
DR EMBL; AF374470; AAL27539.1; -; mRNA.
DR EMBL; AY049062; AAK85825.1; -; mRNA.
DR EMBL; AK054139; BAC35667.1; -; mRNA.
DR EMBL; AK171639; BAE42579.1; -; mRNA.
DR CCDS; CCDS22073.1; -. [Q91ZX1-1]
DR RefSeq; NP_573501.1; NM_133238.5. [Q91ZX1-1]
DR AlphaFoldDB; Q91ZX1; -.
DR SMR; Q91ZX1; -.
DR STRING; 10090.ENSMUSP00000012847; -.
DR GlyGen; Q91ZX1; 2 sites.
DR iPTMnet; Q91ZX1; -.
DR PhosphoSitePlus; Q91ZX1; -.
DR MaxQB; Q91ZX1; -.
DR PaxDb; Q91ZX1; -.
DR PRIDE; Q91ZX1; -.
DR DNASU; 170786; -.
DR Ensembl; ENSMUST00000012847; ENSMUSP00000012847; ENSMUSG00000031494. [Q91ZX1-1]
DR Ensembl; ENSMUST00000207979; ENSMUSP00000146702; ENSMUSG00000031494. [Q91ZX1-2]
DR GeneID; 170786; -.
DR KEGG; mmu:170786; -.
DR UCSC; uc009ksq.2; mouse. [Q91ZX1-1]
DR UCSC; uc012fyt.1; mouse. [Q91ZX1-2]
DR CTD; 170786; -.
DR MGI; MGI:2157942; Cd209a.
DR VEuPathDB; HostDB:ENSMUSG00000031494; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155012; -.
DR HOGENOM; CLU_049894_7_3_1; -.
DR InParanoid; Q91ZX1; -.
DR OMA; ILVKVYK; -.
DR OrthoDB; 1232767at2759; -.
DR PhylomeDB; Q91ZX1; -.
DR TreeFam; TF333341; -.
DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-MMU-8851680; Butyrophilin (BTN) family interactions.
DR BioGRID-ORCS; 170786; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q91ZX1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91ZX1; protein.
DR Bgee; ENSMUSG00000031494; Expressed in granulocyte and 46 other tissues.
DR ExpressionAtlas; Q91ZX1; baseline and differential.
DR Genevisible; Q91ZX1; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISS:MGI.
DR GO; GO:0097367; F:carbohydrate derivative binding; IDA:MGI.
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 GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0042129; P:regulation of T cell proliferation; 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 Alternative splicing; Calcium; Disulfide bond; Endocytosis; Glycoprotein;
KW Lectin; Mannose-binding; Membrane; Metal-binding; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..238
FT /note="CD209 antigen-like protein A"
FT /id="PRO_0000046604"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 115..229
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 136..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 207..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 75..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11581173"
FT /id="VSP_010067"
SQ SEQUENCE 238 AA; 27149 MW; 05C025FCF2E63DC2 CRC64;
MSDSKEMGKR QLRPLDEELL TSSHTRHSIK GFGFQTNSGF SSFTGCLVHS QVPLALQVLF
LAVCSVLLVV ILVKVYKIPS SQEENNQMNV YQELTQLKAG VDRLCRSCPW DWTHFQGSCY
FFSVAQKSWN DSATACHNVG AQLVVIKSDE EQNFLQQTSK KRGYTWMGLI DMSKESTWYW
VDGSPLTLSF MKYWSKGEPN NLGEEDCAEF RDDGWNDTKC TNKKFWICKK LSTSCPSK
