CD209_MACMU
ID CD209_MACMU Reviewed; 404 AA.
AC Q95J96; Q8HXL6; Q8HXL7; Q8HXL8; Q8HXL9; Q8SQB2; Q95LA8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=CD209 antigen;
DE AltName: Full=Dendritic cell-specific ICAM-3-grabbing non-integrin 1;
DE Short=DC-SIGN1;
DE AltName: CD_antigen=CD209;
GN Name=CD209;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION WITH
RP ICAM2; ICAM3 AND HIV-1 GP120.
RC TISSUE=Lymph node;
RX PubMed=11595296; DOI=10.1016/s0165-2478(01)00279-6;
RA Geijtenbeek T.B.H., Koopman G., van Duijnhoven G.C.F., van Vliet S.J.,
RA van Schijndel A.C.H.W., Engering A., Heeney J.L., van Kooyk Y.;
RT "Rhesus and chimpanzee DC-SIGN act as HIV/SIV gp120 trans-receptors,
RT similar as human DC-SIGN.";
RL Immunol. Lett. 79:101-107(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2), AND INTERACTION WITH HIV-1; HIV-2; SIV AND
RP ICAM3.
RX PubMed=11581396; DOI=10.1128/jvi.75.21.10281-10289.2001;
RA Baribaud F., Pohlmann S., Sparwasser T., Kimata M.T., Choi Y.K.,
RA Haggarty B.S., Ahmad N., Macfarlan T., Edwards T.G., Leslie G.J.,
RA Arnason J., Reinhart T.A., Kimata J.T., Littman D.R., Hoxie J.A.,
RA Doms R.W.;
RT "Functional and antigenic characterization of human, rhesus macaque,
RT pigtailed macaque, and murine DC-SIGN.";
RL J. Virol. 75:10281-10289(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH HIV-1 AND SIV.
RX PubMed=11818554; DOI=10.1073/pnas.032654399;
RA Wu L., Bashirova A.A., Martin T.D., Villamide L., Mehlhop E., Chertov A.O.,
RA Unutmaz D., Pope M., Carrington M., Kewalramani V.N.;
RT "Rhesus macaque dendritic cells efficiently transmit primate lentiviruses
RT independently of DC-SIGN.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1568-1573(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2; 3; 4 AND 5).
RX PubMed=12230940; DOI=10.1089/088922202760265641;
RA Santos P.R., Petitprez K., Butor C.;
RT "Gene for Chinese rhesus macaque DC-SIGN predicts the existence of A but
RT not B isoforms of the protein.";
RL AIDS Res. Hum. Retroviruses 18:977-981(2002).
CC -!- FUNCTION: Pathogen-recognition receptor expressed on the surface of
CC immature dendritic cells (DCs) and involved in initiation of primary
CC immune response. Thought to mediate the endocytosis of pathogens which
CC are subsequently degraded in lysosomal compartments. The receptor
CC returns to the cell membrane surface and the pathogen-derived antigens
CC are presented to resting T-cells via MHC class II proteins to initiate
CC the adaptive immune response. Probably recognizes in a calcium-
CC dependent manner high mannose N-linked oligosaccharides in a variety of
CC pathogen antigens (By similarity). {ECO:0000250}.
CC -!- FUNCTION: On DCs it is a high affinity receptor for ICAM2 and ICAM3 by
CC binding to mannose-like carbohydrates. May act as a DC rolling receptor
CC that mediates transendothelial migration of DC presursors from blood to
CC tissues by binding endothelial ICAM2. Seems to regulate DC-induced T-
CC cell proliferation by binding to ICAM3 on T-cells in the immunological
CC synapse formed between DC and T-cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. Interacts with C1QBP; the interaction is
CC indicative for a C1q:C1QBP:CD209 signaling complex. Interacts with
CC ICAM2 and ICAM3 by binding to mannose-like carbohydrates. Interacts
CC (via C-type lectin domain) with CEACAM1 (via Lewis X moieties); this
CC interaction is regulated by the glycosylation pattern of CEACAM1 on
CC cell types and regulates contact between dendritic cells and
CC neutrophils. {ECO:0000250|UniProtKB:Q9NNX6}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q95J96-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q95J96-2; Sequence=VSP_010053;
CC Name=3;
CC IsoId=Q95J96-3; Sequence=VSP_010053, VSP_010054;
CC Name=4;
CC IsoId=Q95J96-4; Sequence=VSP_010052;
CC Name=5;
CC IsoId=Q95J96-5; Sequence=VSP_010051;
CC -!- MISCELLANEOUS: In vitro, is a receptor for HIV-1, HIV-2 and SIV and
CC transmits viruses to permissive T-cells.
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DR EMBL; AF391086; AAK97459.1; -; mRNA.
DR EMBL; AF369755; AAL14438.1; -; mRNA.
DR EMBL; AY040319; AAK74185.1; -; mRNA.
DR EMBL; AJ439425; CAD28396.1; -; Genomic_DNA.
DR EMBL; AJ439425; CAD28397.1; -; Genomic_DNA.
DR EMBL; AJ439425; CAD28398.1; -; Genomic_DNA.
DR EMBL; AJ439425; CAD28399.1; -; Genomic_DNA.
DR RefSeq; NP_001028042.1; NM_001032870.1.
DR RefSeq; NP_001028261.1; NM_001033089.1.
DR AlphaFoldDB; Q95J96; -.
DR SMR; Q95J96; -.
DR STRING; 9544.ENSMMUP00000029556; -.
DR GeneID; 574211; -.
DR KEGG; mcc:574211; -.
DR CTD; 30835; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q95J96; -.
DR OrthoDB; 1232767at2759; -.
DR Proteomes; UP000006718; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0005537; F:mannose binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Calcium; Cell adhesion;
KW Disulfide bond; Endocytosis; Glycoprotein; Immunity; Innate immunity;
KW Lectin; Mannose-binding; Membrane; Metal-binding; Receptor;
KW Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..404
FT /note="CD209 antigen"
FT /id="PRO_0000046599"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..404
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REPEAT 96..118
FT /note="1"
FT REPEAT 119..141
FT /note="2"
FT REPEAT 142..164
FT /note="3"
FT REPEAT 165..187
FT /note="4"
FT REPEAT 188..210
FT /note="5"
FT REPEAT 211..233
FT /note="6"
FT REPEAT 234..257
FT /note="7"
FT DOMAIN 263..378
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 96..257
FT /note="7 X approximate tandem repeats"
FT REGION 382..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..15
FT /note="Endocytosis signal"
FT /evidence="ECO:0000250"
FT MOTIF 16..18
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT MOTIF 31..34
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 256..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 284..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 356..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 74..308
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_010051"
FT VAR_SEQ 143..235
FT /note="LQEIYQELTRLKAAVGELPEKSKMQEIYQELSRLKAAVGDLPEKSKQQEIYQ
FT ELSRLKAAVGDLPEKSKQQEIYQKLTQLKAAVDGLPDRSKQ -> L (in isoform
FT 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_010052"
FT VAR_SEQ 165..187
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11818554"
FT /id="VSP_010053"
FT VAR_SEQ 301..306
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_010054"
FT CONFLICT 13
FT /note="D -> G (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="G -> D (in Ref. 1; AAK97459)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="R -> W (in Ref. 1; AAK97459)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="S -> T (in Ref. 1; AAK97459)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="D -> E (in Ref. 4; CAD28397/CAD28398)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="H -> R (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="D -> N (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="A -> E (in Ref. 3; AAK74185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 45554 MW; E4C5D69FA7FCDB70 CRC64;
MSDSKEPRLQ QLDLLEEEQL GGVGFRQTRG YKSLAGCLGH GPLVLQLLSF TLLAGLLVQV
SKVPSSLSQG QSKQDAIYQN LTQLKVAVSE LSEKSKQQEI YQELTRLKAA VGELPEKSKQ
QEIYEELTRL KAAVGELPEK SKLQEIYQEL TRLKAAVGEL PEKSKMQEIY QELSRLKAAV
GDLPEKSKQQ EIYQELSRLK AAVGDLPEKS KQQEIYQKLT QLKAAVDGLP DRSKQQEIYQ
ELIQLKAAVE RLCHPCPWEW TFFQGNCYFM SNSQRNWHDS ITACQEVGAQ LVVIKSAEEQ
NFLQLQSSRS NRFTWMGLSD LNHEGTWQWV DGSPLLPSFK QYWNKGEPNN IGEEDCAEFS
GNGWNDDKCN LAKFWICKKS AASCSGDEER LLSPAPTTPN PPPA
