CD209_NOMCO
ID CD209_NOMCO Reviewed; 404 AA.
AC Q8HY01;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 Nomascus concolor (Black crested gibbon) (Hylobates concolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=29089;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate B128;
RX PubMed=12477827; DOI=10.1128/jvi.77.1.217-227.2003;
RA Bashirova A.A., Wu L., Cheng J., Martin T.D., Martin M.P., Benveniste R.E.,
RA Lifson J.D., Kewalramani V.N., Hughes A., Carrington M.;
RT "Novel member of the CD209 (DC-SIGN) gene family in primates.";
RL J. Virol. 77:217-227(2003).
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 -!- DOMAIN: The tandem repeat domain, also called neck domain, mediates
CC oligomerization. {ECO:0000250}.
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DR EMBL; AY078891; AAL89540.1; -; Genomic_DNA.
DR EMBL; AY078885; AAL89540.1; JOINED; Genomic_DNA.
DR EMBL; AY078886; AAL89540.1; JOINED; Genomic_DNA.
DR EMBL; AY078887; AAL89540.1; JOINED; Genomic_DNA.
DR EMBL; AY078888; AAL89540.1; JOINED; Genomic_DNA.
DR EMBL; AY078889; AAL89540.1; JOINED; Genomic_DNA.
DR EMBL; AY078890; AAL89540.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q8HY01; -.
DR SMR; Q8HY01; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Adaptive immunity; Calcium; Cell adhesion; Disulfide bond; Endocytosis;
KW Glycoprotein; Immunity; Innate immunity; Lectin; Mannose-binding; Membrane;
KW Metal-binding; Receptor; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..404
FT /note="CD209 antigen"
FT /id="PRO_0000046596"
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 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"
SQ SEQUENCE 404 AA; 45562 MW; E95F92E3C5DC97F0 CRC64;
MSDSKEPSVQ QLGLLEEEQL RGLGFRQTRG YKSLAGCLGH GALVLQLLSF TLLAGLLIQV
SKFPSSISQE QSKQDAIYQN LTQLKAAVGE LSEKSKLQEI YQELTQLKAA VGELPEKSKQ
QEIYQELTQL KAAVGELPEK SKQQEIYQEL TQLKAAVGEL PEKSKQQEIY QELTRLKAAV
GELPEKSQQQ EIYQELTQLK AAVGELPEKS KQQEIYQELT RLKAAVGELP EKSKQQEIYQ
ELTQLKAAVE RLCRPCPWEW TFFQGNCYFM SNSQRDWHDS VTACQEVGAQ LVVIKSAEEQ
NFLQLQSSRS NRFAWMGLSD LNQEGTWQWV DGSPLSPSFK QYWNRGEPNN VGEEDCAEFS
GNGWNDDKCN LAKFWICKKS AASCSRDEEQ FLSPAPATPN PPPA
