CD209_CHLAE
ID CD209_CHLAE Reviewed; 381 AA.
AC P60883;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, AND
RP INTERACTION WITH SIV.
RC STRAIN=Isolate 96028, and Isolate 97026; TISSUE=Lymph node;
RX PubMed=14694112; DOI=10.1128/jvi.78.2.798-810.2004;
RA Ploquin M.J.-Y., Diop O.M., Sol-Foulon N., Mortara L., Faye A.,
RA Soares M.A., Nerrienet E., Le Grand R., Van Kooyk Y., Amara A.,
RA Schwartz O., Barre-Sinoussi F., Mueller-Trutwin M.C.;
RT "DC-SIGN from African green monkeys is expressed in lymph nodes and
RT mediates infection in trans of simian immunodeficiency virus SIVagm.";
RL J. Virol. 78:798-810(2004).
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=3;
CC Name=1;
CC IsoId=P60883-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60883-2; Sequence=VSP_010035, VSP_010036;
CC Name=3;
CC IsoId=P60883-3; Sequence=VSP_010036;
CC -!- TISSUE SPECIFICITY: Expressed in lymph nodes.
CC {ECO:0000269|PubMed:14694112}.
CC -!- DOMAIN: The tandem repeat domain, also called neck domain, mediates
CC oligomerization. {ECO:0000250}.
CC -!- MISCELLANEOUS: In vitro, is a receptor for SIV and transmits virus to
CC permissive T-cells.
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DR EMBL; AY189944; AAP03436.1; -; mRNA.
DR EMBL; AY189945; AAP03437.1; -; mRNA.
DR EMBL; AY189946; AAP03438.1; -; mRNA.
DR EMBL; AY189947; AAP03439.1; -; mRNA.
DR AlphaFoldDB; P60883; -.
DR SMR; P60883; -.
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 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; Repeat;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..381
FT /note="CD209 antigen"
FT /id="PRO_0000046593"
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..381
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..234
FT /note="6"
FT DOMAIN 240..355
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 96..303
FT /note="6 X approximate tandem repeats"
FT REGION 359..381
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 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 343
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 233..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 261..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 333..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 16..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14694112"
FT /id="VSP_010035"
FT VAR_SEQ 85..268
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14694112"
FT /id="VSP_010036"
SQ SEQUENCE 381 AA; 42957 MW; 7FFA286780DF7178 CRC64;
MSDSKEPRLQ QLGLLEEEQL GGVGFRQTRG YKSLAGCLGH GPLVLQLLSF TLLAGLLVQV
SKVPSSLSQG QSKQDAIYQN LTQLKVAVSE LSEKSKQQEI YQELTRLKAA VGELPEKSKQ
QEIYQELTRL KAAVGELPEK SKLQEIYQEL TRLKAAVGEL PEKSKQQEIY QELSQLKAAV
GDLPEKSKQQ EIYQKLTQLK AAVDGLPDRS KQQEIYQELI QLKAAVERLC RPCPWEWTFF
QGNCYFMSNS QRNWHNSITA CQEVGAQLVV IKSAEEQNFL QLQSSRSNRF TWMGLSDLNH
EGTWQWVDGS PLLPSFKQYW NKGEPNNIGE EDCAEFSGNG WNDDKCNLAK FWICKKSAAS
CSGDEERLLS PTPTTPNPPP E
