CD209_GORGO
ID CD209_GORGO Reviewed; 427 AA.
AC Q8HXZ8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate Ggo3;
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; AY078912; AAL89543.1; -; Genomic_DNA.
DR EMBL; AY078906; AAL89543.1; JOINED; Genomic_DNA.
DR EMBL; AY078907; AAL89543.1; JOINED; Genomic_DNA.
DR EMBL; AY078908; AAL89543.1; JOINED; Genomic_DNA.
DR EMBL; AY078909; AAL89543.1; JOINED; Genomic_DNA.
DR EMBL; AY078910; AAL89543.1; JOINED; Genomic_DNA.
DR EMBL; AY078911; AAL89543.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q8HXZ8; -.
DR SMR; Q8HXZ8; -.
DR STRING; 9593.ENSGGOP00000019779; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q8HXZ8; -.
DR Proteomes; UP000001519; 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 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; Reference proteome; Repeat; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..427
FT /note="CD209 antigen"
FT /id="PRO_0000046594"
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..427
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..256
FT /note="7"
FT REPEAT 257..280
FT /note="8"
FT DOMAIN 286..401
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 96..280
FT /note="8 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 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 389
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 279..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 307..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 379..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 427 AA; 48400 MW; 2A75B519E7FFE3B2 CRC64;
MSDSKEPRLQ QLGLLEEEQL RGLGFRQTRG YKSLAGCLGH GPLVLQLLSF TLLAALLVQV
SKVPSSISQE QSRQDAIYQN LTQFKAAVGE LSEKSKLQEI YQELTQLKAA VGELPEKSKQ
QEIYQELSQL KAAVGELPEK SKQQEIYQEL SQLKAAVGEL PEKSKQQEIY QELTRLKAAV
GELPEKSKQQ EIYQELSQLK AAVGELPEKS KQQEIYQELS QLKAAVGELP EKSKQQEIYQ
ELTQLKAAVG ELPEKSKQQE IYQELTQLKA AVERLCRRCP WEWTFFQGNC YFMSNSQRNW
HDSITACQEV GAQLVVIKSA EEQNFLQLQS SRSNRFTWMG LSDLNHEGTW QWVDGSPLLP
SFKQYWNRGE PNNVGEEDCA EFSGNGWNDD KCNLAKFWIC KKSAASCSRD EEQFLSPASA
TPNPPPE
