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Protein

CD209 antigen

Gene

CD209

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) and involved in initiation of primary immune response. Thought to mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. The receptor returns to the cell membrane surface and the pathogen-derived antigens are presented to resting T-cells via MHC class II proteins to initiate the adaptive immune response.1 Publication
On DCs it is a high affinity receptor for ICAM2 and ICAM3 by binding to mannose-like carbohydrates. May act as a DC rolling receptor that mediates transendothelial migration of DC presursors from blood to tissues by binding endothelial ICAM2. Seems to regulate DC-induced T-cell proliferation by binding to ICAM3 on T-cells in the immunological synapse formed between DC and T-cells.3 Publications
(Microbial infection) Acts as an attachment receptor for HIV-1 and HIV-2 (PubMed:11799126, PubMed:12502850, PubMed:1518869). Acts as an attachment receptor for ebolavirus (PubMed:12502850, PubMed:12504546). Acts as an attachment receptor for cytomegalovirus (PubMed:12433371, PubMed:22496863). Acts as an attachment receptor for HCV (PubMed:15371595, PubMed:16816373). Acts as an attachment receptor for dengue virus (PubMed:12682107). Acts as an attachment receptor for measles virus (PubMed:16537615). Acts as an attachment receptor for herpes simplex virus 1 (PubMed:18796707). Acts as an attachment receptor for Influenzavirus A (PubMed:21191006). Acts as an attachment receptor for SARS coronavirus (PubMed:15140961). Acts as an attachment receptor for Japanese encephalitis virus (PubMed:24623090). Acts as an attachment receptor for Lassa virus (PubMed:23966408). Acts as an attachment receptor for marburg virusn (PubMed:15479853). Acts as an attachment receptor for Respiratory syncytial virus (PubMed:22090124). Acts as an attachment receptor for Rift valley fever virus and uukuniemi virus (PubMed:21767814). Acts as an attachment receptor for west-nile virus (PubMed:16415006). Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of bacterial pathogen antigens, including Leishmania pifanoi LPG, Lewis-x antigen in Helicobacter pylori LPS, mannose in Klebsiella pneumonae LPS, di-mannose and tri-mannose in Mycobacterium tuberculosis ManLAM and Lewis-x antigen in Schistosoma mansoni SEA (PubMed:16379498). Recognition of M.tuberculosis by dendritic cells occurs partially via this molecule (PubMed:16092920, PubMed:21203928).22 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi347Calcium1
Metal bindingi349Calcium1
Metal bindingi351Calcium; via carbonyl oxygen1
Metal bindingi354Calcium1
Metal bindingi365Calcium1
Metal bindingi366Calcium1

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB
  • mannose binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • peptide antigen binding Source: UniProtKB
  • virion binding Source: UniProtKB
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • antigen processing and presentation Source: UniProtKB
  • cell-cell recognition Source: UniProtKB
  • endocytosis Source: UniProtKB-KW
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • intracellular signal transduction Source: UniProtKB
  • intracellular transport of virus Source: UniProtKB
  • leukocyte cell-cell adhesion Source: UniProtKB
  • modulation by virus of host morphology or physiology Source: UniProtKB
  • peptide antigen transport Source: UniProtKB
  • regulation of T cell proliferation Source: MGI
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • viral genome replication Source: UniProtKB
  • virion attachment to host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Receptor

Keywords - Biological processi

Adaptive immunity, Cell adhesion, Endocytosis, Host-virus interaction, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Lectin, Mannose-binding, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-5621575. CD209 (DC-SIGN) signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
CD209 antigen
Alternative name(s):
C-type lectin domain family 4 member L
Dendritic cell-specific ICAM-3-grabbing non-integrin 1
Short name:
DC-SIGN
Short name:
DC-SIGN1
CD_antigen: CD209
Gene namesi
Name:CD209
Synonyms:CLEC4L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1641. CD209.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 37CytoplasmicCuratedAdd BLAST37
Transmembranei38 – 58Helical; Signal-anchor for type II membrane proteinCuratedAdd BLAST21
Topological domaini59 – 404ExtracellularCuratedAdd BLAST346

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi14 – 15LL → AA: Loss of antigen internalization by endocytosis. 1 Publication2
Mutagenesisi320D → A: Loss of binding to ICAM3 and HIV-1 gp120. 1 Publication1
Mutagenesisi324E → A: Loss of binding to ICAM3 and HIV-1 gp120. 1 Publication1
Mutagenesisi347E → Q: Loss of binding to ICAM3 and HIV-1 gp120. 1 Publication1
Mutagenesisi349N → D: Loss of binding to ICAM3 and HIV-1 gp120. 1 Publication1
Mutagenesisi350N → A: Loss of binding to ICAM3 and HIV-1 gp120. 1 Publication1
Mutagenesisi355D → A: Loss of binding to ICAM3 and HIV-1 gp120. 1 Publication1
Mutagenesisi365N → D: Loss of binding to ICAM3 and HIV-1 gp120. 1 Publication1
Mutagenesisi366D → A: Loss of binding to ICAM3 and HIV-1 gp120. 1 Publication1

Organism-specific databases

DisGeNETi30835.
MalaCardsiCD209.
MIMi604672. gene+phenotype.
607948. phenotype.
614371. phenotype.
OpenTargetsiENSG00000090659.
PharmGKBiPA26199.

Chemistry databases

ChEMBLiCHEMBL1795114.

Polymorphism and mutation databases

BioMutaiCD209.
DMDMi46396012.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000465951 – 404CD209 antigenAdd BLAST404

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi80N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi256 ↔ 267
Disulfide bondi284 ↔ 377
Disulfide bondi356 ↔ 369

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9NNX6.
PeptideAtlasiQ9NNX6.
PRIDEiQ9NNX6.

2D gel databases

REPRODUCTION-2DPAGEQ9NNX6.

PTM databases

iPTMnetiQ9NNX6.
PhosphoSitePlusiQ9NNX6.

Expressioni

Tissue specificityi

Predominantly expressed in dendritic cells and in DC-residing tissues. Also found in placental macrophages, endothelial cells of placental vascular channels, peripheral blood mononuclear cells, and THP-1 monocytes.2 Publications

Gene expression databases

BgeeiENSG00000090659.
ExpressionAtlasiQ9NNX6. baseline and differential.
GenevisibleiQ9NNX6. HS.

Organism-specific databases

HPAiCAB032436.
CAB033831.

Interactioni

Subunit structurei

Homotetramer. Interacts with C1QBP; the interaction is indicative for a C1q:C1QBP:CD209 signaling complex. Interacts with ICAM2 and ICAM3 by binding to mannose-like carbohydrates. Interacts (via C-type lectin domain) with CEACAM1 (via Lewis X moieties); this interaction is regulated by the glycosylation pattern of CEACAM1 on cell types and regulates contact between dendritic cells and neutrophils (PubMed:16246332).6 Publications
(Microbial infection) Interacts with HIV-1 and HIV-2 gp120 (PubMed:11799126, PubMed:12502850, PubMed:1518869).3 Publications
(Microbial infection) Interacts with ebolavirus envelope glycoproteins (PubMed:12502850, PubMed:12504546).2 Publications
(Microbial infection) Interacts with cytomegalovirus gB protein (PubMed:12433371, PubMed:22496863).2 Publications
(Microbial infection) Interacts with HCV E2 protein (PubMed:15371595, PubMed:16816373).2 Publications
(Microbial infection) Interacts with dengue virus major envelope protein E.1 Publication
(Microbial infection) Interacts with measles hemagglutinin.1 Publication
(Microbial infection) Interacts with herpes simplex virus 1 surface proteins.1 Publication
(Microbial infection) Interacts with Influenzavirus A hemagglutinin.1 Publication
(Microbial infection) Interacts with SARS coronavirus glycoprotein.1 Publication
(Microbial infection) Interacts with Japanese encephalitis virus E protein.1 Publication
(Microbial infection) Interacts with Lassa virus Glycoprotein.1 Publication
(Microbial infection) Interacts with marburg virus glycoprotein.1 Publication
(Microbial infection) Interacts with Respiratory syncytial virus glycoprotein G.1 Publication
(Microbial infection) Interacts with Rift valley fever virus and uukuniemi virus envelope glycoprotein.1 Publication
(Microbial infection) Interacts with west-nile virus envelope glycoprotein.1 Publication
(Microbial infection) Interacts with whole M.bovis cells in a Ca2+-dependent and independent manner; in vitro experiments suggest it interacts with CH60.1 (groL1), DnaK, GADPH (gap) and LrpG (PubMed:21203928).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q034632EBI-9257341,EBI-9257330From a different organism.
VAC14Q08AM63EBI-9257341,EBI-2107455

Protein-protein interaction databases

BioGridi119051. 14 interactors.
DIPiDIP-60629N.
IntActiQ9NNX6. 2 interactors.
MINTiMINT-5201078.
STRINGi9606.ENSP00000315477.

Chemistry databases

BindingDBiQ9NNX6.

Structurei

Secondary structure

1404
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi261 – 263Combined sources3
Beta strandi266 – 270Combined sources5
Helixi277 – 286Combined sources10
Helixi297 – 310Combined sources14
Beta strandi314 – 323Combined sources10
Beta strandi326 – 329Combined sources4
Helixi337 – 342Combined sources6
Beta strandi356 – 360Combined sources5
Beta strandi363 – 367Combined sources5
Beta strandi373 – 380Combined sources8
Turni381 – 383Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K9IX-ray2.50A/B/C/D/E/F/G/H/I/J250-404[»]
1SL4X-ray1.55A250-404[»]
1SL5X-ray1.80A250-388[»]
2B6Belectron microscopy25.00D251-404[»]
2IT5X-ray2.40A250-388[»]
2IT6X-ray1.95A250-404[»]
2XR5X-ray1.42A254-404[»]
2XR6X-ray1.35A250-404[»]
ProteinModelPortaliQ9NNX6.
SMRiQ9NNX6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NNX6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati96 – 1181Add BLAST23
Repeati119 – 1412Add BLAST23
Repeati142 – 1643Add BLAST23
Repeati165 – 1874Add BLAST23
Repeati188 – 2105Add BLAST23
Repeati211 – 2336Add BLAST23
Repeati234 – 2577Add BLAST24
Domaini263 – 378C-type lectinPROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni96 – 2577 X approximate tandem repeatsAdd BLAST162

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi14 – 15Endocytosis signal2
Motifi16 – 18Endocytosis signalSequence analysis3
Motifi31 – 34Endocytosis signalSequence analysis4

Domaini

The tandem repeat domain, also called neck domain, mediates oligomerization.

Sequence similaritiesi

Contains 1 C-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00760000118924.
HOVERGENiHBG050992.
InParanoidiQ9NNX6.
KOiK06563.
OMAiNLAKFWI.
OrthoDBiEOG091G0G9W.
PhylomeDBiQ9NNX6.
TreeFamiTF333341.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequences (12)i

Sequence statusi: Complete.

This entry describes 12 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist. Several splicing events may be used independently in a modular way. Deletion of the transmembrane domain encoding exon through alternative splicing produces soluble isoforms.1 Publication
Isoform 1 (identifier: Q9NNX6-1) [UniParc]FASTAAdd to basket
Also known as: mDC-SIGN1A type I

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSDSKEPRLQ QLGLLEEEQL RGLGFRQTRG YKSLAGCLGH GPLVLQLLSF
60 70 80 90 100
TLLAGLLVQV SKVPSSISQE QSRQDAIYQN LTQLKAAVGE LSEKSKLQEI
110 120 130 140 150
YQELTQLKAA VGELPEKSKL QEIYQELTRL KAAVGELPEK SKLQEIYQEL
160 170 180 190 200
TWLKAAVGEL PEKSKMQEIY QELTRLKAAV GELPEKSKQQ EIYQELTRLK
210 220 230 240 250
AAVGELPEKS KQQEIYQELT RLKAAVGELP EKSKQQEIYQ ELTQLKAAVE
260 270 280 290 300
RLCHPCPWEW TFFQGNCYFM SNSQRNWHDS ITACKEVGAQ LVVIKSAEEQ
310 320 330 340 350
NFLQLQSSRS NRFTWMGLSD LNQEGTWQWV DGSPLLPSFK QYWNRGEPNN
360 370 380 390 400
VGEEDCAEFS GNGWNDDKCN LAKFWICKKS AASCSRDEEQ FLSPAPATPN

PPPA
Length:404
Mass (Da):45,775
Last modified:October 1, 2000 - v1
Checksum:iA23FA246014533C0
GO
Isoform 2 (identifier: Q9NNX6-2) [UniParc]FASTAAdd to basket
Also known as: mDC-SIGN1A type II

The sequence of this isoform differs from the canonical sequence as follows:
     301-306: Missing.

Show »
Length:398
Mass (Da):45,031
Checksum:iD925764886701D2E
GO
Isoform 3 (identifier: Q9NNX6-3) [UniParc]FASTAAdd to basket
Also known as: mDC-SIGN1A type III

The sequence of this isoform differs from the canonical sequence as follows:
     158-249: Missing.

Show »
Length:312
Mass (Da):35,236
Checksum:iE915D23CB096AA44
GO
Isoform 4 (identifier: Q9NNX6-4) [UniParc]FASTAAdd to basket
Also known as: mDC-SIGN1A type IV

The sequence of this isoform differs from the canonical sequence as follows:
     74-309: Missing.

Show »
Length:168
Mass (Da):18,646
Checksum:i901718CE96B9F59C
GO
Isoform 5 (identifier: Q9NNX6-5) [UniParc]FASTAAdd to basket
Also known as: mDC-SIGN1B type I

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSDSKEPRLQQLGLL → MASACPGSDFTSIHS

Show »
Length:404
Mass (Da):45,571
Checksum:iD4D570727D9DCC30
GO
Isoform 6 (identifier: Q9NNX6-6) [UniParc]FASTAAdd to basket
Also known as: sDC-SIGN1A type I

The sequence of this isoform differs from the canonical sequence as follows:
     36-59: Missing.

Show »
Length:380
Mass (Da):43,330
Checksum:iBCF9CC45ABEF6B02
GO
Isoform 7 (identifier: Q9NNX6-7) [UniParc]FASTAAdd to basket
Also known as: sDC-SIGN1A type II

The sequence of this isoform differs from the canonical sequence as follows:
     16-59: Missing.

Show »
Length:360
Mass (Da):41,009
Checksum:i6ABE2B9AAEDFAAA8
GO
Isoform 8 (identifier: Q9NNX6-8) [UniParc]FASTAAdd to basket
Also known as: sDC-SIGN1A type III

The sequence of this isoform differs from the canonical sequence as follows:
     16-59: Missing.
     142-233: Missing.

Show »
Length:268
Mass (Da):30,427
Checksum:i113E1ED1B5748693
GO
Isoform 9 (identifier: Q9NNX6-9) [UniParc]FASTAAdd to basket
Also known as: sDC-SIGN1A type IV

The sequence of this isoform differs from the canonical sequence as follows:
     30-34: GYKSL → RNQKC
     35-404: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:34
Mass (Da):4,046
Checksum:i51F5A6911CDAC150
GO
Isoform 10 (identifier: Q9NNX6-10) [UniParc]FASTAAdd to basket
Also known as: sDC-SIGN1B type I

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSDSKEPRLQQLGLL → MASACPGSDFTSIHS
     36-59: Missing.

Show »
Length:380
Mass (Da):43,126
Checksum:iF3D098F9FB7D044B
GO
Isoform 11 (identifier: Q9NNX6-11) [UniParc]FASTAAdd to basket
Also known as: sDC-SIGN1B type II

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSDSKEPRLQQLGLL → MASACPGSDFTSIHS
     36-59: Missing.
     191-236: Missing.

Show »
Length:334
Mass (Da):37,844
Checksum:i8E796FC4111C86BF
GO
Isoform 12 (identifier: Q9NNX6-12) [UniParc]FASTAAdd to basket
Also known as: sDC-SIGN1B type III

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSDSKEPRLQQLGLL → MASACPGSDFTSIHS
     36-59: Missing.
     301-321: NFLQLQSSRSNRFTWMGLSDL → LQAVLEQRRAQQRWGGRLRGI
     322-404: Missing.

Show »
Length:297
Mass (Da):33,874
Checksum:iC8C0951B915FC5BF
GO

Sequence cautioni

The sequence AAK91858 differs from that shown. Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti152W → Q in AAK91848 (PubMed:11337487).Curated1

Polymorphismi

Genetic variations in the CD209 promoter determine M.tuberculosis susceptibility [MIMi:607948] (PubMed:16379498).1 Publication
Genetic variations in CD209 may influence susceptibility or resistance to dengue virus infection, as well as disease progression and severity [MIMi:614371]. A promoter polymorphism in the CD209 gene is associated with protection from dengue fever, but not dengue hemorrhagic fever.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_050104168E → D.Corresponds to variant rs11465377dbSNPEnsembl.1
Natural variantiVAR_036689214E → D.Corresponds to variant rs11465377dbSNPEnsembl.1
Natural variantiVAR_036690242L → V.Corresponds to variant rs11465380dbSNPEnsembl.1
Natural variantiVAR_050105382A → S.Corresponds to variant rs11465393dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0100371 – 15MSDSK…QLGLL → MASACPGSDFTSIHS in isoform 5, isoform 10, isoform 11 and isoform 12. 2 PublicationsAdd BLAST15
Alternative sequenceiVSP_01003816 – 59Missing in isoform 7 and isoform 8. 1 PublicationAdd BLAST44
Alternative sequenceiVSP_01003930 – 34GYKSL → RNQKC in isoform 9. 1 Publication5
Alternative sequenceiVSP_01004035 – 404Missing in isoform 9. 1 PublicationAdd BLAST370
Alternative sequenceiVSP_01004136 – 59Missing in isoform 6, isoform 10, isoform 11 and isoform 12. 2 PublicationsAdd BLAST24
Alternative sequenceiVSP_01004274 – 309Missing in isoform 4. 1 PublicationAdd BLAST236
Alternative sequenceiVSP_010043142 – 233Missing in isoform 8. 1 PublicationAdd BLAST92
Alternative sequenceiVSP_010044158 – 249Missing in isoform 3. 1 PublicationAdd BLAST92
Alternative sequenceiVSP_010047191 – 236Missing in isoform 11. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_010048301 – 321NFLQL…GLSDL → LQAVLEQRRAQQRWGGRLRG I in isoform 12. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_010049301 – 306Missing in isoform 2. 1 Publication6
Alternative sequenceiVSP_010050322 – 404Missing in isoform 12. 1 PublicationAdd BLAST83

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98457 mRNA. Translation: AAF77072.1.
AF209479 Genomic DNA. Translation: AAG13814.1.
AF290886 mRNA. Translation: AAK20997.1.
AY042221 mRNA. Translation: AAK91846.1.
AY042222 mRNA. Translation: AAK91847.1.
AY042223 mRNA. Translation: AAK91848.1.
AY042224 mRNA. Translation: AAK91849.1.
AY042225 mRNA. Translation: AAK91850.1.
AY042226 mRNA. Translation: AAK91851.1.
AY042227 mRNA. Translation: AAK91852.1.
AY042228 mRNA. Translation: AAK91853.1.
AY042229 mRNA. Translation: AAK91854.1.
AY042230 mRNA. Translation: AAK91855.1.
AY042231 mRNA. Translation: AAK91856.1.
AY042232 mRNA. Translation: AAK91857.1.
AY042233 mRNA. Translation: AAK91858.1. Sequence problems.
AK293089 mRNA. Translation: BAF85778.1.
AC008763 Genomic DNA. No translation available.
AC008812 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW68991.1.
CH471139 Genomic DNA. Translation: EAW68993.1.
CH471139 Genomic DNA. Translation: EAW68997.1.
CH471139 Genomic DNA. Translation: EAW68998.1.
BC110615 mRNA. Translation: AAI10616.1.
CCDSiCCDS12186.1. [Q9NNX6-1]
CCDS45949.1. [Q9NNX6-7]
CCDS45950.1. [Q9NNX6-6]
CCDS45951.1. [Q9NNX6-2]
CCDS45952.1. [Q9NNX6-3]
CCDS59344.1. [Q9NNX6-8]
PIRiA46274.
RefSeqiNP_001138365.1. NM_001144893.1.
NP_001138366.1. NM_001144894.1. [Q9NNX6-7]
NP_001138367.1. NM_001144895.1. [Q9NNX6-3]
NP_001138368.1. NM_001144896.1. [Q9NNX6-6]
NP_001138369.1. NM_001144897.1. [Q9NNX6-2]
NP_066978.1. NM_021155.3. [Q9NNX6-1]
UniGeneiHs.278694.

Genome annotation databases

EnsembliENST00000204801; ENSP00000204801; ENSG00000090659. [Q9NNX6-7]
ENST00000315591; ENSP00000315407; ENSG00000090659. [Q9NNX6-6]
ENST00000315599; ENSP00000315477; ENSG00000090659. [Q9NNX6-1]
ENST00000354397; ENSP00000346373; ENSG00000090659. [Q9NNX6-2]
ENST00000394161; ENSP00000377716; ENSG00000090659. [Q9NNX6-4]
ENST00000601256; ENSP00000470658; ENSG00000090659. [Q9NNX6-12]
ENST00000601951; ENSP00000468827; ENSG00000090659. [Q9NNX6-10]
ENST00000602261; ENSP00000471137; ENSG00000090659. [Q9NNX6-3]
GeneIDi30835.
KEGGihsa:30835.
UCSCiuc002mhr.3. human. [Q9NNX6-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

DC-SIGN entry

Functional Glycomics Gateway - Glycan Binding

DC-SIGN

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98457 mRNA. Translation: AAF77072.1.
AF209479 Genomic DNA. Translation: AAG13814.1.
AF290886 mRNA. Translation: AAK20997.1.
AY042221 mRNA. Translation: AAK91846.1.
AY042222 mRNA. Translation: AAK91847.1.
AY042223 mRNA. Translation: AAK91848.1.
AY042224 mRNA. Translation: AAK91849.1.
AY042225 mRNA. Translation: AAK91850.1.
AY042226 mRNA. Translation: AAK91851.1.
AY042227 mRNA. Translation: AAK91852.1.
AY042228 mRNA. Translation: AAK91853.1.
AY042229 mRNA. Translation: AAK91854.1.
AY042230 mRNA. Translation: AAK91855.1.
AY042231 mRNA. Translation: AAK91856.1.
AY042232 mRNA. Translation: AAK91857.1.
AY042233 mRNA. Translation: AAK91858.1. Sequence problems.
AK293089 mRNA. Translation: BAF85778.1.
AC008763 Genomic DNA. No translation available.
AC008812 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW68991.1.
CH471139 Genomic DNA. Translation: EAW68993.1.
CH471139 Genomic DNA. Translation: EAW68997.1.
CH471139 Genomic DNA. Translation: EAW68998.1.
BC110615 mRNA. Translation: AAI10616.1.
CCDSiCCDS12186.1. [Q9NNX6-1]
CCDS45949.1. [Q9NNX6-7]
CCDS45950.1. [Q9NNX6-6]
CCDS45951.1. [Q9NNX6-2]
CCDS45952.1. [Q9NNX6-3]
CCDS59344.1. [Q9NNX6-8]
PIRiA46274.
RefSeqiNP_001138365.1. NM_001144893.1.
NP_001138366.1. NM_001144894.1. [Q9NNX6-7]
NP_001138367.1. NM_001144895.1. [Q9NNX6-3]
NP_001138368.1. NM_001144896.1. [Q9NNX6-6]
NP_001138369.1. NM_001144897.1. [Q9NNX6-2]
NP_066978.1. NM_021155.3. [Q9NNX6-1]
UniGeneiHs.278694.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K9IX-ray2.50A/B/C/D/E/F/G/H/I/J250-404[»]
1SL4X-ray1.55A250-404[»]
1SL5X-ray1.80A250-388[»]
2B6Belectron microscopy25.00D251-404[»]
2IT5X-ray2.40A250-388[»]
2IT6X-ray1.95A250-404[»]
2XR5X-ray1.42A254-404[»]
2XR6X-ray1.35A250-404[»]
ProteinModelPortaliQ9NNX6.
SMRiQ9NNX6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119051. 14 interactors.
DIPiDIP-60629N.
IntActiQ9NNX6. 2 interactors.
MINTiMINT-5201078.
STRINGi9606.ENSP00000315477.

Chemistry databases

BindingDBiQ9NNX6.
ChEMBLiCHEMBL1795114.

PTM databases

iPTMnetiQ9NNX6.
PhosphoSitePlusiQ9NNX6.

Polymorphism and mutation databases

BioMutaiCD209.
DMDMi46396012.

2D gel databases

REPRODUCTION-2DPAGEQ9NNX6.

Proteomic databases

PaxDbiQ9NNX6.
PeptideAtlasiQ9NNX6.
PRIDEiQ9NNX6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000204801; ENSP00000204801; ENSG00000090659. [Q9NNX6-7]
ENST00000315591; ENSP00000315407; ENSG00000090659. [Q9NNX6-6]
ENST00000315599; ENSP00000315477; ENSG00000090659. [Q9NNX6-1]
ENST00000354397; ENSP00000346373; ENSG00000090659. [Q9NNX6-2]
ENST00000394161; ENSP00000377716; ENSG00000090659. [Q9NNX6-4]
ENST00000601256; ENSP00000470658; ENSG00000090659. [Q9NNX6-12]
ENST00000601951; ENSP00000468827; ENSG00000090659. [Q9NNX6-10]
ENST00000602261; ENSP00000471137; ENSG00000090659. [Q9NNX6-3]
GeneIDi30835.
KEGGihsa:30835.
UCSCiuc002mhr.3. human. [Q9NNX6-1]

Organism-specific databases

CTDi30835.
DisGeNETi30835.
GeneCardsiCD209.
HGNCiHGNC:1641. CD209.
HPAiCAB032436.
CAB033831.
MalaCardsiCD209.
MIMi604672. gene+phenotype.
607948. phenotype.
614371. phenotype.
neXtProtiNX_Q9NNX6.
OpenTargetsiENSG00000090659.
PharmGKBiPA26199.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4297. Eukaryota.
ENOG410XPJ1. LUCA.
GeneTreeiENSGT00760000118924.
HOVERGENiHBG050992.
InParanoidiQ9NNX6.
KOiK06563.
OMAiNLAKFWI.
OrthoDBiEOG091G0G9W.
PhylomeDBiQ9NNX6.
TreeFamiTF333341.

Enzyme and pathway databases

ReactomeiR-HSA-5621575. CD209 (DC-SIGN) signaling.

Miscellaneous databases

EvolutionaryTraceiQ9NNX6.
GeneWikiiDC-SIGN.
GenomeRNAii30835.
PROiQ9NNX6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000090659.
ExpressionAtlasiQ9NNX6. baseline and differential.
GenevisibleiQ9NNX6. HS.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCD209_HUMAN
AccessioniPrimary (citable) accession number: Q9NNX6
Secondary accession number(s): A8KAM4
, A8MVQ9, G5E9C4, Q2TB19, Q96QP7, Q96QP8, Q96QP9, Q96QQ0, Q96QQ1, Q96QQ2, Q96QQ3, Q96QQ4, Q96QQ5, Q96QQ6, Q96QQ7, Q96QQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

In vitro, is a receptor for HIV-1 and transmits HIV-1 either in trans without DC infection, or in cis following a DC infection to permissive T-cells to induce a robust infection. Bound HIV-1 remains infectious over a prolonged period of time and it is proposed that bound HIV-1 is not degraded but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the HIV-1 infectious potential during transport by DCs from the periphery to lymphoid organs.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.