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Q9NNX6

- CD209_HUMAN

UniProt

Q9NNX6 - CD209_HUMAN

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Protein
CD209 antigen
Gene
CD209, CLEC4L
Organism
Homo sapiens (Human)
Status
Reviewed - 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. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, cytomegalovirus gB, HCV E2, dengue virus gE, 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.6 Publications
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.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi347 – 3471Calcium
Metal bindingi349 – 3491Calcium
Metal bindingi351 – 3511Calcium; via carbonyl oxygen
Metal bindingi354 – 3541Calcium
Metal bindingi365 – 3651Calcium
Metal bindingi366 – 3661Calcium

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB
  2. mannose binding Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. peptide antigen binding Source: UniProtKB
  5. virion binding Source: UniProtKB

GO - Biological processi

  1. antigen processing and presentation Source: UniProtKB
  2. cell-cell recognition Source: UniProtKB
  3. endocytosis Source: UniProtKB-KW
  4. heterophilic cell-cell adhesion Source: UniProtKB
  5. innate immune response Source: UniProtKB-KW
  6. intracellular signal transduction Source: UniProtKB
  7. intracellular transport of virus Source: UniProtKB
  8. leukocyte cell-cell adhesion Source: UniProtKB
  9. modulation by virus of host morphology or physiology Source: UniProtKB
  10. peptide antigen transport Source: UniProtKB
  11. regulation of T cell proliferation Source: MGI
  12. viral genome replication Source: UniProtKB
  13. virion attachment to host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

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

Keywords - Ligandi

Calcium, Lectin, Mannose-binding, Metal-binding

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
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:1641. CD209.

Subcellular locationi

Isoform 1 : Cell membrane; Single-pass type II membrane protein Inferred 1 Publication
Isoform 2 : Cell membrane; Single-pass type II membrane protein Inferred 1 Publication
Isoform 3 : Cell membrane; Single-pass type II membrane protein Inferred 1 Publication
Isoform 4 : Cell membrane; Single-pass type II membrane protein Inferred 1 Publication
Isoform 5 : Cell membrane; Single-pass type II membrane protein Inferred 1 Publication
Isoform 6 : Secreted Inferred 1 Publication
Isoform 7 : Secreted Inferred 1 Publication
Isoform 8 : Secreted Inferred 1 Publication
Isoform 9 : Secreted Inferred 1 Publication
Isoform 10 : Secreted Inferred 1 Publication
Isoform 11 : Secreted Inferred 1 Publication
Isoform 12 : Secreted Inferred 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3737Cytoplasmic Inferred
Add
BLAST
Transmembranei38 – 5821Helical; Signal-anchor for type II membrane protein; Inferred
Add
BLAST
Topological domaini59 – 404346Extracellular Inferred
Add
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: UniProtKB
  5. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 152LL → AA: Loss of antigen internalization by endocytosis. 1 Publication
Mutagenesisi320 – 3201D → A: Loss of binding to ICAM3 and HIV-1 gp120. 2 Publications
Mutagenesisi324 – 3241E → A: Loss of binding to ICAM3 and HIV-1 gp120. 2 Publications
Mutagenesisi347 – 3471E → Q: Loss of binding to ICAM3 and HIV-1 gp120. 2 Publications
Mutagenesisi349 – 3491N → D: Loss of binding to ICAM3 and HIV-1 gp120. 2 Publications
Mutagenesisi350 – 3501N → A: Loss of binding to ICAM3 and HIV-1 gp120. 2 Publications
Mutagenesisi355 – 3551D → A: Loss of binding to ICAM3 and HIV-1 gp120. 2 Publications
Mutagenesisi365 – 3651N → D: Loss of binding to ICAM3 and HIV-1 gp120. 2 Publications
Mutagenesisi366 – 3661D → A: Loss of binding to ICAM3 and HIV-1 gp120. 2 Publications

Organism-specific databases

MIMi604672. gene+phenotype.
607948. phenotype.
614371. phenotype.
PharmGKBiPA26199.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 404404CD209 antigen
PRO_0000046595Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi80 – 801N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi256 ↔ 267
Disulfide bondi284 ↔ 377
Disulfide bondi356 ↔ 369

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9NNX6.
PRIDEiQ9NNX6.

2D gel databases

REPRODUCTION-2DPAGEQ9NNX6.

PTM databases

PhosphoSiteiQ9NNX6.

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

ArrayExpressiQ9NNX6.
BgeeiQ9NNX6.
GenevestigatoriQ9NNX6.

Organism-specific databases

HPAiCAB032436.
CAB033831.

Interactioni

Subunit structurei

Homotetramer. Binds to many viral surface glycoproteins such as HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus envelope glycoproteins, cytomegalovirus gB, HCV E2 and dengue virus major envelope protein E. Interacts with C1QBP; the interaction is indicative for a C1q:C1QBP:CD209 signaling complex.9 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi119051. 5 interactions.
DIPiDIP-60629N.
IntActiQ9NNX6. 1 interaction.
MINTiMINT-5201078.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi261 – 2633
Beta strandi266 – 2705
Helixi277 – 28610
Helixi297 – 31014
Beta strandi314 – 32310
Beta strandi326 – 3294
Helixi337 – 3426
Beta strandi356 – 3605
Beta strandi363 – 3675
Beta strandi373 – 3808
Turni381 – 3833

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 59-197, 207-383.

Miscellaneous databases

EvolutionaryTraceiQ9NNX6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati96 – 118231
Add
BLAST
Repeati119 – 141232
Add
BLAST
Repeati142 – 164233
Add
BLAST
Repeati165 – 187234
Add
BLAST
Repeati188 – 210235
Add
BLAST
Repeati211 – 233236
Add
BLAST
Repeati234 – 257247
Add
BLAST
Domaini263 – 378116C-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 2571627 X approximate tandem repeats
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi14 – 152Endocytosis signal
Motifi16 – 183Endocytosis signal Reviewed prediction
Motifi31 – 344Endocytosis signal Reviewed prediction

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG311341.
HOVERGENiHBG050992.
KOiK06563.
OMAiDSKEPRL.
OrthoDBiEOG7DFXC9.
PhylomeDBiQ9NNX6.
TreeFamiTF333341.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_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. Align

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.

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

MSDSKEPRLQ QLGLLEEEQL RGLGFRQTRG YKSLAGCLGH GPLVLQLLSF    50
TLLAGLLVQV SKVPSSISQE QSRQDAIYQN LTQLKAAVGE LSEKSKLQEI 100
YQELTQLKAA VGELPEKSKL QEIYQELTRL KAAVGELPEK SKLQEIYQEL 150
TWLKAAVGEL PEKSKMQEIY QELTRLKAAV GELPEKSKQQ EIYQELTRLK 200
AAVGELPEKS KQQEIYQELT RLKAAVGELP EKSKQQEIYQ ELTQLKAAVE 250
RLCHPCPWEW TFFQGNCYFM SNSQRNWHDS ITACKEVGAQ LVVIKSAEEQ 300
NFLQLQSSRS NRFTWMGLSD LNQEGTWQWV DGSPLLPSFK QYWNRGEPNN 350
VGEEDCAEFS GNGWNDDKCN LAKFWICKKS AASCSRDEEQ FLSPAPATPN 400
PPPA 404
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 AAK91858.1 differs from that shown. Reason: Aberrant splicing.

Polymorphismi

Genetic variations in CD209 determine Mycobacterium tuberculosis susceptibility [MIMi:607948].
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti168 – 1681E → D.
Corresponds to variant rs11465377 [ dbSNP | Ensembl ].
VAR_050104
Natural varianti214 – 2141E → D.
Corresponds to variant rs11465377 [ dbSNP | Ensembl ].
VAR_036689
Natural varianti242 – 2421L → V.
Corresponds to variant rs11465380 [ dbSNP | Ensembl ].
VAR_036690
Natural varianti382 – 3821A → S.
Corresponds to variant rs11465393 [ dbSNP | Ensembl ].
VAR_050105

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515MSDSK…QLGLL → MASACPGSDFTSIHS in isoform 5, isoform 10, isoform 11 and isoform 12.
VSP_010037Add
BLAST
Alternative sequencei16 – 5944Missing in isoform 7 and isoform 8.
VSP_010038Add
BLAST
Alternative sequencei30 – 345GYKSL → RNQKC in isoform 9.
VSP_010039
Alternative sequencei35 – 404370Missing in isoform 9.
VSP_010040Add
BLAST
Alternative sequencei36 – 5924Missing in isoform 6, isoform 10, isoform 11 and isoform 12.
VSP_010041Add
BLAST
Alternative sequencei74 – 309236Missing in isoform 4.
VSP_010042Add
BLAST
Alternative sequencei142 – 23392Missing in isoform 8.
VSP_010043Add
BLAST
Alternative sequencei158 – 24992Missing in isoform 3.
VSP_010044Add
BLAST
Alternative sequencei191 – 23646Missing in isoform 11.
VSP_010047Add
BLAST
Alternative sequencei301 – 32121NFLQL…GLSDL → LQAVLEQRRAQQRWGGRLRG I in isoform 12.
VSP_010048Add
BLAST
Alternative sequencei301 – 3066Missing in isoform 2.
VSP_010049
Alternative sequencei322 – 40483Missing in isoform 12.
VSP_010050Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521W → Q in AAK91848. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
ENST00000301357; ENSP00000301357; ENSG00000090659. [Q9NNX6-8]
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.
UCSCiuc002mhq.2. human. [Q9NNX6-5]
uc002mhr.2. human. [Q9NNX6-10]
uc002mhs.2. human. [Q9NNX6-11]
uc002mht.2. human. [Q9NNX6-1]
uc002mhu.2. human.
uc002mhv.2. human. [Q9NNX6-6]
uc002mhx.2. human. [Q9NNX6-7]
uc010dvp.2. human. [Q9NNX6-12]
uc010dvq.2. human. [Q9NNX6-2]
uc010dvr.2. human. [Q9NNX6-4]

Polymorphism databases

DMDMi46396012.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS12186.1. [Q9NNX6-1 ]
CCDS45949.1. [Q9NNX6-7 ]
CCDS45950.1. [Q9NNX6-6 ]
CCDS45951.1. [Q9NNX6-2 ]
CCDS45952.1. [Q9NNX6-3 ]
CCDS59344.1. [Q9NNX6-8 ]
PIRi A46274.
RefSeqi NP_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 ]
UniGenei Hs.278694.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K9I X-ray 2.50 A/B/C/D/E/F/G/H/I/J 250-404 [» ]
1SL4 X-ray 1.55 A 250-404 [» ]
1SL5 X-ray 1.80 A 250-388 [» ]
2B6B electron microscopy 25.00 D 251-404 [» ]
2IT5 X-ray 2.40 A 250-388 [» ]
2IT6 X-ray 1.95 A 250-404 [» ]
2XR5 X-ray 1.42 A 254-404 [» ]
2XR6 X-ray 1.35 A 250-404 [» ]
ProteinModelPortali Q9NNX6.
SMRi Q9NNX6. Positions 59-197, 207-383.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119051. 5 interactions.
DIPi DIP-60629N.
IntActi Q9NNX6. 1 interaction.
MINTi MINT-5201078.

Chemistry

ChEMBLi CHEMBL1795114.

PTM databases

PhosphoSitei Q9NNX6.

Polymorphism databases

DMDMi 46396012.

2D gel databases

REPRODUCTION-2DPAGE Q9NNX6.

Proteomic databases

PaxDbi Q9NNX6.
PRIDEi Q9NNX6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000204801 ; ENSP00000204801 ; ENSG00000090659 . [Q9NNX6-7 ]
ENST00000301357 ; ENSP00000301357 ; ENSG00000090659 . [Q9NNX6-8 ]
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 ]
GeneIDi 30835.
KEGGi hsa:30835.
UCSCi uc002mhq.2. human. [Q9NNX6-5 ]
uc002mhr.2. human. [Q9NNX6-10 ]
uc002mhs.2. human. [Q9NNX6-11 ]
uc002mht.2. human. [Q9NNX6-1 ]
uc002mhu.2. human.
uc002mhv.2. human. [Q9NNX6-6 ]
uc002mhx.2. human. [Q9NNX6-7 ]
uc010dvp.2. human. [Q9NNX6-12 ]
uc010dvq.2. human. [Q9NNX6-2 ]
uc010dvr.2. human. [Q9NNX6-4 ]

Organism-specific databases

CTDi 30835.
GeneCardsi GC19M007804.
HGNCi HGNC:1641. CD209.
HPAi CAB032436.
CAB033831.
MIMi 604672. gene+phenotype.
607948. phenotype.
614371. phenotype.
neXtProti NX_Q9NNX6.
PharmGKBi PA26199.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG311341.
HOVERGENi HBG050992.
KOi K06563.
OMAi DSKEPRL.
OrthoDBi EOG7DFXC9.
PhylomeDBi Q9NNX6.
TreeFami TF333341.

Miscellaneous databases

EvolutionaryTracei Q9NNX6.
GeneWikii DC-SIGN.
GenomeRNAii 30835.
NextBioi 52950.
PROi Q9NNX6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NNX6.
Bgeei Q9NNX6.
Genevestigatori Q9NNX6.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view ]
Pfami PF00059. Lectin_C. 1 hit.
[Graphical view ]
SMARTi SM00034. CLECT. 1 hit.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
PROSITEi PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp 120."
    Curtis B.M., Scharnowske S., Watson A.J.
    Proc. Natl. Acad. Sci. U.S.A. 89:8356-8360(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH HIV-1 GP120.
    Tissue: Placenta.
  2. "DC-SIGN, a related gene, DC-SIGNR, and CD23 form a cluster on 19p13."
    Soilleux E.J., Barten R., Trowsdale J.
    J. Immunol. 165:2937-2942(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  3. "A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection."
    Bashirova A.A., Geijtenbeek T.B.H., van Duijnhoven G.C.F., van Vliet S.J., Eilering J.B.G., Martin M.P., Wu L., Martin T.D., Viebig N., Knolle P.A., Kewalramani V.N., van Kooyk Y., Carrington M.
    J. Exp. Med. 193:671-678(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  4. "Extensive repertoire of membrane-bound and soluble dendritic cell-specific ICAM-3-grabbing nonintegrin 1 (DC-SIGN1) and DC-SIGN2 isoforms. Inter-individual variation in expression of DC-SIGN transcripts."
    Mummidi S., Catano G., Lam L., Hoefle A., Telles V., Begum K., Jimenez F., Ahuja S.S., Ahuja S.K.
    J. Biol. Chem. 276:33196-33212(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10; 11 AND 12), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Uterus.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
  9. Cited for: FUNCTION, INTERACTION WITH ICAM3.
  10. Cited for: FUNCTION, INTERACTION WITH ICAM2.
  11. "A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands."
    Mitchell D.A., Fadden A.J., Drickamer K.
    J. Biol. Chem. 276:28939-28945(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, LIGAND-BINDING.
  12. "Human cytomegalovirus binding to DC-SIGN is required for dendritic cell infection and target cell trans-infection."
    Halary F., Amara A., Lortat-Jacob H., Messerle M., Delaunay T., Houles C., Fieschi F., Arenzana-Seisdedos F., Moreau J.-F., Dechanet-Merville J.
    Immunity 17:653-664(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CYTOMEGALOVIRUS GLYCOPROTEIN B (GB).
  13. "Identification of different binding sites in the dendritic cell-specific receptor DC-SIGN for intercellular adhesion molecule 3 and HIV-1."
    Geijtenbeek T.B.H., van Duijnhoven G.C.F., van Vliet S.J., Krieger E., Vriend G., Figdor C.G., van Kooyk Y.
    J. Biol. Chem. 277:11314-11320(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ICAM 3 AND HIV-1 GP120, MUTAGENESIS OF ASP-320; GLU-324; GLU-347; ASN-349; ASN-350; ASP-355; ASN-365 AND ASP-366.
  14. "The dendritic cell-specific adhesion receptor DC-SIGN internalizes antigen for presentation to T cells."
    Engering A., Geijtenbeek T.B.H., van Vliet S.J., Wijers M., van Liempt E., Demaurex N., Lanzavecchia A., Fransen J., Figdor C.G., Piguet V., van Kooyk Y.
    J. Immunol. 168:2118-2126(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 14-LEU-LEU-15.
  15. "DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection."
    Kwon D.S., Gregorio G., Bitton N., Hendrickson W.A., Littman D.R.
    Immunity 16:135-144(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE IN HIV-1 INFECTION.
  16. "Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR."
    Lin G., Simmons G., Poehlmann S., Baribaud F., Ni H., Leslie G.J., Haggarty B.S., Bates P., Weissman D., Hoxie J.A., Doms R.W.
    J. Virol. 77:1337-1346(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 GP120; HIV-2 GP120; SIV GP120 AND EBOLA GLYCOPROTEINS.
  17. "Inhibition of human immunodeficiency virus type 1 Env-mediated fusion by DC-SIGN."
    Nobile C., Moris A., Porrot F., Sol-Foulon N., Schwartz O.
    J. Virol. 77:5313-5323(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HIV-1 INFECTION.
  18. "Carbohydrate profiling identifies new pathogens that interact with dendritic cell-specific ICAM-3-grabbing nonintegrin on dendritic cells."
    Appelmelk B.J., van Die I., van Vliet S.J., Vandenbroucke-Grauls C.M., Geijtenbeek T.B.H., van Kooyk Y.
    J. Immunol. 170:1635-1639(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. Cited for: REVIEW ON ROLE IN HIV-1 INFECTION AND ON PATHOGEN BINDING.
  20. "The role of dendritic cell C-type lectin receptors in HIV pathogenesis."
    Turville S., Wilkinson J., Cameron P., Dable J., Cunningham A.L.
    J. Leukoc. Biol. 74:710-718(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN HIV-1 INFECTION.
  21. "L-SIGN (CD209L) and DC-SIGN (CD209) mediate transinfection of liver cells by hepatitis C virus."
    Cormier E.G., Durso R.J., Tsamis F., Boussemart L., Manix C., Olson W.C., Gardner J.P., Dragic T.
    Proc. Natl. Acad. Sci. U.S.A. 101:14067-14072(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCV E2 GLYCOPROTEIN.
  22. Cited for: POLYMORPHISM, INVOLVEMENT IN SUSCEPTIBILITY TO DENGUE VIRUS INFECTION.
  23. "DC-SIGN, C1q, and gC1qR form a trimolecular receptor complex on the surface of monocyte-derived immature dendritic cells."
    Hosszu K.K., Valentino A., Vinayagasundaram U., Vinayagasundaram R., Joyce M.G., Ji Y., Peerschke E.I., Ghebrehiwet B.
    Blood 120:1228-1236(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C1QBP.
  24. "Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR."
    Feinberg H., Mitchell D.A., Drickamer K., Weis W.I.
    Science 294:2163-2166(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 254-382 IN COMPLEX WITH GLCNAC(2)-MAN(3) PENTASACCHARIDE.
  25. "Promoter variation in the DC-SIGN-encoding gene CD209 is associated with tuberculosis."
    Barreiro L.B., Neyrolles O., Babb C.L., Tailleux L., Quach H., McElreavey K., Helden P.D., Hoal E.G., Gicquel B., Quintana-Murci L.
    PLoS Med. 3:230-235(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MYCOBACTERIUM TUBERCULOSIS SUSCEPTIBILITY.

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: September 3, 2014
This is version 133 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

External Data

Dasty 3

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