Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NNX6 (CD209_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CD209
Synonyms:CLEC4L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10 Ref.14 Ref.15 Ref.17 Ref.18

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. Ref.9 Ref.10 Ref.14 Ref.15 Ref.17 Ref.18

Subunit structure

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. Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.21 Ref.23

Subcellular location

Isoform 1: Cell membrane; Single-pass type II membrane protein Probable Ref.1.

Isoform 2: Cell membrane; Single-pass type II membrane protein Probable Ref.1.

Isoform 3: Cell membrane; Single-pass type II membrane protein Probable Ref.1.

Isoform 4: Cell membrane; Single-pass type II membrane protein Probable Ref.1.

Isoform 5: Cell membrane; Single-pass type II membrane protein Probable Ref.1.

Isoform 6: Secreted Probable Ref.1.

Isoform 7: Secreted Probable Ref.1.

Isoform 8: Secreted Probable Ref.1.

Isoform 9: Secreted Probable Ref.1.

Isoform 10: Secreted Probable Ref.1.

Isoform 11: Secreted Probable Ref.1.

Isoform 12: Secreted Probable Ref.1.

Tissue specificity

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. Ref.3 Ref.4

Domain

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

Polymorphism

Genetic variations in CD209 determine Mycobacterium tuberculosis susceptibility [MIM:607948].

Genetic variations in CD209 may influence susceptibility or resistance to dengue virus infection, as well as disease progression and severity [MIM:614371]. A promoter polymorphism in the CD209 gene is associated with protection from dengue fever, but not dengue hemorrhagic fever.

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.

Sequence similarities

Contains 1 C-type lectin domain.

Sequence caution

The sequence AAK91858.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
   Biological processAdaptive immunity
Cell adhesion
Endocytosis
Host-virus interaction
Immunity
Innate immunity
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal-anchor
Transmembrane
Transmembrane helix
   LigandCalcium
Lectin
Mannose-binding
Metal-binding
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation

Non-traceable author statement Ref.4. Source: UniProtKB

cell-cell recognition

Traceable author statement Ref.4. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

heterophilic cell-cell adhesion

Traceable author statement Ref.1. Source: UniProtKB

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Non-traceable author statement Ref.4. Source: UniProtKB

intracellular transport of virus

Traceable author statement Ref.4. Source: UniProtKB

leukocyte cell-cell adhesion

Non-traceable author statement Ref.4. Source: UniProtKB

modulation by virus of host morphology or physiology

Traceable author statement Ref.4. Source: UniProtKB

peptide antigen transport

Non-traceable author statement Ref.4. Source: UniProtKB

regulation of T cell proliferation

Inferred from direct assay PubMed 12456590. Source: MGI

viral genome replication

Non-traceable author statement Ref.4. Source: UniProtKB

virion attachment to host cell

Traceable author statement Ref.4. Source: UniProtKB

   Cellular_componentcytoplasm

Non-traceable author statement Ref.4. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Traceable author statement Ref.1. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbohydrate binding

Non-traceable author statement Ref.4. Source: UniProtKB

mannose binding

Traceable author statement Ref.1. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptide antigen binding

Non-traceable author statement Ref.4. Source: UniProtKB

virion binding

Traceable author statement Ref.4. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]

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)

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.
Isoform 2 (identifier: Q9NNX6-2)

Also known as: mDC-SIGN1A type II;

The sequence of this isoform differs from the canonical sequence as follows:
     301-306: Missing.
Isoform 3 (identifier: Q9NNX6-3)

Also known as: mDC-SIGN1A type III;

The sequence of this isoform differs from the canonical sequence as follows:
     158-249: Missing.
Isoform 4 (identifier: Q9NNX6-4)

Also known as: mDC-SIGN1A type IV;

The sequence of this isoform differs from the canonical sequence as follows:
     74-309: Missing.
Isoform 5 (identifier: Q9NNX6-5)

Also known as: mDC-SIGN1B type I;

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSDSKEPRLQQLGLL → MASACPGSDFTSIHS
Isoform 6 (identifier: Q9NNX6-6)

Also known as: sDC-SIGN1A type I;

The sequence of this isoform differs from the canonical sequence as follows:
     36-59: Missing.
Isoform 7 (identifier: Q9NNX6-7)

Also known as: sDC-SIGN1A type II;

The sequence of this isoform differs from the canonical sequence as follows:
     16-59: Missing.
Isoform 8 (identifier: Q9NNX6-8)

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.
Isoform 9 (identifier: Q9NNX6-9)

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.
Isoform 10 (identifier: Q9NNX6-10)

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.
Isoform 11 (identifier: Q9NNX6-11)

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.
Isoform 12 (identifier: Q9NNX6-12)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 404404CD209 antigen
PRO_0000046595

Regions

Topological domain1 – 3737Cytoplasmic Probable
Transmembrane38 – 5821Helical; Signal-anchor for type II membrane protein; Probable
Topological domain59 – 404346Extracellular Probable
Repeat96 – 118231
Repeat119 – 141232
Repeat142 – 164233
Repeat165 – 187234
Repeat188 – 210235
Repeat211 – 233236
Repeat234 – 257247
Domain263 – 378116C-type lectin
Region96 – 2571627 X approximate tandem repeats
Motif14 – 152Endocytosis signal
Motif16 – 183Endocytosis signal Potential
Motif31 – 344Endocytosis signal Potential

Sites

Metal binding3471Calcium
Metal binding3491Calcium
Metal binding3511Calcium; via carbonyl oxygen
Metal binding3541Calcium
Metal binding3651Calcium
Metal binding3661Calcium

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Potential
Disulfide bond256 ↔ 267
Disulfide bond284 ↔ 377
Disulfide bond356 ↔ 369

Natural variations

Alternative sequence1 – 1515MSDSK…QLGLL → MASACPGSDFTSIHS in isoform 5, isoform 10, isoform 11 and isoform 12.
VSP_010037
Alternative sequence16 – 5944Missing in isoform 7 and isoform 8.
VSP_010038
Alternative sequence30 – 345GYKSL → RNQKC in isoform 9.
VSP_010039
Alternative sequence35 – 404370Missing in isoform 9.
VSP_010040
Alternative sequence36 – 5924Missing in isoform 6, isoform 10, isoform 11 and isoform 12.
VSP_010041
Alternative sequence74 – 309236Missing in isoform 4.
VSP_010042
Alternative sequence142 – 23392Missing in isoform 8.
VSP_010043
Alternative sequence158 – 24992Missing in isoform 3.
VSP_010044
Alternative sequence191 – 23646Missing in isoform 11.
VSP_010047
Alternative sequence301 – 32121NFLQL…GLSDL → LQAVLEQRRAQQRWGGRLRG I in isoform 12.
VSP_010048
Alternative sequence301 – 3066Missing in isoform 2.
VSP_010049
Alternative sequence322 – 40483Missing in isoform 12.
VSP_010050
Natural variant1681E → D.
Corresponds to variant rs11465377 [ dbSNP | Ensembl ].
VAR_050104
Natural variant2141E → D.
Corresponds to variant rs11465377 [ dbSNP | Ensembl ].
VAR_036689
Natural variant2421L → V.
Corresponds to variant rs11465380 [ dbSNP | Ensembl ].
VAR_036690
Natural variant3821A → S.
Corresponds to variant rs11465393 [ dbSNP | Ensembl ].
VAR_050105

Experimental info

Mutagenesis14 – 152LL → AA: Loss of antigen internalization by endocytosis. Ref.14
Mutagenesis3201D → A: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14
Mutagenesis3241E → A: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14
Mutagenesis3471E → Q: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14
Mutagenesis3491N → D: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14
Mutagenesis3501N → A: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14
Mutagenesis3551D → A: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14
Mutagenesis3651N → D: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14
Mutagenesis3661D → A: Loss of binding to ICAM3 and HIV-1 gp120. Ref.13 Ref.14
Sequence conflict1521W → Q in AAK91848. Ref.4

Secondary structure

...................... 404
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (mDC-SIGN1A type I) [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A23FA246014533C0

FASTA40445,775
        10         20         30         40         50         60 
MSDSKEPRLQ QLGLLEEEQL RGLGFRQTRG YKSLAGCLGH GPLVLQLLSF TLLAGLLVQV 

        70         80         90        100        110        120 
SKVPSSISQE QSRQDAIYQN LTQLKAAVGE LSEKSKLQEI YQELTQLKAA VGELPEKSKL 

       130        140        150        160        170        180 
QEIYQELTRL KAAVGELPEK SKLQEIYQEL TWLKAAVGEL PEKSKMQEIY QELTRLKAAV 

       190        200        210        220        230        240 
GELPEKSKQQ EIYQELTRLK AAVGELPEKS KQQEIYQELT RLKAAVGELP EKSKQQEIYQ 

       250        260        270        280        290        300 
ELTQLKAAVE RLCHPCPWEW TFFQGNCYFM SNSQRNWHDS ITACKEVGAQ LVVIKSAEEQ 

       310        320        330        340        350        360 
NFLQLQSSRS NRFTWMGLSD LNQEGTWQWV DGSPLLPSFK QYWNRGEPNN VGEEDCAEFS 

       370        380        390        400 
GNGWNDDKCN LAKFWICKKS AASCSRDEEQ FLSPAPATPN PPPA 

« Hide

Isoform 2 (mDC-SIGN1A type II) [UniParc].

Checksum: D925764886701D2E
Show »

FASTA39845,031
Isoform 3 (mDC-SIGN1A type III) [UniParc].

Checksum: E915D23CB096AA44
Show »

FASTA31235,236
Isoform 4 (mDC-SIGN1A type IV) [UniParc].

Checksum: 901718CE96B9F59C
Show »

FASTA16818,646
Isoform 5 (mDC-SIGN1B type I) [UniParc].

Checksum: D4D570727D9DCC30
Show »

FASTA40445,571
Isoform 6 (sDC-SIGN1A type I) [UniParc].

Checksum: BCF9CC45ABEF6B02
Show »

FASTA38043,330
Isoform 7 (sDC-SIGN1A type II) [UniParc].

Checksum: 6ABE2B9AAEDFAAA8
Show »

FASTA36041,009
Isoform 8 (sDC-SIGN1A type III) [UniParc].

Checksum: 113E1ED1B5748693
Show »

FASTA26830,427
Isoform 9 (sDC-SIGN1A type IV) [UniParc].

Checksum: 51F5A6911CDAC150
Show »

FASTA344,046
Isoform 10 (sDC-SIGN1B type I) [UniParc].

Checksum: F3D098F9FB7D044B
Show »

FASTA38043,126
Isoform 11 (sDC-SIGN1B type II) [UniParc].

Checksum: 8E796FC4111C86BF
Show »

FASTA33437,844
Isoform 12 (sDC-SIGN1B type III) [UniParc].

Checksum: C8C0951B915FC5BF
Show »

FASTA29733,874

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells."
Geijtenbeek T.B.H., Kwon D.S., Torensma R., van Vliet S.J., van Duijnhoven G.C.F., Middel J., Cornelissen I.L., Nottet H.S., Kewalramani V.N., Littman D.R., Figdor C.G., van Kooyk Y.
Cell 100:587-597(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ICAM3.
[10]"DC-SIGN-ICAM-2 interaction mediates dendritic cell trafficking."
Geijtenbeek T.B.H., Krooshoop D.J., Bleijs D.A., van Vliet S.J., van Duijnhoven G.C.F., Grabovsky V., Alon R., Figdor C.G., van Kooyk Y.
Nat. Immunol. 1:353-357(2000) [PubMed] [Europe PMC] [Abstract]
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]"DC-SIGN: escape mechanism for pathogens."
van Kooyk Y., Geijtenbeek T.B.H.
Nat. Rev. Immunol. 3:697-709(2003) [PubMed] [Europe PMC] [Abstract]
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]"A variant in the CD209 promoter is associated with severity of dengue disease."
Sakuntabhai A., Turbpaiboon C., Casademont I., Chuansumrit A., Lowhnoo T., Kajaste-Rudnitski A., Kalayanarooj S.M., Tangnararatchakit K., Tangthawornchaikul N., Vasanawathana S., Chaiyaratana W., Yenchitsomanus P.T., Suriyaphol P., Avirutnan P., Chokephaibulkit K., Matsuda F., Yoksan S., Jacob Y. expand/collapse author list , Lathrop G.M., Malasit P., Despres P., Julier C.
Nat. Genet. 37:507-513(2005) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS12186.1. [Q9NNX6-1]
CCDS45949.1. [Q9NNX6-7]
CCDS45950.1. [Q9NNX6-6]
CCDS45951.1. [Q9NNX6-2]
CCDS45952.1. [Q9NNX6-3]
CCDS59344.1. [Q9NNX6-8]
PIRA46274.
RefSeqNP_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]
UniGeneHs.278694.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9NNX6.
SMRQ9NNX6. Positions 59-197, 207-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119051. 5 interactions.
DIPDIP-60629N.
MINTMINT-5201078.

Chemistry

ChEMBLCHEMBL1795114.

PTM databases

PhosphoSiteQ9NNX6.

Polymorphism databases

DMDM46396012.

2D gel databases

REPRODUCTION-2DPAGEQ9NNX6.

Proteomic databases

PaxDbQ9NNX6.
PRIDEQ9NNX6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000204801; 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]
GeneID30835.
KEGGhsa:30835.
UCSCuc002mhq.2. human. [Q9NNX6-5]
uc002mhr.2. human. [Q9NNX6-10]
uc002mhs.2. human. [Q9NNX6-11]
uc002mht.2. human. [Q9NNX6-1]
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

CTD30835.
GeneCardsGC19M007804.
HGNCHGNC:1641. CD209.
HPACAB032436.
CAB033831.
MIM604672. gene+phenotype.
607948. phenotype.
614371. phenotype.
neXtProtNX_Q9NNX6.
PharmGKBPA26199.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG311341.
HOVERGENHBG050992.
KOK06563.
OMADSKEPRL.
OrthoDBEOG7DFXC9.
PhylomeDBQ9NNX6.
TreeFamTF333341.

Gene expression databases

ArrayExpressQ9NNX6.
BgeeQ9NNX6.
GenevestigatorQ9NNX6.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]
PfamPF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NNX6.
GeneWikiDC-SIGN.
GenomeRNAi30835.
NextBio52950.
PROQ9NNX6.
SOURCESearch...

Entry information

Entry nameCD209_HUMAN
AccessionPrimary (citable) accession number: Q9NNX6
Secondary accession number(s): A8KAM4 expand/collapse secondary AC list , A8MVQ9, G5E9C4, Q2TB19, Q96QP7, Q96QP8, Q96QP9, Q96QQ0, Q96QQ1, Q96QQ2, Q96QQ3, Q96QQ4, Q96QQ5, Q96QQ6, Q96QQ7, Q96QQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries