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Q9NNX6

- CD209_HUMAN

UniProt

Q9NNX6 - CD209_HUMAN

Protein

CD209 antigen

Gene

CD209

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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.
    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.

    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. protein binding Source: IntAct
    6. 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

    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

    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

    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 antigenPRO_0000046595Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
    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.10 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

    1
    404
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NNX6.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3737CytoplasmicCuratedAdd
    BLAST
    Topological domaini59 – 404346ExtracellularCuratedAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei38 – 5821Helical; Signal-anchor for type II membrane proteinCuratedAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

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

    Region

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

    Motif

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

    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

    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.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

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti152 – 1521W → Q in AAK91848. (PubMed:11337487)Curated

    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. 2 PublicationsVSP_010037Add
    BLAST
    Alternative sequencei16 – 5944Missing in isoform 7 and isoform 8. 1 PublicationVSP_010038Add
    BLAST
    Alternative sequencei30 – 345GYKSL → RNQKC in isoform 9. 1 PublicationVSP_010039
    Alternative sequencei35 – 404370Missing in isoform 9. 1 PublicationVSP_010040Add
    BLAST
    Alternative sequencei36 – 5924Missing in isoform 6, isoform 10, isoform 11 and isoform 12. 2 PublicationsVSP_010041Add
    BLAST
    Alternative sequencei74 – 309236Missing in isoform 4. 1 PublicationVSP_010042Add
    BLAST
    Alternative sequencei142 – 23392Missing in isoform 8. 1 PublicationVSP_010043Add
    BLAST
    Alternative sequencei158 – 24992Missing in isoform 3. 1 PublicationVSP_010044Add
    BLAST
    Alternative sequencei191 – 23646Missing in isoform 11. 1 PublicationVSP_010047Add
    BLAST
    Alternative sequencei301 – 32121NFLQL…GLSDL → LQAVLEQRRAQQRWGGRLRG I in isoform 12. 1 PublicationVSP_010048Add
    BLAST
    Alternative sequencei301 – 3066Missing in isoform 2. 1 PublicationVSP_010049
    Alternative sequencei322 – 40483Missing in isoform 12. 1 PublicationVSP_010050Add
    BLAST

    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

    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

    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

    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: October 1, 2014
    This is version 134 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