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Q9H2X3

- CLC4M_HUMAN

UniProt

Q9H2X3 - CLC4M_HUMAN

Protein

C-type lectin domain family 4 member M

Gene

CLEC4M

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Probable pathogen-recognition receptor involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. 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, HCV E2, and human SARS coronavirus protein S. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates. Is presumably a coreceptor for the SARS coronavirus.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi359 – 3591Calcium
    Metal bindingi361 – 3611Calcium
    Metal bindingi363 – 3631Calcium; via carbonyl oxygen
    Metal bindingi366 – 3661Calcium
    Metal bindingi377 – 3771Calcium
    Metal bindingi378 – 3781Calcium

    GO - Molecular functioni

    1. carbohydrate binding Source: UniProtKB
    2. ICAM-3 receptor activity Source: UniProtKB
    3. mannose binding Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW
    5. peptide antigen binding Source: UniProtKB
    6. receptor activity Source: UniProtKB
    7. 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. innate immune response Source: UniProtKB-KW
    5. intracellular signal transduction Source: UniProtKB
    6. intracellular transport of virus Source: UniProtKB
    7. leukocyte cell-cell adhesion Source: UniProtKB
    8. modulation by virus of host morphology or physiology Source: UniProtKB
    9. peptide antigen transport Source: UniProtKB
    10. regulation of blood coagulation Source: UniProt
    11. regulation of gene expression Source: UniProt
    12. viral genome replication Source: UniProtKB
    13. virion attachment to host cell Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

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

    Keywords - Ligandi

    Calcium, Lectin, Mannose-binding, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C-type lectin domain family 4 member M
    Alternative name(s):
    CD209 antigen-like protein 1
    DC-SIGN-related protein
    Short name:
    DC-SIGNR
    Dendritic cell-specific ICAM-3-grabbing non-integrin 2
    Short name:
    DC-SIGN2
    Liver/lymph node-specific ICAM-3-grabbing non-integrin
    Short name:
    L-SIGN
    CD_antigen: CD299
    Gene namesi
    Name:CLEC4M
    Synonyms:CD209L, CD209L1, CD299
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:13523. CLEC4M.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular region Source: UniProtKB-SubCell
    3. integral component of plasma membrane Source: ProtInc
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26200.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 399399C-type lectin domain family 4 member MPRO_0000046626Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi92 – 921N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi265 ↔ 395
    Disulfide bondi268 ↔ 279
    Disulfide bondi296 ↔ 389
    Glycosylationi361 – 3611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi368 ↔ 381

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9H2X3.
    PRIDEiQ9H2X3.

    PTM databases

    PhosphoSiteiQ9H2X3.

    Expressioni

    Tissue specificityi

    Predominantly highly expressed in liver sinusoidal endothelial cells and in lymph node. Found in placental endothelium but not in macrophages. Expressed in type II alveolar cells and lung endothelial cells.3 Publications

    Gene expression databases

    ArrayExpressiQ9H2X3.
    BgeeiQ9H2X3.
    GenevestigatoriQ9H2X3.

    Organism-specific databases

    HPAiCAB033689.
    CAB033691.
    HPA042661.

    Interactioni

    Subunit structurei

    Homotetramer. Binds to many viral surface glycoproteins such as HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus S protein.2 Publications

    Protein-protein interaction databases

    BioGridi115615. 5 interactions.
    IntActiQ9H2X3. 2 interactions.
    MINTiMINT-1489134.

    Structurei

    Secondary structure

    1
    399
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi220 – 23213
    Helixi262 – 2643
    Beta strandi273 – 2753
    Beta strandi278 – 2825
    Helixi289 – 29810
    Helixi309 – 32214
    Beta strandi326 – 3316
    Beta strandi333 – 3353
    Helixi349 – 3546
    Beta strandi362 – 3654
    Beta strandi368 – 3725
    Beta strandi375 – 3795
    Beta strandi385 – 3928

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K9JX-ray1.90A/B262-399[»]
    1SL6X-ray2.25A/B/C/D/E/F216-399[»]
    1XARX-ray2.25A/B216-399[»]
    1XPHX-ray1.41A250-399[»]
    1Z0Ymodel-A/B/C/D85-399[»]
    3JQHX-ray2.20A101-264[»]
    ProteinModelPortaliQ9H2X3.
    SMRiQ9H2X3. Positions 71-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H2X3.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4949CytoplasmicCuratedAdd
    BLAST
    Topological domaini71 – 399329ExtracellularCuratedAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei50 – 7021Helical; Signal-anchor for type II membrane proteinCuratedAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati108 – 130231Add
    BLAST
    Repeati131 – 153232Add
    BLAST
    Repeati154 – 176233Add
    BLAST
    Repeati177 – 199234Add
    BLAST
    Repeati200 – 222235Add
    BLAST
    Repeati223 – 245236Add
    BLAST
    Repeati246 – 268237Add
    BLAST
    Domaini274 – 390117C-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni108 – 2691627 X approximate tandem repeatsAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi14 – 152Endocytosis signalBy similarity

    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

    eggNOGiNOG314197.
    HOVERGENiHBG050992.
    InParanoidiQ9H2X3.
    KOiK06563.
    OMAiDNYWICK.
    OrthoDBiEOG7DFXC9.
    PhylomeDBiQ9H2X3.
    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 (10)i

    Sequence statusi: Complete.

    This entry describes 10 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist. Several splicing events may occur independently in a modular way. Deletion of the transmembrane domain encoding exon through alternative splicing produces soluble isoforms.

    Isoform 1 (identifier: Q9H2X3-1) [UniParc]FASTAAdd to Basket

    Also known as: mDC-SIGN2 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

    MSDSKEPRVQ QLGLLEEDPT TSGIRLFPRD FQFQQIHGHK SSTGCLGHGA    50
    LVLQLLSFML LAGVLVAILV QVSKVPSSLS QEQSEQDAIY QNLTQLKAAV 100
    GELSEKSKLQ EIYQELTQLK AAVGELPEKS KLQEIYQELT RLKAAVGELP 150
    EKSKLQEIYQ ELTRLKAAVG ELPEKSKLQE IYQELTRLKA AVGELPEKSK 200
    LQEIYQELTE LKAAVGELPE KSKLQEIYQE LTQLKAAVGE LPDQSKQQQI 250
    YQELTDLKTA FERLCRHCPK DWTFFQGNCY FMSNSQRNWH DSVTACQEVR 300
    AQLVVIKTAE EQNFLQLQTS RSNRFSWMGL SDLNQEGTWQ WVDGSPLSPS 350
    FQRYWNSGEP NNSGNEDCAE FSGSGWNDNR CDVDNYWICK KPAACFRDE 399
    Length:399
    Mass (Da):45,350
    Last modified:March 1, 2001 - v1
    Checksum:i0FADC99F72AEA593
    GO
    Isoform 2 (identifier: Q9H2X3-2) [UniParc]FASTAAdd to Basket

    Also known as: mDC-SIGN2 type III, mDC-SIGN2 type IV

    The sequence of this isoform differs from the canonical sequence as follows:
         262-272: ERLCRHCPKDW → GEFLHIKGPWA
         273-399: Missing.

    Note: May be due to intron retention.

    Show »
    Length:272
    Mass (Da):30,481
    Checksum:iB26BE2F2DE541F5E
    GO
    Isoform 3 (identifier: Q9H2X3-3) [UniParc]FASTAAdd to Basket

    Also known as: mDC-SIGN2 type V

    The sequence of this isoform differs from the canonical sequence as follows:
         313-324: NFLQLQTSRSNR → LPAVLEQWRTQQ
         325-399: Missing.

    Show »
    Length:324
    Mass (Da):36,769
    Checksum:iB22BD6E0C926649A
    GO
    Isoform 4 (identifier: Q9H2X3-4) [UniParc]FASTAAdd to Basket

    Also known as: mDC-SIGN2 type VI

    The sequence of this isoform differs from the canonical sequence as follows:
         170-238: Missing.
         239-261: Missing.
         313-324: NFLQLQTSRSNR → LPAVLEQWRTQQ
         325-399: Missing.

    Show »
    Length:232
    Mass (Da):26,283
    Checksum:iB50EB1500097CB70
    GO
    Isoform 5 (identifier: Q9H2X3-5) [UniParc]FASTAAdd to Basket

    Also known as: sDC-SIGN2 type I

    The sequence of this isoform differs from the canonical sequence as follows:
         44-71: GCLGHGALVLQLLSFMLLAGVLVAILVQ → VPFLLGP
         177-199: Missing.
         239-261: Missing.

    Show »
    Length:332
    Mass (Da):37,954
    Checksum:iC6FDEF92C1B073C6
    GO
    Isoform 6 (identifier: Q9H2X3-6) [UniParc]FASTAAdd to Basket

    Also known as: sDC-SIGN2 type II

    The sequence of this isoform differs from the canonical sequence as follows:
         44-71: GCLGHGALVLQLLSFMLLAGVLVAILVQ → VPFLLGP
         262-272: ERLCRHCPKDW → GEFLHIKGPWA
         273-399: Missing.

    Note: May be due to intron retention.

    Show »
    Length:251
    Mass (Da):28,373
    Checksum:i86F69F6CD6055D6E
    GO
    Isoform 7 (identifier: Q9H2X3-7) [UniParc]FASTAAdd to Basket

    Also known as: sDC-SIGN2 type III

    The sequence of this isoform differs from the canonical sequence as follows:
         44-71: GCLGHGALVLQLLSFMLLAGVLVAILVQ → VPFLLGP
         147-261: Missing.

    Show »
    Length:263
    Mass (Da):30,131
    Checksum:i2BB0AAF2C506495E
    GO
    Isoform 8 (identifier: Q9H2X3-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         177-199: Missing.

    Note: Non-canonical intron-exon splice junction.

    Show »
    Length:376
    Mass (Da):42,724
    Checksum:i36CB19991F23BE90
    GO
    Isoform 9 (identifier: Q9H2X3-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         16-43: Missing.
         313-324: NFLQLQTSRSNR → LPAVLEQWRTQQ
         325-399: Missing.

    Show »
    Length:296
    Mass (Da):33,528
    Checksum:i70228F848F2DE64F
    GO
    Isoform 10 (identifier: Q9H2X3-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         16-43: Missing.
         44-71: Missing.
         262-272: ERLCRHCPKDW → GEFLHIKGPWA
         273-399: Missing.

    Note: May be due to intron retention.

    Show »
    Length:216
    Mass (Da):24,408
    Checksum:i45F01AD20E279619
    GO

    Sequence cautioni

    The sequence AAR04559.1 differs from that shown. Reason: Aberrant splicing.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti99 – 991A → T in BAB14667. 1 PublicationCurated

    Polymorphismi

    The number of repeats in the tandem repeat domain is shown to vary between 3 and 9 per allele thus contributing to a further variability in addition to alternative splicing. The shown 7 repeat-containing form has been shown to be the most frequent one (53.9%) in a study with 350 Caucasian individuals.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti164 – 1641R → Q.1 Publication
    Corresponds to variant rs11465376 [ dbSNP | Ensembl ].
    VAR_050107
    Natural varianti205 – 2051Y → C.
    Corresponds to variant rs479448 [ dbSNP | Ensembl ].
    VAR_050108
    Natural varianti251 – 2511Y → C.
    Corresponds to variant rs479448 [ dbSNP | Ensembl ].
    VAR_050109
    Natural varianti291 – 2911D → N.1 Publication
    Corresponds to variant rs2277998 [ dbSNP | Ensembl ].
    VAR_021957

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei16 – 4328Missing in isoform 9 and isoform 10. 2 PublicationsVSP_010056Add
    BLAST
    Alternative sequencei44 – 7128Missing in isoform 10. 1 PublicationVSP_010057Add
    BLAST
    Alternative sequencei44 – 7128GCLGH…AILVQ → VPFLLGP in isoform 5, isoform 6 and isoform 7. 1 PublicationVSP_010058Add
    BLAST
    Alternative sequencei147 – 261115Missing in isoform 7. 1 PublicationVSP_010059Add
    BLAST
    Alternative sequencei170 – 23869Missing in isoform 4. 1 PublicationVSP_010060Add
    BLAST
    Alternative sequencei177 – 19923Missing in isoform 5 and isoform 8. 3 PublicationsVSP_010061Add
    BLAST
    Alternative sequencei239 – 26123Missing in isoform 4 and isoform 5. 1 PublicationVSP_010062Add
    BLAST
    Alternative sequencei262 – 27211ERLCRHCPKDW → GEFLHIKGPWA in isoform 2, isoform 6 and isoform 10. 2 PublicationsVSP_010063Add
    BLAST
    Alternative sequencei273 – 399127Missing in isoform 2, isoform 6 and isoform 10. 2 PublicationsVSP_010064Add
    BLAST
    Alternative sequencei313 – 32412NFLQL…SRSNR → LPAVLEQWRTQQ in isoform 3, isoform 4 and isoform 9. 2 PublicationsVSP_010065Add
    BLAST
    Alternative sequencei325 – 39975Missing in isoform 3, isoform 4 and isoform 9. 2 PublicationsVSP_010066Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015629 mRNA. Translation: BAA76496.1.
    AF245219 mRNA. Translation: AAG13848.2.
    AF209481, AF209480 Genomic DNA. Translation: AAG13815.2.
    AY042234 mRNA. Translation: AAK91859.1.
    AY042235 mRNA. Translation: AAK91860.1.
    AY042236 mRNA. Translation: AAK91861.1.
    AY042237 mRNA. Translation: AAK91862.1.
    AY042238 mRNA. Translation: AAK91863.1.
    AY042239 mRNA. Translation: AAK91864.1.
    AY042240 mRNA. Translation: AAK91865.1.
    AF290887 mRNA. Translation: AAK20998.1.
    AY343913 mRNA. Translation: AAR04559.1. Sequence problems.
    AK023750 mRNA. Translation: BAB14667.1.
    AK292278 mRNA. Translation: BAF84967.1.
    AC008812 Genomic DNA. No translation available.
    BC038851 mRNA. Translation: AAH38851.1.
    CCDSiCCDS12187.1. [Q9H2X3-1]
    CCDS59346.1. [Q9H2X3-4]
    CCDS59347.1. [Q9H2X3-7]
    CCDS59348.1. [Q9H2X3-9]
    RefSeqiNP_001138377.1. NM_001144905.1.
    NP_001138378.1. NM_001144906.1. [Q9H2X3-7]
    NP_001138379.1. NM_001144907.1. [Q9H2X3-5]
    NP_001138380.1. NM_001144908.1. [Q9H2X3-4]
    NP_001138381.1. NM_001144909.1.
    NP_001138382.1. NM_001144910.1. [Q9H2X3-8]
    NP_001138383.1. NM_001144911.1. [Q9H2X3-9]
    NP_055072.3. NM_014257.4. [Q9H2X3-1]
    XP_006722678.1. XM_006722615.1. [Q9H2X3-3]
    UniGeneiHs.421437.

    Genome annotation databases

    EnsembliENST00000327325; ENSP00000316228; ENSG00000104938. [Q9H2X3-1]
    ENST00000359059; ENSP00000351954; ENSG00000104938. [Q9H2X3-5]
    ENST00000595496; ENSP00000470132; ENSG00000104938. [Q9H2X3-7]
    ENST00000596363; ENSP00000471125; ENSG00000104938. [Q9H2X3-9]
    ENST00000597522; ENSP00000471132; ENSG00000104938. [Q9H2X3-4]
    GeneIDi10332.
    KEGGihsa:10332.
    UCSCiuc002mhy.2. human. [Q9H2X3-10]
    uc002mhz.3. human. [Q9H2X3-4]
    uc002mia.3. human. [Q9H2X3-7]
    uc002mic.3. human. [Q9H2X3-9]
    uc002mih.3. human. [Q9H2X3-8]
    uc010xjw.2. human. [Q9H2X3-5]

    Polymorphism databases

    DMDMi46395990.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    DC-SIGNR

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB015629 mRNA. Translation: BAA76496.1 .
    AF245219 mRNA. Translation: AAG13848.2 .
    AF209481 , AF209480 Genomic DNA. Translation: AAG13815.2 .
    AY042234 mRNA. Translation: AAK91859.1 .
    AY042235 mRNA. Translation: AAK91860.1 .
    AY042236 mRNA. Translation: AAK91861.1 .
    AY042237 mRNA. Translation: AAK91862.1 .
    AY042238 mRNA. Translation: AAK91863.1 .
    AY042239 mRNA. Translation: AAK91864.1 .
    AY042240 mRNA. Translation: AAK91865.1 .
    AF290887 mRNA. Translation: AAK20998.1 .
    AY343913 mRNA. Translation: AAR04559.1 . Sequence problems.
    AK023750 mRNA. Translation: BAB14667.1 .
    AK292278 mRNA. Translation: BAF84967.1 .
    AC008812 Genomic DNA. No translation available.
    BC038851 mRNA. Translation: AAH38851.1 .
    CCDSi CCDS12187.1. [Q9H2X3-1 ]
    CCDS59346.1. [Q9H2X3-4 ]
    CCDS59347.1. [Q9H2X3-7 ]
    CCDS59348.1. [Q9H2X3-9 ]
    RefSeqi NP_001138377.1. NM_001144905.1.
    NP_001138378.1. NM_001144906.1. [Q9H2X3-7 ]
    NP_001138379.1. NM_001144907.1. [Q9H2X3-5 ]
    NP_001138380.1. NM_001144908.1. [Q9H2X3-4 ]
    NP_001138381.1. NM_001144909.1.
    NP_001138382.1. NM_001144910.1. [Q9H2X3-8 ]
    NP_001138383.1. NM_001144911.1. [Q9H2X3-9 ]
    NP_055072.3. NM_014257.4. [Q9H2X3-1 ]
    XP_006722678.1. XM_006722615.1. [Q9H2X3-3 ]
    UniGenei Hs.421437.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K9J X-ray 1.90 A/B 262-399 [» ]
    1SL6 X-ray 2.25 A/B/C/D/E/F 216-399 [» ]
    1XAR X-ray 2.25 A/B 216-399 [» ]
    1XPH X-ray 1.41 A 250-399 [» ]
    1Z0Y model - A/B/C/D 85-399 [» ]
    3JQH X-ray 2.20 A 101-264 [» ]
    ProteinModelPortali Q9H2X3.
    SMRi Q9H2X3. Positions 71-398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115615. 5 interactions.
    IntActi Q9H2X3. 2 interactions.
    MINTi MINT-1489134.

    Chemistry

    ChEMBLi CHEMBL2176858.

    PTM databases

    PhosphoSitei Q9H2X3.

    Polymorphism databases

    DMDMi 46395990.

    Proteomic databases

    PaxDbi Q9H2X3.
    PRIDEi Q9H2X3.

    Protocols and materials databases

    DNASUi 10332.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327325 ; ENSP00000316228 ; ENSG00000104938 . [Q9H2X3-1 ]
    ENST00000359059 ; ENSP00000351954 ; ENSG00000104938 . [Q9H2X3-5 ]
    ENST00000595496 ; ENSP00000470132 ; ENSG00000104938 . [Q9H2X3-7 ]
    ENST00000596363 ; ENSP00000471125 ; ENSG00000104938 . [Q9H2X3-9 ]
    ENST00000597522 ; ENSP00000471132 ; ENSG00000104938 . [Q9H2X3-4 ]
    GeneIDi 10332.
    KEGGi hsa:10332.
    UCSCi uc002mhy.2. human. [Q9H2X3-10 ]
    uc002mhz.3. human. [Q9H2X3-4 ]
    uc002mia.3. human. [Q9H2X3-7 ]
    uc002mic.3. human. [Q9H2X3-9 ]
    uc002mih.3. human. [Q9H2X3-8 ]
    uc010xjw.2. human. [Q9H2X3-5 ]

    Organism-specific databases

    CTDi 10332.
    GeneCardsi GC19P007828.
    HGNCi HGNC:13523. CLEC4M.
    HPAi CAB033689.
    CAB033691.
    HPA042661.
    MIMi 605872. gene.
    neXtProti NX_Q9H2X3.
    PharmGKBi PA26200.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG314197.
    HOVERGENi HBG050992.
    InParanoidi Q9H2X3.
    KOi K06563.
    OMAi DNYWICK.
    OrthoDBi EOG7DFXC9.
    PhylomeDBi Q9H2X3.
    TreeFami TF333341.

    Miscellaneous databases

    EvolutionaryTracei Q9H2X3.
    GeneWikii CLEC4M.
    GenomeRNAii 10332.
    NextBioi 39173.
    PROi Q9H2X3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H2X3.
    Bgeei Q9H2X3.
    Genevestigatori Q9H2X3.

    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. "Selection of cDNAs encoding putative type II membrane proteins on the cell surface from a human full-length cDNA bank."
      Yokoyama-Kobayashi M., Yamaguchi T., Sekine S., Kato S.
      Gene 228:161-167(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
      Tissue: Liver.
    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 / MRNA] (ISOFORM 1).
    3. "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; 4; 5; 6 AND 7), ALTERNATIVE SPLICING (ISOFORM 3), POLYMORPHISM, VARIANT GLN-164.
    4. "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 8), TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH ICAM3 AND HIV-1 GP120, POLYMORPHISM.
    5. "L-SIGN interaction with HIV-1."
      Bruen S., Bashirova A., Carrington M., KewalRamani V.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-291.
    6. "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] (ISOFORMS 8 AND 10).
      Tissue: Placenta and Testis.
    7. "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].
    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 1).
      Tissue: Brain.
    9. "DC-SIGNR, a DC-SIGN homologue expressed in endothelial cells, binds to human and simian immunodeficiency viruses and activates infection in trans."
      Poehlmann S., Soilleux E.J., Baribaud F., Leslie G.J., Morris L.S., Trowsdale J., Lee B., Coleman N., Doms R.W.
      Proc. Natl. Acad. Sci. U.S.A. 98:2670-2675(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH HIV-1 GP120, ROLE IN HIV-1 INFECTION.
    10. "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.
    11. "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.
    12. "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.
    13. Cited for: INTERACTION WITH SARS CORONAVIRUS S PROTEIN, TISSUE SPECIFICITY.
    14. "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 (1.9 ANGSTROMS) OF 265-394 IN COMPLEX WITH GLCNAC(2)-MAN(3) PENTASACCHARIDE.
    15. "Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR."
      Feinberg H., Guo Y., Mitchell D.A., Drickamer K., Weis W.I.
      J. Biol. Chem. 280:1327-1335(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 216-399, DISULFIDE BONDS.
    16. "The structure of DC-SIGNR with a portion of its repeat domain lends insights to modeling of the receptor tetramer."
      Snyder G.A., Colonna M., Sun P.D.
      J. Mol. Biol. 347:979-989(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 250-399, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCLC4M_HUMAN
    AccessioniPrimary (citable) accession number: Q9H2X3
    Secondary accession number(s): A6NKI4
    , A8K8B3, Q69F40, Q969M4, Q96QP3, Q96QP4, Q96QP5, Q96QP6, Q9BXS3, Q9H2Q9, Q9H8F0, Q9Y2A8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 135 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 to permissive T-cells.

    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