Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NY25

- CLC5A_HUMAN

UniProt

Q9NY25 - CLC5A_HUMAN

Protein

C-type lectin domain family 5 member A

Gene

CLEC5A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Functions as a positive regulator of osteoclastogenesis. Cell surface receptor that signals via TYROBP. Regulates inflammatory responses. Acts as a key regulator of synovial injury and bone erosion during autoimmune joint inflammation By similarity. Critical macrophage receptor for dengue virus serotypes 1-4. The binding of dengue virus to CLEC5A triggers signaling through the phosphylation of TYROBP, this interaction does not result in viral entry, but stimulates proinflammatory cytokine release.By similarity2 Publications

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. virus receptor activity Source: UniProtKB

    GO - Biological processi

    1. cellular defense response Source: ProtInc
    2. innate immune response Source: UniProtKB
    3. negative regulation of apoptotic process Source: UniProtKB
    4. negative regulation of myeloid cell apoptotic process Source: Ensembl
    5. osteoblast development Source: UniProtKB
    6. positive regulation of cytokine secretion Source: Ensembl
    7. response to virus Source: GOC
    8. signal transduction Source: ProtInc
    9. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Immunity, Innate immunity

    Keywords - Ligandi

    Lectin

    Enzyme and pathway databases

    ReactomeiREACT_147694. DAP12 interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C-type lectin domain family 5 member A
    Alternative name(s):
    C-type lectin superfamily member 5
    Myeloid DAP12-associating lectin 1
    Short name:
    MDL-1
    Gene namesi
    Name:CLEC5A
    Synonyms:CLECSF5, MDL1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:2054. CLEC5A.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 161K → I: Abolishes interaction with TYROBP. 1 Publication

    Organism-specific databases

    PharmGKBiPA26583.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 188188C-type lectin domain family 5 member APRO_0000046632Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi32 – 321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi71 ↔ 82PROSITE-ProRule annotation
    Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi99 ↔ 183PROSITE-ProRule annotation
    Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi161 ↔ 175PROSITE-ProRule annotation

    Post-translational modificationi

    N-glycosylated. Contains sialic acid residues By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9NY25.
    PRIDEiQ9NY25.

    Expressioni

    Tissue specificityi

    Expressed in peripheral blood monocytes and in the monocyte/macrophage cell lines U-937 and Mono-Mac-6, but not in cell lines of other origins. Expression is down-regulated when monocytes differentiate into dendritic cells.1 Publication

    Gene expression databases

    ArrayExpressiQ9NY25.
    BgeeiQ9NY25.
    CleanExiHS_CLEC5A.
    GenevestigatoriQ9NY25.

    Interactioni

    Subunit structurei

    Monomer. Homodimer. The majority of CLEC5A is expressed as a monomeric form on macrophages. Interacts with TYROBP/DAP12. The interaction with TYROBP is required for CLEC5 cell surface expression. Interacts with HCST/DAP10. Forms an CLEC5A/TYROBP/HCST trimolecular complex depending almost solely on TYROBP.2 Publications

    Protein-protein interaction databases

    DIPiDIP-60627N.
    STRINGi9606.ENSP00000265306.

    Structurei

    Secondary structure

    1
    188
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi76 – 783
    Beta strandi81 – 855
    Helixi92 – 1009
    Turni101 – 1033
    Helixi112 – 12211
    Beta strandi127 – 1337
    Turni135 – 1373
    Beta strandi138 – 1425
    Turni143 – 1453
    Beta strandi152 – 1543
    Beta strandi161 – 17313
    Beta strandi179 – 1868

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YHFX-ray1.90A/B/C/D/E/F/G/H/I70-187[»]
    ProteinModelPortaliQ9NY25.
    SMRiQ9NY25. Positions 70-187.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NY25.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44CytoplasmicSequence Analysis
    Topological domaini28 – 188161ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2723Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini78 – 184107C-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG269413.
    HOGENOMiHOG000252978.
    HOVERGENiHBG081250.
    InParanoidiQ9NY25.
    KOiK10073.
    OMAiFNCVTIG.
    PhylomeDBiQ9NY25.
    TreeFamiTF337735.

    Family and domain databases

    Gene3Di3.10.100.10. 1 hit.
    InterProiIPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    [Graphical view]
    PfamiPF00059. Lectin_C. 1 hit.
    [Graphical view]
    SMARTiSM00034. CLECT. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.
    PROSITEiPS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NY25-1) [UniParc]FASTAAdd to Basket

    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

    MNWHMIISGL IVVVLKVVGM TLFLLYFPQI FNKSNDGFTT TRSYGTVSQI    50
    FGSSSPSPNG FITTRSYGTV CPKDWEFYQA RCFFLSTSES SWNESRDFCK 100
    GKGSTLAIVN TPEKLKFLQD ITDAEKYFIG LIYHREEKRW RWINNSVFNG 150
    NVTNQNQNFN CATIGLTKTF DAASCDISYR RICEKNAK 188
    Length:188
    Mass (Da):21,521
    Last modified:October 1, 2000 - v1
    Checksum:i94A2DBD520DC1985
    GO
    Isoform 2 (identifier: Q9NY25-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         116-116: Missing.

    Show »
    Length:187
    Mass (Da):21,393
    Checksum:i9FC97A17AF8C62F9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti141 – 1411R → H.
    Corresponds to variant rs35942193 [ dbSNP | Ensembl ].
    VAR_050110

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei116 – 1161Missing in isoform 2. 1 PublicationVSP_012839

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF139768 mRNA. Translation: AAF02491.1.
    AJ271684 mRNA. Translation: CAB71334.1.
    AC073647 Genomic DNA. Translation: AAS07444.1.
    BC093714 mRNA. Translation: AAH93714.1.
    BC112099 mRNA. Translation: AAI12100.1.
    BC113098 mRNA. Translation: AAI13099.1.
    CCDSiCCDS5870.1. [Q9NY25-1]
    RefSeqiNP_037384.1. NM_013252.2. [Q9NY25-1]
    UniGeneiHs.446235.

    Genome annotation databases

    EnsembliENST00000546910; ENSP00000449999; ENSG00000258227. [Q9NY25-1]
    GeneIDi23601.
    KEGGihsa:23601.
    UCSCiuc003vwv.1. human. [Q9NY25-1]
    uc003vww.1. human. [Q9NY25-2]

    Polymorphism databases

    DMDMi59797971.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    MDL-1

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF139768 mRNA. Translation: AAF02491.1 .
    AJ271684 mRNA. Translation: CAB71334.1 .
    AC073647 Genomic DNA. Translation: AAS07444.1 .
    BC093714 mRNA. Translation: AAH93714.1 .
    BC112099 mRNA. Translation: AAI12100.1 .
    BC113098 mRNA. Translation: AAI13099.1 .
    CCDSi CCDS5870.1. [Q9NY25-1 ]
    RefSeqi NP_037384.1. NM_013252.2. [Q9NY25-1 ]
    UniGenei Hs.446235.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YHF X-ray 1.90 A/B/C/D/E/F/G/H/I 70-187 [» ]
    ProteinModelPortali Q9NY25.
    SMRi Q9NY25. Positions 70-187.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60627N.
    STRINGi 9606.ENSP00000265306.

    Polymorphism databases

    DMDMi 59797971.

    Proteomic databases

    PaxDbi Q9NY25.
    PRIDEi Q9NY25.

    Protocols and materials databases

    DNASUi 23601.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000546910 ; ENSP00000449999 ; ENSG00000258227 . [Q9NY25-1 ]
    GeneIDi 23601.
    KEGGi hsa:23601.
    UCSCi uc003vwv.1. human. [Q9NY25-1 ]
    uc003vww.1. human. [Q9NY25-2 ]

    Organism-specific databases

    CTDi 23601.
    GeneCardsi GC07M141627.
    HGNCi HGNC:2054. CLEC5A.
    MIMi 604987. gene.
    neXtProti NX_Q9NY25.
    PharmGKBi PA26583.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG269413.
    HOGENOMi HOG000252978.
    HOVERGENi HBG081250.
    InParanoidi Q9NY25.
    KOi K10073.
    OMAi FNCVTIG.
    PhylomeDBi Q9NY25.
    TreeFami TF337735.

    Enzyme and pathway databases

    Reactomei REACT_147694. DAP12 interactions.

    Miscellaneous databases

    EvolutionaryTracei Q9NY25.
    GeneWikii CLEC5A.
    GenomeRNAii 23601.
    NextBioi 46284.
    PROi Q9NY25.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NY25.
    Bgeei Q9NY25.
    CleanExi HS_CLEC5A.
    Genevestigatori Q9NY25.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi IPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    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 PS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Myeloid DAP12-associating lectin (MDL)-1 is a cell surface receptor involved in the activation of myeloid cells."
      Bakker A.B.H., Baker E., Sutherland G.R., Phillips J.H., Lanier L.L.
      Proc. Natl. Acad. Sci. U.S.A. 96:9792-9796(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TYROBP, MUTAGENESIS OF LYS-16.
    2. "Expression of MDL-1 in human blood and cell lines."
      Mueller A., Merz H., Feller A.C.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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).
    5. Cited for: FUNCTION AS A DENGUE VIRUS RECEPTOR.
    6. "Structural flexibility of the macrophage dengue virus receptor CLEC5A: Implications for ligand binding and signaling."
      Watson A.A., Lebedev A.A., Hall B.A., Fenton-May A.E., Vagin A.A., Dejnirattisai W., Felce J., Mongkolsapaya J., Palma A.S., Liu Y., Feizi T., Screaton G.R., Murshudov G.N., O'Callaghan C.A.
      J. Biol. Chem. 286:24208-24218(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 71-187, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH DENGUE VIRUS.

    Entry informationi

    Entry nameiCLC5A_HUMAN
    AccessioniPrimary (citable) accession number: Q9NY25
    Secondary accession number(s): Q52M11, Q9UKQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 109 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3