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Q9R007

- CLC5A_MOUSE

UniProt

Q9R007 - CLC5A_MOUSE

Protein

C-type lectin domain family 5 member A

Gene

Clec5a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (28 Jun 2011)
      Previous versions | rss
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    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. Critical macrophage receptor for dengue virus serotypes 1-4. The binding of dengue virus to CLEC5A triggers signaling through phosphylation of TYROBP, this interaction does not result in viral entry but stimulates proinflammatory cytokine release.4 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. innate immune response Source: UniProtKB
    2. negative regulation of apoptotic process Source: UniProtKB
    3. negative regulation of myeloid cell apoptotic process Source: MGI
    4. osteoblast development Source: UniProtKB
    5. positive regulation of cytokine secretion Source: UniProtKB
    6. response to virus Source: GOC

    Keywords - Biological processi

    Immunity, Innate immunity

    Keywords - Ligandi

    Lectin

    Enzyme and pathway databases

    ReactomeiREACT_188188. 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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1345151. 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 membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Involved in the pathogenetic mechanisms of Japanese encephalitis virus (JEV) infection of the brain. JEV infection of young mice results in increased expression of CLEC5A in spleen and brain with consequent activation of proinflammatory cytokines secretion.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 190190C-type lectin domain family 5 member APRO_0000046633Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi101 ↔ 185PROSITE-ProRule annotation
    Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi163 ↔ 177PROSITE-ProRule annotation

    Post-translational modificationi

    N-glycosylated. Contains sialic acid residues.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ9R007.

    Expressioni

    Tissue specificityi

    Expressed in macrophage cell line J-774, but not in T-cell lines, B-cell lines, or mast cell lines. Strong expression in bone marrow cells or thioglycollate induced neutrophils (at protein level).3 Publications

    Inductioni

    Up-regulated during the differentiation of myeloid cell line 32Dcl3 into neutrophils.

    Gene expression databases

    BgeeiQ9R007.
    CleanExiMM_CLEC5A.
    GenevestigatoriQ9R007.

    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.3 Publications

    Protein-protein interaction databases

    DIPiDIP-48775N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R007.
    SMRiQ9R007. Positions 72-189.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44CytoplasmicSequence Analysis
    Topological domaini26 – 190165ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 186107C-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.
    GeneTreeiENSGT00730000111396.
    HOGENOMiHOG000252978.
    HOVERGENiHBG081250.
    InParanoidiQ3SXC9.
    KOiK10073.
    OMAiFNCVTIG.
    OrthoDBiEOG7GQXX7.
    PhylomeDBiQ9R007.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 3 (identifier: Q9R007-3) [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 IVVVIKVVGM TFFLLYFPQV FGKSNDGFVP TESYGTTSVQ    50
    NVSQIFGRND ESTMPTRSYG TVCPRNWDFH QGKCFFFSFS ESPWKDSMDY 100
    CATQGSTLAI VNTPEKLKYL QDIAGIENYF IGLVRQPGEK KWRWINNSVF 150
    NGNVTNQDQN FDCVTIGLTK TYDAASCEVS YRWICEMNAK 190
    Length:190
    Mass (Da):21,696
    Last modified:June 28, 2011 - v2
    Checksum:iAB6AACB3A8D36637
    GO
    Isoform 1 (identifier: Q9R007-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         28-57: PQVFGKSNDGFVPTESYGTTSVQNVSQIFG → SQIFG

    Show »
    Length:165
    Mass (Da):19,055
    Checksum:i626D64392A513282
    GO
    Isoform 2 (identifier: Q9R007-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         118-118: Missing.

    Show »
    Length:189
    Mass (Da):21,567
    Checksum:i28C26A90421D745D
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei28 – 5730PQVFG…SQIFG → SQIFG in isoform 1. 2 PublicationsVSP_041577Add
    BLAST
    Alternative sequencei118 – 1181Missing in isoform 2. 1 PublicationVSP_012840

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF139769 mRNA. Translation: AAF02492.1.
    AK036697 mRNA. Translation: BAC29537.1.
    AK046600 mRNA. Translation: BAC32802.1.
    AK137482 mRNA. Translation: BAE23374.1.
    CH466533 Genomic DNA. Translation: EDL13570.1.
    BC104364 mRNA. Translation: AAI04365.1.
    BC104365 mRNA. Translation: AAI04366.1.
    CCDSiCCDS20036.1. [Q9R007-3]
    CCDS20037.1. [Q9R007-1]
    RefSeqiNP_001033693.1. NM_001038604.1. [Q9R007-3]
    NP_067339.1. NM_021364.2. [Q9R007-1]
    UniGeneiMm.103765.

    Genome annotation databases

    EnsembliENSMUST00000101491; ENSMUSP00000099030; ENSMUSG00000029915. [Q9R007-1]
    ENSMUST00000129948; ENSMUSP00000121848; ENSMUSG00000029915. [Q9R007-3]
    ENSMUST00000177178; ENSMUSP00000135240; ENSMUSG00000029915.
    GeneIDi23845.
    KEGGimmu:23845.
    UCSCiuc009bna.1. mouse. [Q9R007-3]
    uc009bnb.1. mouse. [Q9R007-1]
    uc009bnc.1. mouse. [Q9R007-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    MDL-1

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF139769 mRNA. Translation: AAF02492.1 .
    AK036697 mRNA. Translation: BAC29537.1 .
    AK046600 mRNA. Translation: BAC32802.1 .
    AK137482 mRNA. Translation: BAE23374.1 .
    CH466533 Genomic DNA. Translation: EDL13570.1 .
    BC104364 mRNA. Translation: AAI04365.1 .
    BC104365 mRNA. Translation: AAI04366.1 .
    CCDSi CCDS20036.1. [Q9R007-3 ]
    CCDS20037.1. [Q9R007-1 ]
    RefSeqi NP_001033693.1. NM_001038604.1. [Q9R007-3 ]
    NP_067339.1. NM_021364.2. [Q9R007-1 ]
    UniGenei Mm.103765.

    3D structure databases

    ProteinModelPortali Q9R007.
    SMRi Q9R007. Positions 72-189.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48775N.

    Proteomic databases

    PRIDEi Q9R007.

    Protocols and materials databases

    DNASUi 23845.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000101491 ; ENSMUSP00000099030 ; ENSMUSG00000029915 . [Q9R007-1 ]
    ENSMUST00000129948 ; ENSMUSP00000121848 ; ENSMUSG00000029915 . [Q9R007-3 ]
    ENSMUST00000177178 ; ENSMUSP00000135240 ; ENSMUSG00000029915 .
    GeneIDi 23845.
    KEGGi mmu:23845.
    UCSCi uc009bna.1. mouse. [Q9R007-3 ]
    uc009bnb.1. mouse. [Q9R007-1 ]
    uc009bnc.1. mouse. [Q9R007-2 ]

    Organism-specific databases

    CTDi 23601.
    MGIi MGI:1345151. Clec5a.

    Phylogenomic databases

    eggNOGi NOG269413.
    GeneTreei ENSGT00730000111396.
    HOGENOMi HOG000252978.
    HOVERGENi HBG081250.
    InParanoidi Q3SXC9.
    KOi K10073.
    OMAi FNCVTIG.
    OrthoDBi EOG7GQXX7.
    PhylomeDBi Q9R007.
    TreeFami TF337735.

    Enzyme and pathway databases

    Reactomei REACT_188188. DAP12 interactions.

    Miscellaneous databases

    NextBioi 303527.
    PROi Q9R007.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9R007.
    CleanExi MM_CLEC5A.
    Genevestigatori Q9R007.

    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 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TYROBP.
      Strain: BALB/c.
      Tissue: Myeloid.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Adipose tissue and Bone.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      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 3).
    5. Cited for: FUNCTION AS A DENGUE VIRUS RECEPTOR.
    6. "Expression and functional role of MDL-1 (CLEC5A) in mouse myeloid lineage cells."
      Aoki N., Kimura Y., Kimura S., Nagato T., Azumi M., Kobayashi H., Sato K., Tateno M.
      J. Leukoc. Biol. 85:508-517(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH HCST, SUBCELLULAR LOCATION, GLYCOSYLATION, SIALIC ACID CONTENT.
    7. "Signal adaptor DAP10 associates with MDL-1 and triggers osteoclastogenesis in cooperation with DAP12."
      Inui M., Kikuchi Y., Aoki N., Endo S., Maeda T., Sugahara-Tobinai A., Fujimura S., Nakamura A., Kumanogoh A., Colonna M., Takai T.
      Proc. Natl. Acad. Sci. U.S.A. 106:4816-4821(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCST, GLYCOSYLATION, FUNCTION.
    8. "Myeloid DAP12-associating lectin (MDL)-1 regulates synovial inflammation and bone erosion associated with autoimmune arthritis."
      Joyce-Shaikh B., Bigler M.E., Chao C.C., Murphy E.E., Blumenschein W.M., Adamopoulos I.E., Heyworth P.G., Antonenko S., Bowman E.P., McClanahan T.K., Phillips J.H., Cua D.J.
      J. Exp. Med. 207:579-589(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, FUNCTION.
    9. "Expression profile of Japanese encephalitis virus induced neuroinflammation and its implication in disease severity."
      Gupta N., Lomash V., Rao P.V.
      J. Clin. Virol. 49:4-10(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN JAPANESE ENCEPHALITIS VIRUS INFECTION.

    Entry informationi

    Entry nameiCLC5A_MOUSE
    AccessioniPrimary (citable) accession number: Q9R007
    Secondary accession number(s): Q3SXC9, Q3UV97, Q8BL24
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 107 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3