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P29017

- CD1C_HUMAN

UniProt

P29017 - CD1C_HUMAN

Protein

T-cell surface glycoprotein CD1c

Gene

CD1C

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 2 (03 Apr 2007)
      Previous versions | rss
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    Functioni

    Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells.4 Publications

    GO - Molecular functioni

    1. endogenous lipid antigen binding Source: UniProtKB
    2. exogenous lipid antigen binding Source: UniProtKB
    3. glycolipid binding Source: UniProtKB
    4. lipopeptide binding Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation Source: InterPro
    2. T cell activation involved in immune response Source: UniProtKB

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    T-cell surface glycoprotein CD1c
    Alternative name(s):
    CD_antigen: CD1c
    Gene namesi
    Name:CD1C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1636. CD1C.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Endosome membrane
    Note: Subject to intracellular trafficking between the cell membrane and endosomes.

    GO - Cellular componenti

    1. endosome membrane Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26195.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 333316T-cell surface glycoprotein CD1cPRO_0000014580Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)2 Publications
    Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi75 – 751N-linked (GlcNAc...)1 Publication
    Glycosylationi78 – 781N-linked (GlcNAc...); atypical1 Publication
    Disulfide bondi120 ↔ 1851 PublicationPROSITE-ProRule annotation
    Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi225 ↔ 280PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP29017.
    PaxDbiP29017.
    PRIDEiP29017.

    Expressioni

    Tissue specificityi

    Expressed on cortical thymocytes, on certain T-cell leukemias, and in various other tissues.

    Gene expression databases

    ArrayExpressiP29017.
    BgeeiP29017.
    CleanExiHS_CD1C.
    GenevestigatoriP29017.

    Interactioni

    Subunit structurei

    Heterodimer with B2M (beta-2-microglobulin).1 Publication

    Protein-protein interaction databases

    IntActiP29017. 2 interactions.
    MINTiMINT-4656025.
    STRINGi9606.ENSP00000357152.

    Structurei

    Secondary structure

    1
    333
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 4016
    Beta strandi42 – 509
    Beta strandi53 – 597
    Turni60 – 634
    Beta strandi64 – 674
    Turni70 – 756
    Helixi78 – 10023
    Beta strandi112 – 12312
    Beta strandi128 – 1369
    Beta strandi139 – 1457
    Beta strandi148 – 1514
    Helixi157 – 16812
    Helixi173 – 18210
    Helixi184 – 19916

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3OV6X-ray2.50A19-201[»]
    ProteinModelPortaliP29017.
    SMRiP29017. Positions 24-298.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29017.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini18 – 302285ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini324 – 33310CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei303 – 32321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini206 – 29691Ig-likeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi329 – 3324Internalization signal

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG319535.
    HOGENOMiHOG000111666.
    HOVERGENiHBG004453.
    KOiK06448.
    OMAiSFVNQSW.
    OrthoDBiEOG7DZ8K9.
    PhylomeDBiP29017.
    TreeFamiTF336723.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003597. Ig_C1-set.
    IPR011161. MHC_I-like_Ag-recog.
    IPR011162. MHC_I/II-like_Ag-recog.
    [Graphical view]
    PfamiPF07654. C1-set. 1 hit.
    [Graphical view]
    SMARTiSM00407. IGc1. 1 hit.
    [Graphical view]
    SUPFAMiSSF54452. SSF54452. 1 hit.
    PROSITEiPS50835. IG_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P29017-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLFLQFLLLA LLLPGGDNAD ASQEHVSFHV IQIFSFVNQS WARGQGSGWL    50
    DELQTHGWDS ESGTIIFLHN WSKGNFSNEE LSDLELLFRF YLFGLTREIQ 100
    DHASQDYSKY PFEVQVKAGC ELHSGKSPEG FFQVAFNGLD LLSFQNTTWV 150
    PSPGCGSLAQ SVCHLLNHQY EGVTETVYNL IRSTCPRFLL GLLDAGKMYV 200
    HRQVRPEAWL SSRPSLGSGQ LLLVCHASGF YPKPVWVTWM RNEQEQLGTK 250
    HGDILPNADG TWYLQVILEV ASEEPAGLSC RVRHSSLGGQ DIILYWGHHF 300
    SMNWIALVVI VPLVILIVLV LWFKKHCSYQ DIL 333
    Length:333
    Mass (Da):37,654
    Last modified:April 3, 2007 - v2
    Checksum:i8E4E057097E3E440
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti290 – 2901Q → R in CAG33361. 1 PublicationCurated
    Sequence conflicti327 – 3337CSYQDIL → W in AAA51942. (PubMed:2447586)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti70 – 701N → T.
    Corresponds to variant rs3138100 [ dbSNP | Ensembl ].
    VAR_031564
    Natural varianti300 – 3001F → S.1 Publication
    Corresponds to variant rs3138105 [ dbSNP | Ensembl ].
    VAR_031565

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22178
    , M22174, M22175, M22176, M22177 Genomic DNA. Translation: AAA51942.1.
    M28827 mRNA. Translation: AAA51941.1.
    CR457080 mRNA. Translation: CAG33361.1.
    AL121986 Genomic DNA. Translation: CAI10850.1.
    BC126465 mRNA. Translation: AAI26466.1.
    BC126467 mRNA. Translation: AAI26468.1.
    AF142667 Genomic DNA. Translation: AAD37580.1.
    M14667 Genomic DNA. Translation: AAA51938.1.
    CCDSiCCDS1175.1.
    PIRiC45801. HLHUCC.
    RefSeqiNP_001756.2. NM_001765.2.
    UniGeneiHs.132448.

    Genome annotation databases

    EnsembliENST00000368170; ENSP00000357152; ENSG00000158481.
    GeneIDi911.
    KEGGihsa:911.
    UCSCiuc001fru.3. human.

    Polymorphism databases

    DMDMi143811371.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22178
    , M22174 , M22175 , M22176 , M22177 Genomic DNA. Translation: AAA51942.1 .
    M28827 mRNA. Translation: AAA51941.1 .
    CR457080 mRNA. Translation: CAG33361.1 .
    AL121986 Genomic DNA. Translation: CAI10850.1 .
    BC126465 mRNA. Translation: AAI26466.1 .
    BC126467 mRNA. Translation: AAI26468.1 .
    AF142667 Genomic DNA. Translation: AAD37580.1 .
    M14667 Genomic DNA. Translation: AAA51938.1 .
    CCDSi CCDS1175.1.
    PIRi C45801. HLHUCC.
    RefSeqi NP_001756.2. NM_001765.2.
    UniGenei Hs.132448.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3OV6 X-ray 2.50 A 19-201 [» ]
    ProteinModelPortali P29017.
    SMRi P29017. Positions 24-298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P29017. 2 interactions.
    MINTi MINT-4656025.
    STRINGi 9606.ENSP00000357152.

    Polymorphism databases

    DMDMi 143811371.

    Proteomic databases

    MaxQBi P29017.
    PaxDbi P29017.
    PRIDEi P29017.

    Protocols and materials databases

    DNASUi 911.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368170 ; ENSP00000357152 ; ENSG00000158481 .
    GeneIDi 911.
    KEGGi hsa:911.
    UCSCi uc001fru.3. human.

    Organism-specific databases

    CTDi 911.
    GeneCardsi GC01P158259.
    HGNCi HGNC:1636. CD1C.
    MIMi 188340. gene.
    neXtProti NX_P29017.
    PharmGKBi PA26195.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG319535.
    HOGENOMi HOG000111666.
    HOVERGENi HBG004453.
    KOi K06448.
    OMAi SFVNQSW.
    OrthoDBi EOG7DZ8K9.
    PhylomeDBi P29017.
    TreeFami TF336723.

    Miscellaneous databases

    EvolutionaryTracei P29017.
    GenomeRNAii 911.
    NextBioi 3758.
    PROi P29017.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29017.
    Bgeei P29017.
    CleanExi HS_CD1C.
    Genevestigatori P29017.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.30.500.10. 1 hit.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003597. Ig_C1-set.
    IPR011161. MHC_I-like_Ag-recog.
    IPR011162. MHC_I/II-like_Ag-recog.
    [Graphical view ]
    Pfami PF07654. C1-set. 1 hit.
    [Graphical view ]
    SMARTi SM00407. IGc1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54452. SSF54452. 1 hit.
    PROSITEi PS50835. IG_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of the human thymocyte antigens CD1a, CD1b, and CD1c."
      Martin L.H., Calabi F., Lefebvre F.-A., Bilsland C.A.G., Milstein C.
      Proc. Natl. Acad. Sci. U.S.A. 84:9189-9193(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c demonstrates a hierarchy of exclusion in fibroblasts."
      Aruffo A., Seed B.
      J. Immunol. 143:1723-1730(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-300.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-109.
    7. "Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens."
      Martin L.H., Calabi F., Milstein C.
      Proc. Natl. Acad. Sci. U.S.A. 83:9154-9158(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-296.
    8. "Human CD1b and CD1c isoforms survey different intracellular compartments for the presentation of microbial lipid antigens."
      Briken V., Jackman R.M., Watts G.F.M., Rogers R.A., Porcelli S.A.
      J. Exp. Med. 192:281-288(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERNALIZATION SIGNAL, SUBCELLULAR LOCATION.
    9. "CD1c-mediated T-cell recognition of isoprenoid glycolipids in Mycobacterium tuberculosis infection."
      Moody D.B., Ulrichs T., Muehlecker W., Young D.C., Gurcha S.S., Grant E., Rosat J.-P., Brenner M.B., Costello C.E., Besra G.S., Porcelli S.A.
      Nature 404:884-888(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-38; ASN-75 AND ASN-78.
      Tissue: Leukemic T-cell.
    12. "The 2.5 a structure of CD1c in complex with a mycobacterial lipid reveals an open groove ideally suited for diverse antigen presentation."
      Scharf L., Li N.S., Hawk A.J., Garzon D., Zhang T., Fox L.M., Kazen A.R., Shah S., Haddadian E.J., Gumperz J.E., Saghatelian A., Faraldo-Gomez J.D., Meredith S.C., Piccirilli J.A., Adams E.J.
      Immunity 33:853-862(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-201 IN COMPLEX WITH MANNOSYL-BETA1-PHOSPHOMYCOKETIDE, FUNCTION, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-38.

    Entry informationi

    Entry nameiCD1C_HUMAN
    AccessioniPrimary (citable) accession number: P29017
    Secondary accession number(s): Q5TDJ7
    , Q6IAS4, Q9UMM0, Q9UN96
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 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

    During protein synthesis and maturation, CD1 family members bind endogenous lipids that are replaced by lipid or glycolipid antigens when the proteins are internalized and pass through endosomes or lysosomes, before trafficking back to the cell surface.

    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 1
      Human chromosome 1: 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