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)

Q13241

- KLRD1_HUMAN

UniProt

Q13241 - KLRD1_HUMAN

Protein

Natural killer cells antigen CD94

Gene

KLRD1

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 134 (01 Oct 2014)
      Sequence version 2 (31 May 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells.

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. protein binding Source: UniProt
    3. transmembrane signaling receptor activity Source: ProtInc

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: ProtInc
    2. innate immune response Source: Reactome
    3. regulation of immune response Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Ligandi

    Lectin

    Enzyme and pathway databases

    ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_147694. DAP12 interactions.
    REACT_147814. DAP12 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Natural killer cells antigen CD94
    Alternative name(s):
    KP43
    Killer cell lectin-like receptor subfamily D member 1
    NK cell receptor
    CD_antigen: CD94
    Gene namesi
    Name:KLRD1
    Synonyms:CD94
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:6378. KLRD1.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30167.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 179179Natural killer cells antigen CD94PRO_0000046587Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi58 ↔ 70
    Disulfide bondi59 – 59Interchain (with C-116 in NGK2A)
    Disulfide bondi61 ↔ 72
    Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi89 ↔ 174
    Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi152 ↔ 166

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ13241.
    PRIDEiQ13241.

    PTM databases

    PhosphoSiteiQ13241.

    Expressioni

    Tissue specificityi

    Natural killer cells.

    Gene expression databases

    ArrayExpressiQ13241.
    BgeeiQ13241.
    CleanExiHS_KLRD1.
    GenevestigatoriQ13241.

    Interactioni

    Subunit structurei

    Can form disulfide-bonded heterodimer with NKG2 family members.3 Publications

    Protein-protein interaction databases

    BioGridi110023. 4 interactions.
    STRINGi9606.ENSP00000338130.

    Structurei

    Secondary structure

    1
    179
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni62 – 643
    Beta strandi66 – 683
    Beta strandi71 – 755
    Helixi82 – 9110
    Helixi102 – 1087
    Beta strandi118 – 1225
    Turni123 – 1264
    Beta strandi127 – 1304
    Turni138 – 1403
    Helixi142 – 1465
    Beta strandi151 – 1566
    Turni157 – 1593
    Beta strandi160 – 1645
    Beta strandi170 – 1767

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B6EX-ray2.60A52-179[»]
    3BDWX-ray2.50A/C57-179[»]
    3CDGX-ray3.40E/J57-179[»]
    3CIIX-ray4.41G/I59-179[»]
    ProteinModelPortaliQ13241.
    SMRiQ13241. Positions 57-179.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13241.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1010CytoplasmicSequence Analysis
    Topological domaini32 – 179148ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 3121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini68 – 175108C-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

    eggNOGiNOG256912.
    HOGENOMiHOG000220925.
    HOVERGENiHBG099800.
    KOiK06516.
    OMAiVWIFTAF.
    TreeFamiTF336674.

    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 1 (identifier: Q13241-1) [UniParc]FASTAAdd to Basket

    Also known as: CD94-A

    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

    MAVFKTTLWR LISGTLGIIC LSLMSTLGIL LKNSFTKLSI EPAFTPGPNI    50
    ELQKDSDCCS CQEKWVGYRC NCYFISSEQK TWNESRHLCA SQKSSLLQLQ 100
    NTDELDFMSS SQQFYWIGLS YSEEHTAWLW ENGSALSQYL FPSFETFNTK 150
    NCIAYNPNGN ALDESCEDKN RYICKQQLI 179
    Length:179
    Mass (Da):20,513
    Last modified:May 31, 2011 - v2
    Checksum:i01634D3832D4B1A7
    GO
    Isoform 2 (identifier: Q13241-2) [UniParc]FASTAAdd to Basket

    Also known as: CD94-B

    The sequence of this isoform differs from the canonical sequence as follows:
         105-105: L → LQ

    Show »
    Length:180
    Mass (Da):20,641
    Checksum:i2913D0532DAFA866
    GO
    Isoform 3 (identifier: Q13241-3) [UniParc]FASTAAdd to Basket

    Also known as: CD94 alt

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: MAVFKTTLWRLISGTLGIICLSLMSTLGILLKNS → MAA

    Show »
    Length:148
    Mass (Da):17,109
    Checksum:i2C3876E8A2337B44
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251S → A.3 Publications
    Corresponds to variant rs10772256 [ dbSNP | Ensembl ].
    VAR_050103

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3434MAVFK…LLKNS → MAA in isoform 3. 1 PublicationVSP_003052Add
    BLAST
    Alternative sequencei105 – 1051L → LQ in isoform 2. CuratedVSP_003053

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30610 mRNA. Translation: AAC50291.1.
    Y14287, Y14288 Genomic DNA. Translation: CAA74663.1.
    AJ000673 Genomic DNA. Translation: CAA04230.1.
    AJ000001 mRNA. Translation: CAA03845.1.
    AB009597 mRNA. Translation: BAA24450.1.
    AB010084 Genomic DNA. Translation: BAA24451.1.
    AC022075 Genomic DNA. No translation available.
    BC028009 mRNA. Translation: AAH28009.1.
    CCDSiCCDS8621.1. [Q13241-1]
    CCDS8622.1. [Q13241-3]
    RefSeqiNP_001107868.1. NM_001114396.1.
    NP_002253.1. NM_002262.3.
    NP_031360.1. NM_007334.2. [Q13241-3]
    XP_005253420.1. XM_005253363.2. [Q13241-2]
    UniGeneiHs.562457.

    Genome annotation databases

    EnsembliENST00000336164; ENSP00000338130; ENSG00000134539. [Q13241-1]
    ENST00000350274; ENSP00000310929; ENSG00000134539. [Q13241-3]
    ENST00000381908; ENSP00000371333; ENSG00000134539. [Q13241-2]
    GeneIDi3824.
    KEGGihsa:3824.
    UCSCiuc001qxy.4. human. [Q13241-3]
    uc001qxz.4. human. [Q13241-2]
    uc009zhi.3. human. [Q13241-1]

    Polymorphism databases

    DMDMi334302835.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    CD94

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30610 mRNA. Translation: AAC50291.1 .
    Y14287 , Y14288 Genomic DNA. Translation: CAA74663.1 .
    AJ000673 Genomic DNA. Translation: CAA04230.1 .
    AJ000001 mRNA. Translation: CAA03845.1 .
    AB009597 mRNA. Translation: BAA24450.1 .
    AB010084 Genomic DNA. Translation: BAA24451.1 .
    AC022075 Genomic DNA. No translation available.
    BC028009 mRNA. Translation: AAH28009.1 .
    CCDSi CCDS8621.1. [Q13241-1 ]
    CCDS8622.1. [Q13241-3 ]
    RefSeqi NP_001107868.1. NM_001114396.1.
    NP_002253.1. NM_002262.3.
    NP_031360.1. NM_007334.2. [Q13241-3 ]
    XP_005253420.1. XM_005253363.2. [Q13241-2 ]
    UniGenei Hs.562457.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B6E X-ray 2.60 A 52-179 [» ]
    3BDW X-ray 2.50 A/C 57-179 [» ]
    3CDG X-ray 3.40 E/J 57-179 [» ]
    3CII X-ray 4.41 G/I 59-179 [» ]
    ProteinModelPortali Q13241.
    SMRi Q13241. Positions 57-179.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110023. 4 interactions.
    STRINGi 9606.ENSP00000338130.

    PTM databases

    PhosphoSitei Q13241.

    Polymorphism databases

    DMDMi 334302835.

    Proteomic databases

    PaxDbi Q13241.
    PRIDEi Q13241.

    Protocols and materials databases

    DNASUi 3824.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336164 ; ENSP00000338130 ; ENSG00000134539 . [Q13241-1 ]
    ENST00000350274 ; ENSP00000310929 ; ENSG00000134539 . [Q13241-3 ]
    ENST00000381908 ; ENSP00000371333 ; ENSG00000134539 . [Q13241-2 ]
    GeneIDi 3824.
    KEGGi hsa:3824.
    UCSCi uc001qxy.4. human. [Q13241-3 ]
    uc001qxz.4. human. [Q13241-2 ]
    uc009zhi.3. human. [Q13241-1 ]

    Organism-specific databases

    CTDi 3824.
    GeneCardsi GC12P010378.
    HGNCi HGNC:6378. KLRD1.
    MIMi 602894. gene.
    neXtProti NX_Q13241.
    PharmGKBi PA30167.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG256912.
    HOGENOMi HOG000220925.
    HOVERGENi HBG099800.
    KOi K06516.
    OMAi VWIFTAF.
    TreeFami TF336674.

    Enzyme and pathway databases

    Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_147694. DAP12 interactions.
    REACT_147814. DAP12 signaling.

    Miscellaneous databases

    EvolutionaryTracei Q13241.
    GeneWikii KLRD1.
    GenomeRNAii 3824.
    NextBioi 15039.
    PROi Q13241.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13241.
    Bgeei Q13241.
    CleanExi HS_KLRD1.
    Genevestigatori Q13241.

    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. "Molecular characterization of human CD94: a type II membrane glycoprotein related to the C-type lectin superfamily."
      Chang C., Rodriguez A., Carretero M., Lopez-Botet M., Phillips J.H., Lanier L.L.
      Eur. J. Immunol. 25:2433-2437(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-25.
      Tissue: Blood.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-25.
      Tissue: Placenta.
    3. Biassoni R.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3).
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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), VARIANT ALA-25.
      Tissue: Blood.
    7. "Structure of CD94 reveals a novel C-type lectin fold: implications for the NK cell-associated CD94/NKG2 receptors."
      Boyington J.C., Riaz A.N., Patamawenu A., Coligan J.E., Brooks A.G., Sun P.D.
      Immunity 10:75-82(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 52-179, DISULFIDE BONDS.
    8. "The heterodimeric assembly of the CD94-NKG2 receptor family and implications for human leukocyte antigen-E recognition."
      Sullivan L.C., Clements C.S., Beddoe T., Johnson D., Hoare H.L., Lin J., Huyton T., Hopkins E.J., Reid H.H., Wilce M.C., Kabat J., Borrego F., Coligan J.E., Rossjohn J., Brooks A.G.
      Immunity 27:900-911(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 57-179 IN COMPLEX WITH NGK2A, SUBUNIT, DISULFIDE BONDS.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (4.41 ANGSTROMS) OF 59-179 IN COMPLEX WITH NGK2A, SUBUNIT, DISULFIDE BONDS.
    10. "CD94-NKG2A recognition of human leukocyte antigen (HLA)-E bound to an HLA class I leader sequence."
      Petrie E.J., Clements C.S., Lin J., Sullivan L.C., Johnson D., Huyton T., Heroux A., Hoare H.L., Beddoe T., Reid H.H., Wilce M.C., Brooks A.G., Rossjohn J.
      J. Exp. Med. 205:725-735(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 57-179 IN COMPLEX WITH NGK2A, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiKLRD1_HUMAN
    AccessioniPrimary (citable) accession number: Q13241
    Secondary accession number(s): O43321
    , O43773, Q9UBE3, Q9UEQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 31, 2011
    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

    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 12
      Human chromosome 12: 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