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Protein

Natural killer cells antigen CD94

Gene

KLRD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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: UniProtKB-KW
  2. 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010CytoplasmicSequence Analysis
Transmembranei11 – 3121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini32 – 179148ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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

BgeeiQ13241.
CleanExiHS_KLRD1.
ExpressionAtlasiQ13241. baseline and differential.
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 – 643Combined sources
Beta strandi66 – 683Combined sources
Beta strandi71 – 755Combined sources
Helixi82 – 9110Combined sources
Helixi102 – 1087Combined sources
Beta strandi118 – 1225Combined sources
Turni123 – 1264Combined sources
Beta strandi127 – 1304Combined sources
Turni138 – 1403Combined sources
Helixi142 – 1465Combined sources
Beta strandi151 – 1566Combined sources
Turni157 – 1593Combined sources
Beta strandi160 – 1645Combined sources
Beta strandi170 – 1767Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00730000110282.
HOGENOMiHOG000220925.
HOVERGENiHBG099800.
InParanoidiQ13241.
KOiK06516.
OMAiTWNESRH.
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

        10         20         30         40         50
MAVFKTTLWR LISGTLGIIC LSLMSTLGIL LKNSFTKLSI EPAFTPGPNI
60 70 80 90 100
ELQKDSDCCS CQEKWVGYRC NCYFISSEQK TWNESRHLCA SQKSSLLQLQ
110 120 130 140 150
NTDELDFMSS SQQFYWIGLS YSEEHTAWLW ENGSALSQYL FPSFETFNTK
160 170
NCIAYNPNGN ALDESCEDKN RYICKQQLI
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:
EMBLi
GenBanki
DDBJi
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. [Q13241-1]
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi110023. 4 interactions.
STRINGi9606.ENSP00000338130.

PTM databases

PhosphoSiteiQ13241.

Polymorphism databases

DMDMi334302835.

Proteomic databases

PaxDbiQ13241.
PRIDEiQ13241.

Protocols and materials databases

DNASUi3824.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3824.
GeneCardsiGC12P010378.
HGNCiHGNC:6378. KLRD1.
MIMi602894. gene.
neXtProtiNX_Q13241.
PharmGKBiPA30167.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG256912.
GeneTreeiENSGT00730000110282.
HOGENOMiHOG000220925.
HOVERGENiHBG099800.
InParanoidiQ13241.
KOiK06516.
OMAiTWNESRH.
TreeFamiTF336674.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ13241.
GeneWikiiKLRD1.
GenomeRNAii3824.
NextBioi15039.
PROiQ13241.
SOURCEiSearch...

Gene expression databases

BgeeiQ13241.
CleanExiHS_KLRD1.
ExpressionAtlasiQ13241. baseline and differential.
GenevestigatoriQ13241.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 137 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.