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Protein

NKG2-A/NKG2-B type II integral membrane protein

Gene

KLRC1

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. MHC class I protein complex binding Source: UniProtKB
  3. transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  1. cell surface receptor signaling pathway Source: ProtInc
  2. 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.

Names & Taxonomyi

Protein namesi
Recommended name:
NKG2-A/NKG2-B type II integral membrane protein
Alternative name(s):
CD159 antigen-like family member A
NK cell receptor A
NKG2-A/B-activating NK receptor
CD_antigen: CD159a
Gene namesi
Name:KLRC1
Synonyms:NKG2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:6374. KLRC1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7070CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei71 – 9323Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini94 – 233140ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: ProtInc
  2. plasma membrane Source: Reactome
  3. receptor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30163.

Polymorphism and mutation databases

BioMutaiKLRC1.
DMDMi317373399.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 233233NKG2-A/NKG2-B type II integral membrane proteinPRO_0000046659Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi116 – 116Interchain (with C-59 in KLRD1)
Disulfide bondi119 ↔ 130
Disulfide bondi147 ↔ 229
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi208 ↔ 221

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP26715.
PaxDbiP26715.
PRIDEiP26715.

PTM databases

PhosphoSiteiP26715.

Expressioni

Tissue specificityi

Natural killer cells.

Gene expression databases

BgeeiP26715.
CleanExiHS_KLRC1.
ExpressionAtlasiP26715. baseline.
GenevestigatoriP26715.

Interactioni

Subunit structurei

Can form disulfide-bonded heterodimer with CD94.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MALP211453EBI-9018187,EBI-3932027
PMP22Q014533EBI-9018187,EBI-2845982

Protein-protein interaction databases

BioGridi110020. 3 interactions.
IntActiP26715. 2 interactions.
STRINGi9606.ENSP00000352064.

Structurei

Secondary structure

1
233
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi117 – 1193Combined sources
Beta strandi124 – 13815Combined sources
Helixi140 – 14910Combined sources
Beta strandi152 – 1543Combined sources
Helixi160 – 16910Combined sources
Beta strandi171 – 1788Combined sources
Beta strandi191 – 1933Combined sources
Beta strandi208 – 21912Combined sources
Beta strandi225 – 2306Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RMXNMR-B1-15[»]
2YU7NMR-B33-47[»]
3BDWX-ray2.50B/D113-232[»]
3CDGX-ray3.40F/K113-232[»]
3CIIX-ray4.41H/J113-232[»]
ProteinModelPortaliP26715.
SMRiP26715. Positions 113-232.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26715.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini118 – 231114C-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

eggNOGiNOG146673.
GeneTreeiENSGT00730000110282.
HOGENOMiHOG000220925.
HOVERGENiHBG077044.
InParanoidiP26715.
KOiK06541.
OMAiPPNPKRQ.
PhylomeDBiP26715.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform NKG2-A (identifier: P26715-1) [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

        10         20         30         40         50
MDNQGVIYSD LNLPPNPKRQ QRKPKGNKNS ILATEQEITY AELNLQKASQ
60 70 80 90 100
DFQGNDKTYH CKDLPSAPEK LIVGILGIIC LILMASVVTI VVIPSTLIQR
110 120 130 140 150
HNNSSLNTRT QKARHCGHCP EEWITYSNSC YYIGKERRTW EESLLACTSK
160 170 180 190 200
NSSLLSIDNE EEMKFLSIIS PSSWIGVFRN SSHHPWVTMN GLAFKHEIKD
210 220 230
SDNAELNCAV LQVNRLKSAQ CGSSIIYHCK HKL
Length:233
Mass (Da):26,314
Last modified:January 11, 2011 - v2
Checksum:i93879A5C8D110C62
GO
Isoform NKG2-B (identifier: P26715-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     96-113: Missing.

Show »
Length:215
Mass (Da):24,250
Checksum:iFEEE7322C85B2EAE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291N → S.5 Publications
Corresponds to variant rs2253849 [ dbSNP | Ensembl ].
VAR_050120

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei96 – 11318Missing in isoform NKG2-B. 2 PublicationsVSP_003062Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54867 mRNA. Translation: CAA38649.1.
X54868 mRNA. Translation: CAA38650.1.
U54786
, U54783, U54784, U54785 Genomic DNA. Translation: AAB17133.1.
AF023840 Genomic DNA. Translation: AAC17488.1.
AF461812 mRNA. Translation: AAL65234.1.
AC068775 Genomic DNA. No translation available.
BC012550 mRNA. Translation: AAH12550.1.
BC053840 mRNA. Translation: AAH53840.1.
CCDSiCCDS8625.1. [P26715-1]
CCDS8626.1. [P26715-2]
PIRiPT0372.
RefSeqiNP_002250.1. NM_002259.4.
NP_015567.1. NM_007328.3.
NP_998822.1. NM_213657.2.
NP_998823.1. NM_213658.2.
UniGeneiHs.512576.

Genome annotation databases

EnsembliENST00000347831; ENSP00000256965; ENSG00000134545. [P26715-2]
ENST00000359151; ENSP00000352064; ENSG00000134545. [P26715-1]
ENST00000408006; ENSP00000385304; ENSG00000134545. [P26715-2]
ENST00000544822; ENSP00000438038; ENSG00000134545. [P26715-1]
GeneIDi3821.
KEGGihsa:3821.
UCSCiuc001qyl.3. human. [P26715-1]
uc001qym.3. human. [P26715-2]

Polymorphism and mutation databases

BioMutaiKLRC1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

NKG-2A

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54867 mRNA. Translation: CAA38649.1.
X54868 mRNA. Translation: CAA38650.1.
U54786
, U54783, U54784, U54785 Genomic DNA. Translation: AAB17133.1.
AF023840 Genomic DNA. Translation: AAC17488.1.
AF461812 mRNA. Translation: AAL65234.1.
AC068775 Genomic DNA. No translation available.
BC012550 mRNA. Translation: AAH12550.1.
BC053840 mRNA. Translation: AAH53840.1.
CCDSiCCDS8625.1. [P26715-1]
CCDS8626.1. [P26715-2]
PIRiPT0372.
RefSeqiNP_002250.1. NM_002259.4.
NP_015567.1. NM_007328.3.
NP_998822.1. NM_213657.2.
NP_998823.1. NM_213658.2.
UniGeneiHs.512576.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RMXNMR-B1-15[»]
2YU7NMR-B33-47[»]
3BDWX-ray2.50B/D113-232[»]
3CDGX-ray3.40F/K113-232[»]
3CIIX-ray4.41H/J113-232[»]
ProteinModelPortaliP26715.
SMRiP26715. Positions 113-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110020. 3 interactions.
IntActiP26715. 2 interactions.
STRINGi9606.ENSP00000352064.

PTM databases

PhosphoSiteiP26715.

Polymorphism and mutation databases

BioMutaiKLRC1.
DMDMi317373399.

Proteomic databases

MaxQBiP26715.
PaxDbiP26715.
PRIDEiP26715.

Protocols and materials databases

DNASUi3821.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000347831; ENSP00000256965; ENSG00000134545. [P26715-2]
ENST00000359151; ENSP00000352064; ENSG00000134545. [P26715-1]
ENST00000408006; ENSP00000385304; ENSG00000134545. [P26715-2]
ENST00000544822; ENSP00000438038; ENSG00000134545. [P26715-1]
GeneIDi3821.
KEGGihsa:3821.
UCSCiuc001qyl.3. human. [P26715-1]
uc001qym.3. human. [P26715-2]

Organism-specific databases

CTDi3821.
GeneCardsiGC12M010708.
HGNCiHGNC:6374. KLRC1.
MIMi161555. gene.
neXtProtiNX_P26715.
PharmGKBiPA30163.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG146673.
GeneTreeiENSGT00730000110282.
HOGENOMiHOG000220925.
HOVERGENiHBG077044.
InParanoidiP26715.
KOiK06541.
OMAiPPNPKRQ.
PhylomeDBiP26715.
TreeFamiTF336674.

Enzyme and pathway databases

ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.

Miscellaneous databases

EvolutionaryTraceiP26715.
GenomeRNAii3821.
NextBioi15019.
PROiP26715.
SOURCEiSearch...

Gene expression databases

BgeeiP26715.
CleanExiHS_KLRC1.
ExpressionAtlasiP26715. baseline.
GenevestigatoriP26715.

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. "DNA sequence analysis of NKG2, a family of related cDNA clones encoding type II integral membrane proteins on human natural killer cells."
    Houchins J.P., Yabe T., McSherry C., Bach F.H.
    J. Exp. Med. 173:1017-1020(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NKG2-A AND NKG2-B), VARIANT SER-29.
  2. "Genomic structure, chromosome location, and alternative splicing of the human NKG2A gene."
    Plougastel B., Jones T., Trowsdale J.
    Immunogenetics 44:286-291(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS NKG2-A AND NKG2-B), VARIANT SER-29.
  3. "Sequence analysis of a 62-kb region overlapping the human KLRC cluster of genes."
    Plougastel B., Trowsdale J.
    Genomics 49:193-199(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS NKG2-A AND NKG2-B), VARIANT SER-29.
  4. "Identification and characterization of the NKG2A gene from large granular lymphocytic leukemia (LGL) cells."
    Kothapalli R., Kusmartseva I., Loughran T.P. Jr.
    Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-29.
  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] (ISOFORMS NKG2-A AND NKG2-B), VARIANT SER-29.
    Tissue: Blood and Kidney.
  7. "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 113-232 IN COMPLEX WITH KLRD1, SUBUNIT, DISULFIDE BONDS.
  8. "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 113-232 IN COMPLEX WITH KLRD1, SUBUNIT, DISULFIDE BONDS.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (4.41 ANGSTROMS) OF 113-232 IN COMPLEX WITH KLRD1, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiNKG2A_HUMAN
AccessioniPrimary (citable) accession number: P26715
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 11, 2011
Last modified: April 29, 2015
This is version 144 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.