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Protein

NKG2-C type II integral membrane protein

Gene

KLRC2

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. protein antigen binding Source: UniProtKB
  4. transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  1. cellular defense response Source: ProtInc
  2. innate immune response Source: Reactome
  3. natural killer cell mediated immunity Source: UniProtKB
  4. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiREACT_147694. DAP12 interactions.
REACT_147814. DAP12 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
NKG2-C type II integral membrane protein
Alternative name(s):
CD159 antigen-like family member C
NK cell receptor C
NKG2-C-activating NK receptor
CD_antigen: CD159c
Gene namesi
Name:KLRC2
Synonyms:NKG2C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:6375. KLRC2.

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 – 231138ExtracellularSequence 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

PharmGKBiPA30164.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 231231NKG2-C type II integral membrane proteinPRO_0000046662Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi117 ↔ 128PROSITE-ProRule annotation
Disulfide bondi145 ↔ 227PROSITE-ProRule annotation
Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi206 ↔ 219PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP26717.
PRIDEiP26717.

Expressioni

Tissue specificityi

Natural killer cells.

Gene expression databases

BgeeiP26717.
CleanExiHS_KLRC2.
ExpressionAtlasiP26717. baseline and differential.
GenevestigatoriP26717.

Interactioni

Subunit structurei

Can form disulfide-bonded heterodimer with CD94. Interacts with TYROBP.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TYROBPO439142EBI-3862171,EBI-2214794

Protein-protein interaction databases

BioGridi110021. 2 interactions.
IntActiP26717. 2 interactions.
STRINGi9606.ENSP00000371327.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi76 – 9722

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L35NMR-A72-100[»]
ProteinModelPortaliP26717.
SMRiP26717. Positions 72-99, 111-230.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26717.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 229114C-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

eggNOGiNOG145472.
HOGENOMiHOG000220925.
HOVERGENiHBG077044.
InParanoidiP26717.
KOiK06541.
PhylomeDBiP26717.
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]

Sequencei

Sequence statusi: Complete.

P26717-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKQRGTFSE VSLAQDPKRQ QRKPKGNKSS ISGTEQEIFQ VELNLQNPSL
60 70 80 90 100
NHQGIDKIYD CQGLLPPPEK LTAEVLGIIC IVLMATVLKT IVLIPFLEQN
110 120 130 140 150
NSSPNTRTQK ARHCGHCPEE WITYSNSCYY IGKERRTWEE SLLACTSKNS
160 170 180 190 200
SLLSIDNEEE MKFLASILPS SWIGVFRNSS HHPWVTINGL AFKHKIKDSD
210 220 230
NAELNCAVLQ VNRLKSAQCG SSMIYHCKHK L
Length:231
Mass (Da):26,072
Last modified:January 23, 2002 - v2
Checksum:i6B971EECD7542930
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1611M → I in CAA38651 (PubMed:2007850).Curated

Polymorphismi

Two alleles are known. The sequence shown is that of allele NKG2-C*01.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21S → N in allele NKG2-C*02. 1 Publication
Corresponds to variant rs28403159 [ dbSNP | Ensembl ].
VAR_013404
Natural varianti102 – 1021S → F in allele NKG2-C*02. 1 Publication
VAR_013405

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54869 mRNA. Translation: CAA38651.1.
AJ001684 Genomic DNA. Translation: CAA04922.1.
AF260134 mRNA. Translation: AAF86972.1.
Y13055 mRNA. Translation: CAA73498.1.
AC068775 Genomic DNA. No translation available.
BC093644 mRNA. Translation: AAH93644.1.
BC112039 mRNA. Translation: AAI12040.1.
CCDSiCCDS31745.1.
PIRiPT0374.
RefSeqiNP_002251.2. NM_002260.3.
UniGeneiHs.591157.

Genome annotation databases

EnsembliENST00000381902; ENSP00000371327; ENSG00000205809.
GeneIDi3822.
KEGGihsa:3822.

Polymorphism databases

DMDMi20141529.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54869 mRNA. Translation: CAA38651.1.
AJ001684 Genomic DNA. Translation: CAA04922.1.
AF260134 mRNA. Translation: AAF86972.1.
Y13055 mRNA. Translation: CAA73498.1.
AC068775 Genomic DNA. No translation available.
BC093644 mRNA. Translation: AAH93644.1.
BC112039 mRNA. Translation: AAI12040.1.
CCDSiCCDS31745.1.
PIRiPT0374.
RefSeqiNP_002251.2. NM_002260.3.
UniGeneiHs.591157.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L35NMR-A72-100[»]
ProteinModelPortaliP26717.
SMRiP26717. Positions 72-99, 111-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110021. 2 interactions.
IntActiP26717. 2 interactions.
STRINGi9606.ENSP00000371327.

Polymorphism databases

DMDMi20141529.

Proteomic databases

PaxDbiP26717.
PRIDEiP26717.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381902; ENSP00000371327; ENSG00000205809.
GeneIDi3822.
KEGGihsa:3822.

Organism-specific databases

CTDi3822.
GeneCardsiGC12M010690.
HGNCiHGNC:6375. KLRC2.
MIMi602891. gene.
neXtProtiNX_P26717.
PharmGKBiPA30164.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG145472.
HOGENOMiHOG000220925.
HOVERGENiHBG077044.
InParanoidiP26717.
KOiK06541.
PhylomeDBiP26717.
TreeFamiTF336674.

Enzyme and pathway databases

ReactomeiREACT_147694. DAP12 interactions.
REACT_147814. DAP12 signaling.

Miscellaneous databases

EvolutionaryTraceiP26717.
GeneWikiiKLRC2.
GenomeRNAii3822.
NextBioi15029.
PROiP26717.
SOURCEiSearch...

Gene expression databases

BgeeiP26717.
CleanExiHS_KLRC2.
ExpressionAtlasiP26717. baseline and differential.
GenevestigatoriP26717.

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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genomic organization of NKG2C, E, F, and D receptor genes in the human natural killer gene complex."
    Glienke J., Sobanov Y., Brostjan C., Steffens C., Nguyen C., Lehrach H., Hofer E., Francis F.
    Immunogenetics 48:163-173(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Conservation and variation in human and common chimpanzee CD94 and NKG2 genes."
    Shum B.P., Flodin L.R., Muir D.G., Rajalingam R., Khakoo S.I., Cleland S., Guethlein L.A., Uhrberg M., Parham P.
    J. Immunol. 168:240-252(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-2 AND PHE-102.
  4. Biassoni R.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoid tissue.
  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(2005) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  7. "The structural basis for intramembrane assembly of an activating immunoreceptor complex."
    Call M.E., Wucherpfennig K.W., Chou J.J.
    Nat. Immunol. 11:1023-1029(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 72-100 IN COMPLEX WITH TYROBP, INTERACTION WITH TYROBP.

Entry informationi

Entry nameiNKG2C_HUMAN
AccessioniPrimary (citable) accession number: P26717
Secondary accession number(s): O43802, Q52M74, Q9NR42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2002
Last modified: March 4, 2015
This is version 126 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.