NKG2F_HUMAN
ID NKG2F_HUMAN Reviewed; 158 AA.
AC O43908; O60851;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=NKG2-F type II integral membrane protein;
DE AltName: Full=NK cell receptor F;
DE AltName: Full=NKG2-F-activating NK receptor;
GN Name=KLRC4; Synonyms=NKG2F;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS SER-29 AND SER-104.
RX PubMed=9394807; DOI=10.1002/eji.1830271114;
RA Plougastel B., Trowsdale J.;
RT "Cloning of NKG2-F, a new member of the NKG2 family of human natural killer
RT cell receptor genes.";
RL Eur. J. Immunol. 27:2835-2839(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-29 AND SER-104.
RX PubMed=9598306; DOI=10.1006/geno.1997.5197;
RA Plougastel B., Trowsdale J.;
RT "Sequence analysis of a 62-kb region overlapping the human KLRC cluster of
RT genes.";
RL Genomics 49:193-199(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS SER-29 AND SER-104.
RX PubMed=9683661; DOI=10.1007/s002510050420;
RA Glienke J., Sobanov Y., Brostjan C., Steffens C., Nguyen C., Lehrach H.,
RA Hofer E., Francis F.;
RT "The genomic organization of NKG2C, E, F, and D receptor genes in the human
RT natural killer gene complex.";
RL Immunogenetics 48:163-173(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-29 AND SER-104.
RX PubMed=11751968; DOI=10.4049/jimmunol.168.1.240;
RA Shum B.P., Flodin L.R., Muir D.G., Rajalingam R., Khakoo S.I., Cleland S.,
RA Guethlein L.A., Uhrberg M., Parham P.;
RT "Conservation and variation in human and common chimpanzee CD94 and NKG2
RT genes.";
RL J. Immunol. 168:240-252(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May play a role as a receptor for the recognition of MHC
CC class I HLA-E molecules by NK cells.
CC -!- SUBUNIT: Can form disulfide-bonded heterodimer with CD94.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Natural killer cells.
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DR EMBL; U96846; AAC51910.1; -; Genomic_DNA.
DR EMBL; U96845; AAC51909.1; -; mRNA.
DR EMBL; AF027164; AAC17491.1; -; Genomic_DNA.
DR EMBL; AJ001683; CAA04921.1; -; mRNA.
DR EMBL; AJ001686; CAA04924.1; -; Genomic_DNA.
DR EMBL; AF350018; AAK83805.1; -; mRNA.
DR EMBL; AF350019; AAK83806.1; -; mRNA.
DR EMBL; AC022075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017784; AAH17784.1; -; mRNA.
DR CCDS; CCDS8624.1; -.
DR RefSeq; NP_038459.1; NM_013431.2.
DR AlphaFoldDB; O43908; -.
DR BioGRID; 113903; 35.
DR IntAct; O43908; 2.
DR STRING; 9606.ENSP00000310216; -.
DR TCDB; 1.C.111.1.14; the regiiiGama (regiiiGama) family.
DR iPTMnet; O43908; -.
DR PhosphoSitePlus; O43908; -.
DR BioMuta; KLRC4; -.
DR MassIVE; O43908; -.
DR PaxDb; O43908; -.
DR PeptideAtlas; O43908; -.
DR PRIDE; O43908; -.
DR ProteomicsDB; 49225; -.
DR Antibodypedia; 23310; 60 antibodies from 18 providers.
DR DNASU; 8302; -.
DR Ensembl; ENST00000309384.3; ENSP00000310216.1; ENSG00000183542.6.
DR GeneID; 8302; -.
DR KEGG; hsa:8302; -.
DR MANE-Select; ENST00000309384.3; ENSP00000310216.1; NM_013431.2; NP_038459.1.
DR UCSC; uc001qye.4; human.
DR CTD; 8302; -.
DR DisGeNET; 8302; -.
DR GeneCards; KLRC4; -.
DR HGNC; HGNC:6377; KLRC4.
DR HPA; ENSG00000183542; Tissue enhanced (lymphoid).
DR MalaCards; KLRC4; -.
DR MIM; 602893; gene.
DR neXtProt; NX_O43908; -.
DR OpenTargets; ENSG00000183542; -.
DR Orphanet; 117; Behcet disease.
DR PharmGKB; PA30166; -.
DR VEuPathDB; HostDB:ENSG00000183542; -.
DR eggNOG; ENOG502S6IE; Eukaryota.
DR GeneTree; ENSGT00940000166632; -.
DR HOGENOM; CLU_049894_9_4_1; -.
DR InParanoid; O43908; -.
DR OMA; EEILICF; -.
DR OrthoDB; 1161111at2759; -.
DR PhylomeDB; O43908; -.
DR PathwayCommons; O43908; -.
DR SignaLink; O43908; -.
DR BioGRID-ORCS; 8302; 20 hits in 986 CRISPR screens.
DR GeneWiki; KLRC4; -.
DR GenomeRNAi; 8302; -.
DR Pharos; O43908; Tbio.
DR PRO; PR:O43908; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O43908; protein.
DR Bgee; ENSG00000183542; Expressed in granulocyte and 103 other tissues.
DR Genevisible; O43908; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IBA:GO_Central.
DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR SUPFAM; SSF56436; SSF56436; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Membrane; Receptor; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..158
FT /note="NKG2-F type II integral membrane protein"
FT /id="PRO_0000046673"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 29
FT /note="I -> S (in allele NKG2-F*02; dbSNP:rs1841958)"
FT /evidence="ECO:0000269|PubMed:11751968,
FT ECO:0000269|PubMed:9394807, ECO:0000269|PubMed:9598306,
FT ECO:0000269|PubMed:9683661"
FT /id="VAR_013406"
FT VARIANT 104
FT /note="N -> S (in allele NKG2-F*02; dbSNP:rs2617170)"
FT /evidence="ECO:0000269|PubMed:11751968,
FT ECO:0000269|PubMed:9394807, ECO:0000269|PubMed:9598306,
FT ECO:0000269|PubMed:9683661"
FT /id="VAR_013407"
SQ SEQUENCE 158 AA; 18234 MW; 1AABC0E5ED26ACCC CRC64;
MNKQRGTYSE VSLAQDPKRQ QRKLKGNKIS ISGTKQEIFQ VELNLQNASS DHQGNDKTYH
CKGLLPPPEK LTAEVLGIIC IVLMATVLKT IVLIPCIGVL EQNNFSLNRR MQKARHCGHC
PEEWITYSNS CYYIGKERRT WEERVCWPVL RRTLICFL
