KLRG1_HUMAN
ID KLRG1_HUMAN Reviewed; 195 AA.
AC Q96E93; B7ZAM2; O43198; O75613;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Killer cell lectin-like receptor subfamily G member 1;
DE AltName: Full=C-type lectin domain family 15 member A;
DE AltName: Full=ITIM-containing receptor MAFA-L;
DE AltName: Full=MAFA-like receptor;
DE AltName: Full=Mast cell function-associated antigen;
GN Name=KLRG1; Synonyms=CLEC15A, MAFA, MAFAL;
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 [MRNA] (ISOFORM 2).
RX PubMed=9765598; DOI=10.1016/s0167-4781(98)00107-9;
RA Lamers M.B.A.C., Lamont A.G., Williams D.H.;
RT "Human MAFA has alternatively spliced variants.";
RL Biochim. Biophys. Acta 1399:209-212(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=9842918;
RX DOI=10.1002/(sici)1521-4141(199811)28:11<3755::aid-immu3755>3.0.co;2-3;
RA Butcher S., Arney K.L., Cook G.P.;
RT "MAFA-L, an ITIM-containing receptor encoded by the human NK cell gene
RT complex and expressed by basophils and NK cells.";
RL Eur. J. Immunol. 28:3755-3762(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
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).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION BY VIRUSES AND PATHOGENS INFECTIONS.
RX PubMed=15879103; DOI=10.4049/jimmunol.174.10.6088;
RA Ibegbu C.C., Xu Y.X., Harris W., Maggio D., Miller J.D., Kourtis A.P.;
RT "Expression of killer cell lectin-like receptor G1 on antigen-specific
RT human CD8+ T lymphocytes during active, latent, and resolved infection and
RT its relation with CD57.";
RL J. Immunol. 174:6088-6094(2005).
RN [7]
RP LIGAND-BINDING.
RX PubMed=17617594; DOI=10.4049/jimmunol.179.2.1022;
RA Schwartzkopff S., Gruendemann C., Schweier O., Rosshart S.,
RA Karjalainen K.E., Becker K.-F., Pircher H.;
RT "Tumor-associated E-cadherin mutations affect binding to the killer cell
RT lectin-like receptor G1 in humans.";
RL J. Immunol. 179:1022-1029(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 75-186 IN COMPLEX WITH CDH1,
RP FUNCTION, SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RX PubMed=19604491; DOI=10.1016/j.immuni.2009.04.019;
RA Li Y., Hofmann M., Wang Q., Teng L., Chlewicki L.K., Pircher H.,
RA Mariuzza R.A.;
RT "Structure of natural killer cell receptor KLRG1 bound to E-cadherin
RT reveals basis for MHC-independent missing self recognition.";
RL Immunity 31:35-46(2009).
CC -!- FUNCTION: Plays an inhibitory role on natural killer (NK) cells and T-
CC cell functions upon binding to their non-MHC ligands. May mediate
CC missing self recognition by binding to a highly conserved site on
CC classical cadherins, enabling it to monitor expression of E-
CC cadherin/CDH1, N-cadherin/CDH2 and R-cadherin/CDH4 on target cells.
CC {ECO:0000269|PubMed:19604491}.
CC -!- SUBUNIT: Forms a monomer and homodimer; disulfide-linked. Interacts
CC (via ITIM motif) with PTPN11 and INPP5D. {ECO:0000250}.
CC -!- INTERACTION:
CC Q96E93; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-750770, EBI-11343438;
CC Q96E93; O15529: GPR42; NbExp=3; IntAct=EBI-750770, EBI-18076404;
CC Q96E93; Q8TED1: GPX8; NbExp=3; IntAct=EBI-750770, EBI-11721746;
CC Q96E93; P26715: KLRC1; NbExp=3; IntAct=EBI-750770, EBI-9018187;
CC Q96E93; O95214: LEPROTL1; NbExp=4; IntAct=EBI-750770, EBI-750776;
CC Q96E93; Q6IN84: MRM1; NbExp=3; IntAct=EBI-750770, EBI-5454865;
CC Q96E93; P16284: PECAM1; NbExp=3; IntAct=EBI-750770, EBI-716404;
CC Q96E93; Q8N205: SYNE4; NbExp=3; IntAct=EBI-750770, EBI-7131783;
CC Q96E93; P37173: TGFBR2; NbExp=3; IntAct=EBI-750770, EBI-296151;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19604491};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:19604491}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96E93-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96E93-2; Sequence=VSP_033151;
CC -!- TISSUE SPECIFICITY: Expressed specifically on natural killer (NK) cells
CC and T-cells, mainly CD8 T-cells. {ECO:0000269|PubMed:15879103,
CC ECO:0000269|PubMed:9842918}.
CC -!- INDUCTION: By pathogens and viruses infections.
CC {ECO:0000269|PubMed:15879103}.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. Upon phosphorylation of
CC ITIM motif KLRG1 associates with the two phosphatases PTPN11 and INPP5D
CC (By similarity). {ECO:0000250}.
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DR EMBL; AF034952; AAC34731.1; -; mRNA.
DR EMBL; AF081675; AAC32200.1; -; mRNA.
DR EMBL; AF097358; AAD03719.1; -; mRNA.
DR EMBL; AK316337; BAH14708.1; -; mRNA.
DR EMBL; CH471116; EAW88594.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88595.1; -; Genomic_DNA.
DR EMBL; BC012621; AAH12621.1; -; mRNA.
DR CCDS; CCDS8599.1; -. [Q96E93-2]
DR CCDS; CCDS86277.1; -. [Q96E93-1]
DR RefSeq; NP_001316028.1; NM_001329099.1. [Q96E93-1]
DR RefSeq; NP_005801.3; NM_005810.3. [Q96E93-2]
DR PDB; 3FF7; X-ray; 1.80 A; C/D=75-186.
DR PDBsum; 3FF7; -.
DR AlphaFoldDB; Q96E93; -.
DR SMR; Q96E93; -.
DR BioGRID; 115514; 7.
DR IntAct; Q96E93; 9.
DR STRING; 9606.ENSP00000349477; -.
DR GlyGen; Q96E93; 4 sites.
DR iPTMnet; Q96E93; -.
DR PhosphoSitePlus; Q96E93; -.
DR BioMuta; KLRG1; -.
DR DMDM; 74731536; -.
DR MassIVE; Q96E93; -.
DR MaxQB; Q96E93; -.
DR PaxDb; Q96E93; -.
DR PeptideAtlas; Q96E93; -.
DR PRIDE; Q96E93; -.
DR Antibodypedia; 23119; 442 antibodies from 34 providers.
DR DNASU; 10219; -.
DR Ensembl; ENST00000266551.8; ENSP00000266551.4; ENSG00000139187.10. [Q96E93-1]
DR Ensembl; ENST00000356986.8; ENSP00000349477.3; ENSG00000139187.10. [Q96E93-2]
DR GeneID; 10219; -.
DR KEGG; hsa:10219; -.
DR MANE-Select; ENST00000356986.8; ENSP00000349477.3; NM_005810.4; NP_005801.3. [Q96E93-2]
DR UCSC; uc001qvg.4; human. [Q96E93-1]
DR CTD; 10219; -.
DR DisGeNET; 10219; -.
DR GeneCards; KLRG1; -.
DR HGNC; HGNC:6380; KLRG1.
DR HPA; ENSG00000139187; Tissue enhanced (lymphoid).
DR MIM; 604874; gene.
DR neXtProt; NX_Q96E93; -.
DR OpenTargets; ENSG00000139187; -.
DR PharmGKB; PA30170; -.
DR VEuPathDB; HostDB:ENSG00000139187; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000156296; -.
DR HOGENOM; CLU_049894_8_3_1; -.
DR InParanoid; Q96E93; -.
DR OMA; SCPDFWM; -.
DR OrthoDB; 1299162at2759; -.
DR PhylomeDB; Q96E93; -.
DR TreeFam; TF336674; -.
DR PathwayCommons; Q96E93; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; Q96E93; -.
DR BioGRID-ORCS; 10219; 8 hits in 1065 CRISPR screens.
DR ChiTaRS; KLRG1; human.
DR EvolutionaryTrace; Q96E93; -.
DR GeneWiki; KLRG1; -.
DR GenomeRNAi; 10219; -.
DR Pharos; Q96E93; Tbio.
DR PRO; PR:Q96E93; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96E93; protein.
DR Bgee; ENSG00000139187; Expressed in granulocyte and 105 other tissues.
DR ExpressionAtlas; Q96E93; baseline and differential.
DR Genevisible; Q96E93; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR042190; KLRG1.
DR InterPro; IPR033992; NKR-like_CTLD.
DR PANTHER; PTHR47648; PTHR47648; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Innate immunity; Lectin; Membrane; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..195
FT /note="Killer cell lectin-like receptor subfamily G member
FT 1"
FT /id="PRO_0000331256"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 82..185
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 5..10
FT /note="ITIM motif"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19604491"
FT DISULFID 103..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19604491"
FT DISULFID 163..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:19604491"
FT VAR_SEQ 187..195
FT /note="CPFADQALF -> VRL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9765598, ECO:0000303|PubMed:9842918"
FT /id="VSP_033151"
FT VARIANT 58
FT /note="W -> R (in dbSNP:rs1805749)"
FT /id="VAR_042750"
FT CONFLICT 32
FT /note="R -> K (in Ref. 1; AAC34731)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="A -> T (in Ref. 1; AAC34731)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="W -> G (in Ref. 1; AAC34731)"
FT /evidence="ECO:0000305"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3FF7"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:3FF7"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:3FF7"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3FF7"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:3FF7"
FT STRAND 131..143
FT /evidence="ECO:0007829|PDB:3FF7"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:3FF7"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:3FF7"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:3FF7"
SQ SEQUENCE 195 AA; 21831 MW; 178EE98E08EEC473 CRC64;
MTDSVIYSML ELPTATQAQN DYGPQQKSSS SRPSCSCLVA IALGLLTAVL LSVLLYQWIL
CQGSNYSTCA SCPSCPDRWM KYGNHCYYFS VEEKDWNSSL EFCLARDSHL LVITDNQEMS
LLQVFLSEAF CWIGLRNNSG WRWEDGSPLN FSRISSNSFV QTCGAINKNG LQASSCEVPL
HWVCKKCPFA DQALF
