KI2L1_HUMAN
ID KI2L1_HUMAN Reviewed; 348 AA.
AC P43626; O43470; Q32WE6; Q6IST4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Killer cell immunoglobulin-like receptor 2DL1 {ECO:0000305};
DE AltName: Full=CD158 antigen-like family member A;
DE AltName: Full=Natural killer-associated transcript 1;
DE Short=NKAT-1;
DE AltName: Full=p58 natural killer cell receptor clones CL-42/47.11;
DE Short=p58 NK receptor CL-42/47.11;
DE AltName: Full=p58.1 MHC class-I-specific NK receptor;
DE AltName: CD_antigen=CD158a;
DE Flags: Precursor;
GN Name=KIR2DL1 {ECO:0000312|HGNC:HGNC:6329}; Synonyms=CD158A, NKAT1;
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 1).
RC TISSUE=Natural killer cell;
RX PubMed=7716543; DOI=10.1126/science.7716543;
RA Colonna M., Samaridis J.;
RT "Cloning of immunoglobulin-superfamily members associated with HLA-C and
RT HLA-B recognition by human natural killer cells.";
RL Science 268:405-408(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 22-45.
RC TISSUE=Natural killer cell;
RX PubMed=7749980; DOI=10.1016/1074-7613(95)90025-x;
RA Wagtmann N., Biassoni R., Cantoni C., Verdiani S., Malnati M.S., Vitale M.,
RA Bottino C., Moretta L., Moretta A., Long E.O.;
RT "Molecular clones of the p58 NK cell receptor reveal immunoglobulin-related
RT molecules with diversity in both the extra- and intracellular domains.";
RL Immunity 2:439-449(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS.
RX PubMed=9430221; DOI=10.1016/s1074-7613(00)80394-5;
RA Uhrberg M., Valiante N.M., Shum B.P., Shilling H.G., Lienert-Weidenbach K.,
RA Corliss B., Tyan D., Lanier L.L., Parham P.;
RT "Human diversity in killer cell inhibitory receptor genes.";
RL Immunity 7:753-763(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PHE-5.
RA Yawata N., Yawata M., Parham P.;
RT "Variants of KIR identified in Japanese donors.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ARG-37 AND
RP LEU-135.
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=18624290; DOI=10.1002/eji.200838434;
RA Della Chiesa M., Romeo E., Falco M., Balsamo M., Augugliaro R., Moretta L.,
RA Bottino C., Moretta A., Vitale M.;
RT "Evidence that the KIR2DS5 gene codes for a surface receptor triggering
RT natural killer cell function.";
RL Eur. J. Immunol. 38:2284-2289(2008).
RN [8]
RP FUNCTION, INTERACTION WITH ARRB2; PTPN6 AND PTPN11, AND MUTAGENESIS OF
RP TYR-302 AND TYR-332.
RX PubMed=18604210; DOI=10.1038/ni.1635;
RA Yu M.-C., Su L.-L., Zou L., Liu Y., Wu N., Kong L., Zhuang Z.-H., Sun L.,
RA Liu H.P., Hu J.-H., Li D., Strominger J.L., Zang J.-W., Pei G., Ge B.-X.;
RT "An essential function for beta-arrestin 2 in the inhibitory signaling of
RT natural killer cells.";
RL Nat. Immunol. 9:898-907(2008).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 22-221, AND DISULFIDE BONDS.
RX PubMed=9288975; DOI=10.1038/38028;
RA Fan Q.R., Mosyak L., Winter C.C., Wagtmann N., Long E.O., Wiley D.C.;
RT "Structure of the inhibitory receptor for human natural killer cells
RT resembles haematopoietic receptors.";
RL Nature 389:96-100(1997).
CC -!- FUNCTION: Receptor on natural killer (NK) cells for some HLA-C alleles
CC such as w4 and w6. Inhibits the activity of NK cells thus preventing
CC cell lysis. {ECO:0000269|PubMed:18604210}.
CC -!- SUBUNIT: Interacts with ARRB2. Interacts with PTPN6; the interaction is
CC enhanced by ARRB2. Interacts with PTPN11; the interaction is enhanced
CC by ARRB2. {ECO:0000269|PubMed:18604210}.
CC -!- INTERACTION:
CC P43626; P01889: HLA-B; NbExp=2; IntAct=EBI-8684277, EBI-1046513;
CC P43626; P10321: HLA-C; NbExp=12; IntAct=EBI-8684277, EBI-1051396;
CC P43626; Q7YQB1: HLA-C; NbExp=2; IntAct=EBI-8684277, EBI-22185948;
CC P43626; Q5RIP0: HLA-Cw; NbExp=2; IntAct=EBI-8684277, EBI-22185566;
CC P43626; P29350: PTPN6; NbExp=4; IntAct=EBI-8684277, EBI-78260;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18624290};
CC Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43626-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43626-2; Sequence=VSP_056314;
CC -!- TISSUE SPECIFICITY: Expressed by NK cells.
CC {ECO:0000269|PubMed:9430221}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; L41267; AAA69868.1; -; mRNA.
DR EMBL; U24076; AAC50335.1; -; mRNA.
DR EMBL; U24078; AAC50337.1; -; mRNA.
DR EMBL; AF022045; AAB95318.1; -; mRNA.
DR EMBL; AY789055; AAX23100.1; -; mRNA.
DR EMBL; AC011501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069344; AAH69344.1; -; mRNA.
DR CCDS; CCDS12904.1; -. [P43626-1]
DR PIR; A56247; A56247.
DR RefSeq; NP_055033.2; NM_014218.2.
DR PDB; 1IM9; X-ray; 2.80 A; D=22-245.
DR PDB; 1NKR; X-ray; 1.70 A; A=22-221.
DR PDBsum; 1IM9; -.
DR PDBsum; 1NKR; -.
DR AlphaFoldDB; P43626; -.
DR SMR; P43626; -.
DR BioGRID; 110003; 29.
DR IntAct; P43626; 16.
DR MINT; P43626; -.
DR STRING; 9606.ENSP00000336769; -.
DR ChEMBL; CHEMBL3712912; -.
DR GlyGen; P43626; 4 sites.
DR iPTMnet; P43626; -.
DR PhosphoSitePlus; P43626; -.
DR BioMuta; KIR2DL1; -.
DR DMDM; 1171726; -.
DR jPOST; P43626; -.
DR MassIVE; P43626; -.
DR PaxDb; P43626; -.
DR PeptideAtlas; P43626; -.
DR PRIDE; P43626; -.
DR ABCD; P43626; 1 sequenced antibody.
DR Antibodypedia; 21559; 743 antibodies from 27 providers.
DR DNASU; 3802; -.
DR Ensembl; ENST00000291633.7; ENSP00000291633.7; ENSG00000125498.20.
DR Ensembl; ENST00000611611.4; ENSP00000478232.1; ENSG00000278738.5.
DR Ensembl; ENST00000615920.4; ENSP00000482120.1; ENSG00000273794.4.
DR Ensembl; ENST00000617376.1; ENSP00000484559.1; ENSG00000278821.4.
DR Ensembl; ENST00000618563.1; ENSP00000484361.1; ENSG00000276625.4.
DR Ensembl; ENST00000620449.1; ENSP00000478263.1; ENSG00000277833.4.
DR Ensembl; ENST00000622463.4; ENSP00000479363.1; ENSG00000278495.4.
DR GeneID; 3802; -.
DR KEGG; hsa:3802; -.
DR UCSC; uc010erz.2; human. [P43626-1]
DR CTD; 3802; -.
DR DisGeNET; 3802; -.
DR GeneCards; KIR2DL1; -.
DR HGNC; HGNC:6329; KIR2DL1.
DR HPA; ENSG00000125498; Tissue enhanced (lymphoid).
DR MIM; 604936; gene.
DR neXtProt; NX_P43626; -.
DR PharmGKB; PA30114; -.
DR VEuPathDB; HostDB:ENSG00000125498; -.
DR eggNOG; ENOG502RU21; Eukaryota.
DR InParanoid; P43626; -.
DR OrthoDB; 1055520at2759; -.
DR PhylomeDB; P43626; -.
DR TreeFam; TF352669; -.
DR PathwayCommons; P43626; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; P43626; -.
DR BioGRID-ORCS; 3802; 9 hits in 1002 CRISPR screens.
DR EvolutionaryTrace; P43626; -.
DR GeneWiki; KIR2DL1; -.
DR GenomeRNAi; 3802; -.
DR Pharos; P43626; Tbio.
DR PRO; PR:P43626; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P43626; protein.
DR Bgee; ENSG00000125498; Expressed in granulocyte and 26 other tissues.
DR ExpressionAtlas; P43626; baseline and differential.
DR Genevisible; P43626; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0002769; P:natural killer cell inhibitory signaling pathway; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 2.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:7749980"
FT CHAIN 22..348
FT /note="Killer cell immunoglobulin-like receptor 2DL1"
FT /id="PRO_0000015078"
FT TOPO_DOM 22..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..107
FT /note="Ig-like C2-type 1"
FT DOMAIN 142..205
FT /note="Ig-like C2-type 2"
FT REGION 220..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..100
FT /evidence="ECO:0000269|PubMed:9288975,
FT ECO:0007744|PDB:1NKR"
FT DISULFID 149..198
FT /evidence="ECO:0000269|PubMed:9288975,
FT ECO:0007744|PDB:1NKR"
FT VAR_SEQ 238..239
FT /note="TG -> TERMFHHVGQACLKLPTSSDPTVSACQS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056314"
FT VARIANT 5
FT /note="V -> F (in dbSNP:rs2304224)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_003949"
FT VARIANT 9
FT /note="A -> V (in dbSNP:rs3810343)"
FT /id="VAR_061332"
FT VARIANT 37
FT /note="P -> R (in dbSNP:rs35509911)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_003950"
FT VARIANT 66
FT /note="F -> Y (in dbSNP:rs673568)"
FT /id="VAR_056091"
FT VARIANT 111
FT /note="V -> L (in dbSNP:rs687885)"
FT /id="VAR_061333"
FT VARIANT 135
FT /note="P -> L (in dbSNP:rs11673144)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_003951"
FT VARIANT 175
FT /note="P -> T (in dbSNP:rs111799279)"
FT /id="VAR_010331"
FT VARIANT 184
FT /note="D -> N (in dbSNP:rs147072532)"
FT /id="VAR_010332"
FT VARIANT 203
FT /note="H -> R (in dbSNP:rs666590)"
FT /id="VAR_010333"
FT VARIANT 237
FT /note="K -> E (in dbSNP:rs75232650)"
FT /id="VAR_010334"
FT VARIANT 266
FT /note="R -> C (in dbSNP:rs34721508)"
FT /id="VAR_010335"
FT MUTAGEN 302
FT /note="Y->A: Abolishes interaction with ARRB2; when
FT associated with A-332. Diminishes interaction with ARRB2."
FT /evidence="ECO:0000269|PubMed:18604210"
FT MUTAGEN 332
FT /note="Y->A: Abolishes interaction with ARRB2; when
FT associated with A-302."
FT /evidence="ECO:0000269|PubMed:18604210"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 80..89
FT /evidence="ECO:0007829|PDB:1NKR"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 194..202
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1NKR"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:1NKR"
SQ SEQUENCE 348 AA; 38505 MW; 3DFBF2D6FDCE1D1E CRC64;
MSLLVVSMAC VGFFLLQGAW PHEGVHRKPS LLAHPGPLVK SEETVILQCW SDVMFEHFLL
HREGMFNDTL RLIGEHHDGV SKANFSISRM TQDLAGTYRC YGSVTHSPYQ VSAPSDPLDI
VIIGLYEKPS LSAQPGPTVL AGENVTLSCS SRSSYDMYHL SREGEAHERR LPAGPKVNGT
FQADFPLGPA THGGTYRCFG SFHDSPYEWS KSSDPLLVSV TGNPSNSWPS PTEPSSKTGN
PRHLHILIGT SVVIILFILL FFLLHRWCSN KKNAAVMDQE SAGNRTANSE DSDEQDPQEV
TYTQLNHCVF TQRKITRPSQ RPKTPPTDII VYTELPNAES RSKVVSCP
