ID   KI2L4_HUMAN             Reviewed;         377 AA.
AC   Q99706; A8W795; O14621; O14622; O14623; O14624; O43534; P78400; P78401;
AC   Q8N738; Q99559; Q99560; Q99561; Q99562; Q9UQJ7;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 3.
DT   05-FEB-2025, entry version 208.
DE   RecName: Full=Killer cell immunoglobulin-like receptor 2DL4;
DE   AltName: Full=CD158 antigen-like family member D;
DE   AltName: Full=G9P;
DE   AltName: Full=Killer cell inhibitory receptor 103AS;
DE            Short=KIR-103AS;
DE   AltName: Full=MHC class I NK cell receptor KIR103AS;
DE   AltName: CD_antigen=CD158d {ECO:0000303|PubMed:23184984};
DE   Flags: Precursor;
GN   Name=KIR2DL4 {ECO:0000303|PubMed:18082267, ECO:0000303|PubMed:23184984,
GN   ECO:0000312|HGNC:HGNC:6332}; Synonyms=CD158D, KIR103AS;
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], AND VARIANTS LEU-87; THR-138; ALA-209 AND
RP   HIS-371.
RX   PubMed=8946682; DOI=10.1111/j.1399-0039.1996.tb02647.x;
RA   Selvakumar A., Steffens U., Dupont B.;
RT   "NK cell receptor gene of the KIR family with two IG domains but highest
RT   homology to KIR receptors with three IG domains.";
RL   Tissue Antigens 48:285-294(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS CYS-53; THR-138; ALA-209; ASN-271
RP   AND HIS-371.
RX   PubMed=9430220; DOI=10.1016/s1074-7613(00)80393-3;
RA   Valiante N.M., Uhrberg M., Shilling H.G., Lienert-Weidenbach K.,
RA   Arnett K.L., D'Andrea A., Phillips J.H., Lanier L.L., Parham P.;
RT   "Functionally and structurally distinct NK cell receptor repertoires in the
RT   peripheral blood of two human donors.";
RL   Immunity 7:739-751(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS LEU-87; THR-138;
RP   ALA-209 AND HIS-371.
RX   PubMed=9059894; DOI=10.1111/j.1600-065x.1997.tb00951.x;
RA   Selvakumar A., Steffens U., Dupont B.;
RT   "Polymorphism and domain variability of human killer cell inhibitory
RT   receptors.";
RL   Immunol. Rev. 155:183-196(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 3; 4 AND 5), AND
RP   VARIANTS LEU-87; THR-138; ALA-209; ASN-271 AND HIS-371.
RX   PubMed=9234477; DOI=10.1111/j.1399-0039.1997.tb02803.x;
RA   Selvakumar A., Steffens U., Palanisamy N., Chaganti R.S.K., Dupont B.;
RT   "Genomic organization and allelic polymorphism of the human killer cell
RT   inhibitory receptor gene KIR103.";
RL   Tissue Antigens 49:564-573(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELE KIR2DL4*0501), AND VARIANT CYS-53.
RX   PubMed=18082267; DOI=10.1016/j.molimm.2007.10.038;
RA   Schellekens J., Tilanus M.G., Rozemuller E.H.;
RT   "The elucidation of KIR2DL4 gene polymorphism.";
RL   Mol. Immunol. 45:1900-1906(2008).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 6), AND VARIANTS THR-138;
RP   ALA-209 AND ASN-271.
RC   TISSUE=Lymphoid tissue;
RA   Biassoni R.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-53 AND ASN-271.
RA   Chan H.W., Salter R.D.;
RT   "Exon deletion contributes to structural diversity of 2DL4 killer
RT   inhibitory receptors.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [8]
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   [9]
RP   FUNCTION, SUBUNIT, AND INTERACTION WITH HLA-G.
RX   PubMed=10190900; DOI=10.1084/jem.189.7.1093;
RA   Rajagopalan S., Long E.O.;
RT   "A human histocompatibility leukocyte antigen (HLA)-G-specific receptor
RT   expressed on all natural killer cells.";
RL   J. Exp. Med. 189:1093-1100(1999).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH HLA-G, AND
RP   MUTAGENESIS OF 246-ARG-TYR-247.
RX   PubMed=16366734; DOI=10.1371/journal.pbio.0040009;
RA   Rajagopalan S., Bryceson Y.T., Kuppusamy S.P., Geraghty D.E.,
RA   van der Meer A., Joosten I., Long E.O.;
RT   "Activation of NK cells by an endocytosed receptor for soluble HLA-G.";
RL   PLoS Biol. 4:E9-E9(2006).
RN   [11]
RP   INTERACTION WITH ARRB2.
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   [12]
RP   TISSUE SPECIFICITY.
RX   PubMed=19304799; DOI=10.1073/pnas.0901173106;
RA   Li C., Houser B.L., Nicotra M.L., Strominger J.L.;
RT   "HLA-G homodimer-induced cytokine secretion through HLA-G receptors on
RT   human decidual macrophages and natural killer cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5767-5772(2009).
RN   [13]
RP   FUNCTION.
RX   PubMed=20179272; DOI=10.1126/scisignal.2000467;
RA   Rajagopalan S., Moyle M.W., Joosten I., Long E.O.;
RT   "DNA-PKcs controls an endosomal signaling pathway for a proinflammatory
RT   response by natural killer cells.";
RL   Sci. Signal. 3:RA14-RA14(2010).
RN   [14]
RP   FUNCTION.
RX   PubMed=23184984; DOI=10.1073/pnas.1208248109;
RA   Rajagopalan S., Long E.O.;
RT   "Cellular senescence induced by CD158d reprograms natural killer cells to
RT   promote vascular remodeling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:20596-20601(2012).
RN   [15]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=29262349; DOI=10.1016/j.immuni.2017.11.018;
RA   Fu B., Zhou Y., Ni X., Tong X., Xu X., Dong Z., Sun R., Tian Z., Wei H.;
RT   "Natural Killer Cells Promote Fetal Development through the Secretion of
RT   Growth-Promoting Factors.";
RL   Immunity 47:1100-1113(2017).
CC   -!- FUNCTION: Receptor for non-classical major histocompatibility class Ib
CC       HLA-G molecules. Recognizes HLA-G in complex with B2M/beta-2
CC       microglobulin and a nonamer self-peptide (peptide-bound HLA-G-B2M). In
CC       decidual NK cells, binds peptide-bound HLA-G-B2M complex and triggers
CC       NK cell senescence-associated secretory phenotype as a molecular switch
CC       to promote vascular remodeling and fetal growth in early pregnancy
CC       (PubMed:16366734, PubMed:23184984, PubMed:29262349). May play a role in
CC       balancing tolerance and antiviral-immunity at maternal-fetal interface
CC       by keeping in check the effector functions of NK, CD8+ T cells and B
CC       cells (PubMed:10190900, PubMed:16366734). Upon interaction with
CC       peptide-bound HLA-G-B2M, initiates signaling from the endosomal
CC       compartment leading to downstream activation of PRKDC-XRCC5 and AKT1,
CC       and ultimately triggering NF-kappa-B-dependent pro-inflammatory
CC       response (PubMed:20179272). {ECO:0000269|PubMed:10190900,
CC       ECO:0000269|PubMed:16366734, ECO:0000269|PubMed:20179272,
CC       ECO:0000269|PubMed:23184984, ECO:0000269|PubMed:29262349}.
CC   -!- SUBUNIT: Interacts with peptide-bound HLA-G-B2M heterotrimeric complex
CC       (PubMed:10190900, PubMed:16366734). Interacts with ARRB2
CC       (PubMed:18604210). {ECO:0000269|PubMed:10190900,
CC       ECO:0000269|PubMed:16366734, ECO:0000269|PubMed:18604210}.
CC   -!- INTERACTION:
CC       Q99706; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-10294579, EBI-953896;
CC       Q99706; P08637: FCGR3A; NbExp=2; IntAct=EBI-10294579, EBI-2833956;
CC       Q99706; Q5TD97: FHL5; NbExp=3; IntAct=EBI-10294579, EBI-750641;
CC       Q99706; Q0VD86: INCA1; NbExp=3; IntAct=EBI-10294579, EBI-6509505;
CC       Q99706; Q93062: RBPMS; NbExp=3; IntAct=EBI-10294579, EBI-740322;
CC       Q99706; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-10294579, EBI-6268651;
CC       Q99706; Q15654: TRIP6; NbExp=3; IntAct=EBI-10294579, EBI-742327;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Early endosome membrane {ECO:0000269|PubMed:16366734}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q99706-1; Sequence=Displayed;
CC       Name=2; Synonyms=AST;
CC         IsoId=Q99706-2; Sequence=VSP_002609;
CC       Name=3; Synonyms=AS;
CC         IsoId=Q99706-3; Sequence=VSP_002610;
CC       Name=4; Synonyms=ASD1;
CC         IsoId=Q99706-4; Sequence=VSP_002609, VSP_002610;
CC       Name=5; Synonyms=ASD2;
CC         IsoId=Q99706-5; Sequence=VSP_002609, VSP_002610, VSP_002611;
CC       Name=6;
CC         IsoId=Q99706-6; Sequence=VSP_002608, VSP_002609, VSP_002610;
CC   -!- TISSUE SPECIFICITY: Expressed in decidual NK cells and innate lymphoid
CC       cell type I (ILC1) (PubMed:29262349). Expressed in a subset of
CC       peripheral NK cells (PubMed:19304799). {ECO:0000269|PubMed:19304799,
CC       ECO:0000269|PubMed:29262349}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR   EMBL; U71199; AAB49756.1; -; mRNA.
DR   EMBL; AF034771; AAB95164.1; -; mRNA.
DR   EMBL; AF034772; AAB95165.1; -; mRNA.
DR   EMBL; AF034773; AAB95166.1; -; mRNA.
DR   EMBL; U73394; AAC51146.1; -; mRNA.
DR   EMBL; AF003123; AAB61926.1; -; Genomic_DNA.
DR   EMBL; AF003116; AAB61926.1; JOINED; Genomic_DNA.
DR   EMBL; AF003117; AAB61926.1; JOINED; Genomic_DNA.
DR   EMBL; AF003118; AAB61926.1; JOINED; Genomic_DNA.
DR   EMBL; AF003119; AAB61926.1; JOINED; Genomic_DNA.
DR   EMBL; AF003121; AAB61926.1; JOINED; Genomic_DNA.
DR   EMBL; AF003122; AAB61926.1; JOINED; Genomic_DNA.
DR   EMBL; AF003120; AAB61926.1; JOINED; Genomic_DNA.
DR   EMBL; AF002979; AAB71387.1; -; mRNA.
DR   EMBL; AF002980; AAB71388.1; -; mRNA.
DR   EMBL; AF002981; AAB71389.1; -; mRNA.
DR   EMBL; AF002982; AAB71390.1; -; mRNA.
DR   EMBL; EU194342; ABW73961.1; -; mRNA.
DR   EMBL; X97229; CAA65868.1; -; mRNA.
DR   EMBL; X99479; CAA67842.1; -; mRNA.
DR   EMBL; X99480; CAA67843.1; -; mRNA.
DR   EMBL; X99481; CAA67844.1; -; mRNA.
DR   EMBL; AF110035; AAD24763.1; -; Genomic_DNA.
DR   EMBL; AF110032; AAD24763.1; JOINED; Genomic_DNA.
DR   EMBL; AF110033; AAD24763.1; JOINED; Genomic_DNA.
DR   EMBL; AF110034; AAD24763.1; JOINED; Genomic_DNA.
DR   EMBL; AC011501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL133414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS42619.1; -. [Q99706-3]
DR   RefSeq; NP_002246.5; NM_002255.5.
DR   PDB; 3WYR; X-ray; 2.80 A; A/B=24-218.
DR   PDBsum; 3WYR; -.
DR   AlphaFoldDB; Q99706; -.
DR   SMR; Q99706; -.
DR   BioGRID; 110006; 94.
DR   IntAct; Q99706; 91.
DR   MINT; Q99706; -.
DR   STRING; 9606.ENSP00000339634; -.
DR   GlyCosmos; Q99706; 2 sites, No reported glycans.
DR   GlyGen; Q99706; 2 sites.
DR   iPTMnet; Q99706; -.
DR   PhosphoSitePlus; Q99706; -.
DR   BioMuta; KIR2DL4; -.
DR   DMDM; 325511396; -.
DR   MassIVE; Q99706; -.
DR   PaxDb; 9606-ENSP00000339634; -.
DR   PeptideAtlas; Q99706; -.
DR   ProteomicsDB; 78417; -. [Q99706-1]
DR   ProteomicsDB; 78418; -. [Q99706-2]
DR   ProteomicsDB; 78419; -. [Q99706-3]
DR   ProteomicsDB; 78420; -. [Q99706-4]
DR   ProteomicsDB; 78421; -. [Q99706-5]
DR   Antibodypedia; 52730; 467 antibodies from 25 providers.
DR   DNASU; 3805; -.
DR   Ensembl; ENST00000345540.10; ENSP00000339634.5; ENSG00000189013.16. [Q99706-3]
DR   Ensembl; ENST00000357494.8; ENSP00000350088.4; ENSG00000189013.16. [Q99706-4]
DR   Ensembl; ENST00000396293.5; ENSP00000379588.1; ENSG00000189013.16. [Q99706-6]
DR   Ensembl; ENST00000611022.4; ENSP00000484469.1; ENSG00000274232.4. [Q99706-3]
DR   Ensembl; ENST00000612573.1; ENSP00000482206.1; ENSG00000275456.1.
DR   Ensembl; ENST00000612660.4; ENSP00000479179.1; ENSG00000275317.4.
DR   Ensembl; ENST00000613053.1; ENSP00000484389.1; ENSG00000277362.1.
DR   Ensembl; ENST00000614653.1; ENSP00000478362.1; ENSG00000277750.1.
DR   Ensembl; ENST00000614680.4; ENSP00000477984.1; ENSG00000273575.4. [Q99706-3]
DR   Ensembl; ENST00000615232.4; ENSP00000479874.1; ENSG00000274232.4. [Q99706-6]
DR   Ensembl; ENST00000615243.4; ENSP00000482454.1; ENSG00000274232.4. [Q99706-4]
DR   Ensembl; ENST00000615970.1; ENSP00000477887.1; ENSG00000278271.1.
DR   Ensembl; ENST00000616354.4; ENSP00000483782.1; ENSG00000278430.4.
DR   Ensembl; ENST00000616384.4; ENSP00000479347.1; ENSG00000276044.4. [Q99706-3]
DR   Ensembl; ENST00000618297.1; ENSP00000477886.1; ENSG00000278074.1.
DR   Ensembl; ENST00000618358.1; ENSP00000483101.1; ENSG00000274609.1.
DR   Ensembl; ENST00000618567.1; ENSP00000482383.1; ENSG00000276779.1.
DR   Ensembl; ENST00000619637.4; ENSP00000478491.1; ENSG00000274955.4.
DR   Ensembl; ENST00000619848.1; ENSP00000480801.1; ENSG00000277964.1.
DR   Ensembl; ENST00000620484.4; ENSP00000477601.1; ENSG00000275317.4.
DR   Ensembl; ENST00000620486.4; ENSP00000482452.1; ENSG00000278430.4.
DR   Ensembl; ENST00000621182.3; ENSP00000479175.1; ENSG00000275699.4. [Q99706-3]
DR   Ensembl; ENST00000638231.1; ENSP00000492368.1; ENSG00000284460.1. [Q99706-6]
DR   Ensembl; ENST00000638248.1; ENSP00000491734.1; ENSG00000284365.1. [Q99706-4]
DR   Ensembl; ENST00000638297.1; ENSP00000492029.1; ENSG00000284365.1. [Q99706-6]
DR   Ensembl; ENST00000638563.2; ENSP00000491532.1; ENSG00000284013.2. [Q99706-4]
DR   Ensembl; ENST00000638897.1; ENSP00000492653.1; ENSG00000283961.1. [Q99706-4]
DR   Ensembl; ENST00000639460.1; ENSP00000491648.1; ENSG00000283869.1. [Q99706-6]
DR   Ensembl; ENST00000639533.1; ENSP00000491289.1; ENSG00000283961.1. [Q99706-6]
DR   Ensembl; ENST00000639577.2; ENSP00000492722.1; ENSG00000284013.2. [Q99706-3]
DR   Ensembl; ENST00000639740.1; ENSP00000492606.1; ENSG00000284509.1. [Q99706-6]
DR   Ensembl; ENST00000639866.1; ENSP00000491202.1; ENSG00000283961.1. [Q99706-3]
DR   Ensembl; ENST00000640163.2; ENSP00000491890.2; ENSG00000284013.2. [Q99706-6]
DR   Ensembl; ENST00000640814.1; ENSP00000491623.1; ENSG00000284365.1. [Q99706-3]
DR   GeneID; 3805; -.
DR   KEGG; hsa:3805; -.
DR   MANE-Select; ENST00000345540.10; ENSP00000339634.5; NM_001080770.2; NP_001074239.1. [Q99706-3]
DR   UCSC; uc002qhg.5; human. [Q99706-1]
DR   AGR; HGNC:6332; -.
DR   CTD; 3805; -.
DR   DisGeNET; 3805; -.
DR   GeneCards; KIR2DL4; -.
DR   HGNC; HGNC:6332; KIR2DL4.
DR   HPA; ENSG00000189013; Tissue enriched (lymphoid).
DR   MalaCards; KIR2DL4; -.
DR   MIM; 604945; gene.
DR   neXtProt; NX_Q99706; -.
DR   OpenTargets; ENSG00000189013; -.
DR   PharmGKB; PA30117; -.
DR   VEuPathDB; HostDB:ENSG00000189013; -.
DR   eggNOG; ENOG502RU21; Eukaryota.
DR   GeneTree; ENSGT01100000263478; -.
DR   HOGENOM; CLU_021100_2_1_1; -.
DR   InParanoid; Q99706; -.
DR   OrthoDB; 9613897at2759; -.
DR   TreeFam; TF352669; -.
DR   PathwayCommons; Q99706; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   SignaLink; Q99706; -.
DR   SIGNOR; Q99706; -.
DR   BioGRID-ORCS; 3805; 7 hits in 1133 CRISPR screens.
DR   EvolutionaryTrace; Q99706; -.
DR   GeneWiki; KIR2DL4; -.
DR   GenomeRNAi; 3805; -.
DR   Pharos; Q99706; Tbio.
DR   PRO; PR:Q99706; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q99706; protein.
DR   Bgee; ENSG00000189013; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 79 other cell types or tissues.
DR   ExpressionAtlas; Q99706; baseline and differential.
DR   GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032394; F:MHC class Ib receptor activity; IDA:UniProtKB.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR   GO; GO:0002764; P:immune response-regulating signaling pathway; IBA:GO_Central.
DR   GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
DR   GO; GO:2000774; P:positive regulation of cellular senescence; IDA:UniProtKB.
DR   GO; GO:0002729; P:positive regulation of natural killer cell cytokine production; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   FunFam; 2.60.40.10:FF:000033; Killer cell immunoglobulin-like receptor; 1.
DR   FunFam; 2.60.40.10:FF:000049; Leukocyte immunoglobulin-like receptor subfamily B member 1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR050412; Ig-like_Receptors_ImmuneReg.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013151; Immunoglobulin_dom.
DR   PANTHER; PTHR11738:SF113; KILLER CELL IMMUNOGLOBULIN-LIKE RECEPTOR 2DL4; 1.
DR   PANTHER; PTHR11738; MHC CLASS I NK CELL RECEPTOR; 1.
DR   Pfam; PF00047; ig; 2.
DR   SMART; SM00409; IG; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW   Endosome; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Proteomics identification; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..377
FT                   /note="Killer cell immunoglobulin-like receptor 2DL4"
FT                   /id="PRO_0000015081"
FT   TOPO_DOM        22..242
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        264..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          44..104
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          139..202
FT                   /note="Ig-like C2-type 2"
FT   REGION          338..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        146..195
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         27..121
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|Ref.6"
FT                   /id="VSP_002608"
FT   VAR_SEQ         219..235
FT                   /note="Missing (in isoform 2, isoform 4, isoform 5 and
FT                   isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:9059894,
FT                   ECO:0000303|PubMed:9234477, ECO:0000303|Ref.6"
FT                   /id="VSP_002609"
FT   VAR_SEQ         236..270
FT                   /note="Missing (in isoform 3, isoform 4, isoform 5 and
FT                   isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:9234477, ECO:0000303|Ref.6"
FT                   /id="VSP_002610"
FT   VAR_SEQ         271..288
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:9234477"
FT                   /id="VSP_002611"
FT   VARIANT         53
FT                   /note="Y -> C (in dbSNP:rs618835)"
FT                   /evidence="ECO:0000269|PubMed:18082267,
FT                   ECO:0000269|PubMed:9430220, ECO:0000269|Ref.7"
FT                   /id="VAR_010307"
FT   VARIANT         87
FT                   /note="V -> L (in dbSNP:rs773420112)"
FT                   /evidence="ECO:0000269|PubMed:8946682,
FT                   ECO:0000269|PubMed:9059894, ECO:0000269|PubMed:9234477"
FT                   /id="VAR_010308"
FT   VARIANT         138
FT                   /note="A -> T (in dbSNP:rs1051454)"
FT                   /evidence="ECO:0000269|PubMed:8946682,
FT                   ECO:0000269|PubMed:9059894, ECO:0000269|PubMed:9234477,
FT                   ECO:0000269|PubMed:9430220, ECO:0000269|Ref.6"
FT                   /id="VAR_010309"
FT   VARIANT         209
FT                   /note="P -> A (in dbSNP:rs1051456)"
FT                   /evidence="ECO:0000269|PubMed:8946682,
FT                   ECO:0000269|PubMed:9059894, ECO:0000269|PubMed:9234477,
FT                   ECO:0000269|PubMed:9430220, ECO:0000269|Ref.6"
FT                   /id="VAR_010310"
FT   VARIANT         271..273
FT                   /note="DAA -> MLL (in allele KIR2DL4*0501)"
FT                   /id="VAR_064649"
FT   VARIANT         271
FT                   /note="D -> N"
FT                   /evidence="ECO:0000269|PubMed:9234477,
FT                   ECO:0000269|PubMed:9430220, ECO:0000269|Ref.6,
FT                   ECO:0000269|Ref.7"
FT                   /id="VAR_010311"
FT   VARIANT         274..377
FT                   /note="Missing (in allele KIR2DL4*0501)"
FT                   /id="VAR_065101"
FT   VARIANT         371
FT                   /note="N -> H (in dbSNP:rs1185997484)"
FT                   /evidence="ECO:0000269|PubMed:8946682,
FT                   ECO:0000269|PubMed:9059894, ECO:0000269|PubMed:9234477,
FT                   ECO:0000269|PubMed:9430220"
FT                   /id="VAR_010312"
FT   MUTAGEN         246..247
FT                   /note="RY->GT: Does not affect targeting to the endosomal
FT                   compartment."
FT                   /evidence="ECO:0000269|PubMed:16366734"
FT   CONFLICT        47
FT                   /note="V -> A (in Ref. 5; ABW73961)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="T -> P (in Ref. 7; AAD24763)"
FT                   /evidence="ECO:0000305"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          39..42
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          47..52
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          54..67
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   HELIX           71..73
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          76..84
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          93..100
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          115..120
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          127..132
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          141..150
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          153..159
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          162..169
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   TURN            174..176
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          177..186
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          191..198
FT                   /evidence="ECO:0007829|PDB:3WYR"
FT   STRAND          213..217
FT                   /evidence="ECO:0007829|PDB:3WYR"
SQ   SEQUENCE   377 AA;  41487 MW;  888B3297332D6C59 CRC64;
     MSMSPTVIIL ACLGFFLDQS VWAHVGGQDK PFCSAWPSAV VPQGGHVTLR CHYRRGFNIF
     TLYKKDGVPV PELYNRIFWN SFLISPVTPA HAGTYRCRGF HPHSPTEWSA PSNPLVIMVT
     GLYEKPSLTA RPGPTVRAGE NVTLSCSSQS SFDIYHLSRE GEAHELRLPA VPSINGTFQA
     DFPLGPATHG ETYRCFGSFH GSPYEWSDPS DPLPVSVTGN PSSSWPSPTE PSFKTGIARH
     LHAVIRYSVA IILFTILPFF LLHRWCSKKK DAAVMNQEPA GHRTVNREDS DEQDPQEVTY
     AQLDHCIFTQ RKITGPSQRS KRPSTDTSVC IELPNAEPRA LSPAHEHHSQ ALMGSSRETT
     ALSQTQLASS NVPAAGI
//