KI2L4_HUMAN
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 03-AUG-2022, entry version 195.
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:23184984, PubMed:29262349, PubMed:16366734). 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; 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; 7.
DR MINT; Q99706; -.
DR STRING; 9606.ENSP00000339634; -.
DR GlyGen; Q99706; 2 sites.
DR iPTMnet; Q99706; -.
DR PhosphoSitePlus; Q99706; -.
DR BioMuta; KIR2DL4; -.
DR DMDM; 325511396; -.
DR MassIVE; Q99706; -.
DR PeptideAtlas; Q99706; -.
DR PRIDE; 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; 426 antibodies from 25 providers.
DR DNASU; 3805; -.
DR Ensembl; ENST00000345540.9; ENSP00000339634.5; ENSG00000189013.15. [Q99706-3]
DR Ensembl; ENST00000357494.8; ENSP00000350088.4; ENSG00000189013.15. [Q99706-4]
DR Ensembl; ENST00000396293.5; ENSP00000379588.1; ENSG00000189013.15. [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 CTD; 3805; -.
DR DisGeNET; 3805; -.
DR GeneCards; KIR2DL4; -.
DR HGNC; HGNC:6332; KIR2DL4.
DR HPA; ENSG00000189013; Tissue enriched (lymphoid).
DR MIM; 604945; gene.
DR neXtProt; NX_Q99706; -.
DR OpenTargets; ENSG00000189013; -.
DR PharmGKB; PA30117; -.
DR VEuPathDB; HostDB:ENSG00000189013; -.
DR eggNOG; ENOG502RU21; Eukaryota.
DR GeneTree; ENSGT01000000214458; -.
DR HOGENOM; CLU_021100_2_1_1; -.
DR InParanoid; Q99706; -.
DR OrthoDB; 1055520at2759; -.
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 1057 CRISPR screens.
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 spleen and 79 other tissues.
DR ExpressionAtlas; Q99706; baseline and differential.
DR Genevisible; Q99706; HS.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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: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 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; Disulfide bond;
KW Endosome; Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; 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 353..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
