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KI3L2_HUMAN
ID   KI3L2_HUMAN             Reviewed;         455 AA.
AC   P43630; Q13238; Q14947; Q14948; Q92684; Q95366; Q95367; Q95368;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 198.
DE   RecName: Full=Killer cell immunoglobulin-like receptor 3DL2 {ECO:0000305};
DE   AltName: Full=CD158 antigen-like family member K;
DE   AltName: Full=Natural killer-associated transcript 4;
DE            Short=NKAT-4;
DE   AltName: Full=p70 natural killer cell receptor clone CL-5;
DE            Short=p70 NK receptor CL-5;
DE   AltName: CD_antigen=CD158k;
DE   Flags: Precursor;
GN   Name=KIR3DL2 {ECO:0000303|PubMed:24018270, ECO:0000312|HGNC:HGNC:6339};
GN   Synonyms=CD158K, NKAT4;
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).
RC   TISSUE=Peripheral blood lymphocyte;
RX   PubMed=8777725; DOI=10.1016/1074-7613(95)90069-1;
RA   Wagtmann N., Rajagopalan S., Winter C.C., Peruzzi M., Long E.O.;
RT   "Killer cell inhibitory receptors specific for HLA-C and HLA-B identified
RT   by direct binding and by functional transfer.";
RL   Immunity 3:801-809(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS ALA-40;
RP   VAL-113; ASP-158 AND HIS-166.
RC   TISSUE=Lymphoid tissue;
RX   PubMed=8760804; DOI=10.1084/jem.184.2.505;
RA   Pende D., Biassoni R., Cantoni C., Verdiani S., Falco M., di Donato C.,
RA   Accame L., Bottino C., Moretta A., Moretta L.;
RT   "The natural killer cell receptor specific for HLA-A allotypes: a novel
RT   member of the p58/p70 family of inhibitory receptors that is characterized
RT   by three immunoglobulin-like domains and is expressed as a 140-kD
RT   disulphide-linked dimer.";
RL   J. Exp. Med. 184:505-518(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8662091; DOI=10.1007/bf02602590;
RA   Doehring C., Samaridis J., Colonna M.;
RT   "Alternatively spliced forms of human killer inhibitory receptors.";
RL   Immunogenetics 44:227-230(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-158.
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   [6]
RP   FUNCTION, SUBUNIT, AND INTERACTION WITH HLA-F.
RX   PubMed=24018270; DOI=10.4049/jimmunol.1300081;
RA   Goodridge J.P., Burian A., Lee N., Geraghty D.E.;
RT   "HLA-F and MHC class I open conformers are ligands for NK cell Ig-like
RT   receptors.";
RL   J. Immunol. 191:3553-3562(2013).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=26928464; DOI=10.1038/nm.4052;
RA   Song S., Miranda C.J., Braun L., Meyer K., Frakes A.E., Ferraiuolo L.,
RA   Likhite S., Bevan A.K., Foust K.D., McConnell M.J., Walker C.M.,
RA   Kaspar B.K.;
RT   "Major histocompatibility complex class I molecules protect motor neurons
RT   from astrocyte-induced toxicity in amyotrophic lateral sclerosis.";
RL   Nat. Med. 22:397-403(2016).
RN   [8]
RP   FUNCTION, SUBUNIT, AND INTERACTION WITH HLA-F.
RX   PubMed=28636952; DOI=10.1016/j.immuni.2017.06.002;
RA   Dulberger C.L., McMurtrey C.P., Holzemer A., Neu K.E., Liu V.,
RA   Steinbach A.M., Garcia-Beltran W.F., Sulak M., Jabri B., Lynch V.J.,
RA   Altfeld M., Hildebrand W.H., Adams E.J.;
RT   "Human Leukocyte Antigen F Presents Peptides and Regulates Immunity through
RT   Interactions with NK Cell Receptors.";
RL   Immunity 46:1018-1029(2017).
RN   [9]
RP   VARIANTS ALA-40; VAL-113; ASP-158; HIS-166; PRO-228 AND THR-252.
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).
CC   -!- FUNCTION: Receptor on natural killer (NK) cells and T cells for MHC
CC       class I molecules (PubMed:24018270, PubMed:28636952). Upon binding of
CC       peptide-free HLA-F open conformer, negatively regulates NK and T cell
CC       effector functions (PubMed:24018270). Acts as a receptor on astrocytes
CC       for HLA-F. Through interaction with HLA-F, may protect motor neurons
CC       from astrocyte-induced toxicity (PubMed:26928464).
CC       {ECO:0000269|PubMed:24018270, ECO:0000269|PubMed:26928464,
CC       ECO:0000269|PubMed:28636952}.
CC   -!- SUBUNIT: Interacts with peptide-free HLA-F open conformer.
CC       {ECO:0000269|PubMed:24018270, ECO:0000269|PubMed:28636952}.
CC   -!- INTERACTION:
CC       P43630; P30511: HLA-F; NbExp=6; IntAct=EBI-6165894, EBI-2811134;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P43630-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P43630-2; Sequence=VSP_047374;
CC   -!- TISSUE SPECIFICITY: Expressed in astrocytes.
CC       {ECO:0000269|PubMed:26928464}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR   EMBL; L41270; AAA69871.1; -; mRNA.
DR   EMBL; U30272; AAB52520.1; -; mRNA.
DR   EMBL; X93595; CAA63791.1; -; mRNA.
DR   EMBL; X93596; CAA63792.1; -; mRNA.
DR   EMBL; X94373; CAA64150.1; -; mRNA.
DR   EMBL; X94374; CAA64151.1; -; mRNA.
DR   EMBL; L76665; AAB36593.1; -; mRNA.
DR   EMBL; L76666; AAB36594.1; -; mRNA.
DR   EMBL; AY789067; AAX23112.1; -; mRNA.
DR   CCDS; CCDS12906.1; -. [P43630-1]
DR   CCDS; CCDS58677.1; -. [P43630-2]
DR   RefSeq; NP_001229796.1; NM_001242867.1. [P43630-2]
DR   RefSeq; NP_006728.2; NM_006737.3. [P43630-1]
DR   AlphaFoldDB; P43630; -.
DR   SMR; P43630; -.
DR   BioGRID; 110013; 37.
DR   ELM; P43630; -.
DR   IntAct; P43630; 24.
DR   STRING; 9606.ENSP00000325525; -.
DR   ChEMBL; CHEMBL4630895; -.
DR   GlyGen; P43630; 4 sites.
DR   iPTMnet; P43630; -.
DR   PhosphoSitePlus; P43630; -.
DR   SwissPalm; P43630; -.
DR   BioMuta; KIR3DL2; -.
DR   DMDM; 1171729; -.
DR   MassIVE; P43630; -.
DR   PaxDb; P43630; -.
DR   PeptideAtlas; P43630; -.
DR   PRIDE; P43630; -.
DR   ProteomicsDB; 55644; -. [P43630-1]
DR   ABCD; P43630; 12 sequenced antibodies.
DR   Antibodypedia; 52684; 131 antibodies from 19 providers.
DR   DNASU; 3812; -.
DR   Ensembl; ENST00000270442.5; ENSP00000270442.5; ENSG00000240403.5. [P43630-2]
DR   Ensembl; ENST00000326321.7; ENSP00000325525.3; ENSG00000240403.5. [P43630-1]
DR   Ensembl; ENST00000611608.4; ENSP00000479903.1; ENSG00000278809.4. [P43630-1]
DR   Ensembl; ENST00000611628.4; ENSP00000481662.1; ENSG00000278474.4.
DR   Ensembl; ENST00000611859.1; ENSP00000480578.1; ENSG00000277181.4. [P43630-2]
DR   Ensembl; ENST00000612138.1; ENSP00000482589.1; ENSG00000274722.4. [P43630-2]
DR   Ensembl; ENST00000613610.4; ENSP00000482301.1; ENSG00000278442.4.
DR   Ensembl; ENST00000613612.4; ENSP00000482565.1; ENSG00000275566.4.
DR   Ensembl; ENST00000614753.4; ENSP00000479299.1; ENSG00000276357.4.
DR   Ensembl; ENST00000617354.4; ENSP00000482110.1; ENSG00000274722.4. [P43630-1]
DR   Ensembl; ENST00000617481.1; ENSP00000481306.1; ENSG00000275083.4. [P43630-2]
DR   Ensembl; ENST00000617666.4; ENSP00000481209.1; ENSG00000278361.4.
DR   Ensembl; ENST00000617957.4; ENSP00000481579.1; ENSG00000275083.4. [P43630-1]
DR   Ensembl; ENST00000618273.1; ENSP00000481871.1; ENSG00000276739.4. [P43630-2]
DR   Ensembl; ENST00000619683.4; ENSP00000478251.1; ENSG00000275626.4.
DR   Ensembl; ENST00000620817.4; ENSP00000479772.1; ENSG00000276739.4. [P43630-1]
DR   Ensembl; ENST00000621155.4; ENSP00000477519.1; ENSG00000275416.4.
DR   Ensembl; ENST00000622024.4; ENSP00000479425.1; ENSG00000276004.4.
DR   Ensembl; ENST00000622453.4; ENSP00000477516.1; ENSG00000277181.4. [P43630-1]
DR   Ensembl; ENST00000622579.1; ENSP00000482655.1; ENSG00000278809.4. [P43630-2]
DR   Ensembl; ENST00000638330.2; ENSP00000492261.2; ENSG00000284381.2. [P43630-1]
DR   Ensembl; ENST00000638726.1; ENSP00000492117.1; ENSG00000283951.1. [P43630-2]
DR   Ensembl; ENST00000638805.1; ENSP00000492880.1; ENSG00000283975.1. [P43630-2]
DR   Ensembl; ENST00000638891.1; ENSP00000491303.1; ENSG00000284063.1. [P43630-1]
DR   Ensembl; ENST00000638970.1; ENSP00000491183.1; ENSG00000283975.1. [P43630-1]
DR   Ensembl; ENST00000639252.2; ENSP00000491248.2; ENSG00000284381.2. [P43630-2]
DR   Ensembl; ENST00000639313.1; ENSP00000491707.1; ENSG00000284063.1. [P43630-2]
DR   Ensembl; ENST00000640782.1; ENSP00000491436.1; ENSG00000283951.1. [P43630-1]
DR   GeneID; 3812; -.
DR   KEGG; hsa:3812; -.
DR   MANE-Select; ENST00000326321.7; ENSP00000325525.3; NM_006737.4; NP_006728.2.
DR   UCSC; uc002qho.5; human. [P43630-1]
DR   CTD; 3812; -.
DR   DisGeNET; 3812; -.
DR   GeneCards; KIR3DL2; -.
DR   HGNC; HGNC:6339; KIR3DL2.
DR   HPA; ENSG00000240403; Tissue enhanced (lymphoid).
DR   MIM; 604947; gene.
DR   neXtProt; NX_P43630; -.
DR   OpenTargets; ENSG00000240403; -.
DR   PharmGKB; PA30124; -.
DR   VEuPathDB; HostDB:ENSG00000240403; -.
DR   eggNOG; ENOG502RU21; Eukaryota.
DR   GeneTree; ENSGT01000000214458; -.
DR   HOGENOM; CLU_021100_2_1_1; -.
DR   InParanoid; P43630; -.
DR   OMA; GEAREYR; -.
DR   PhylomeDB; P43630; -.
DR   TreeFam; TF352669; -.
DR   PathwayCommons; P43630; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   SignaLink; P43630; -.
DR   BioGRID-ORCS; 3812; 6 hits in 1054 CRISPR screens.
DR   GeneWiki; KIR3DL2; -.
DR   GenomeRNAi; 3812; -.
DR   Pharos; P43630; Tbio.
DR   PRO; PR:P43630; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P43630; protein.
DR   Bgee; ENSG00000240403; Expressed in granulocyte and 36 other tissues.
DR   ExpressionAtlas; P43630; baseline and differential.
DR   Genevisible; P43630; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0023029; F:MHC class Ib protein binding; IDA:UniProtKB.
DR   GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR   GO; GO:1901215; P:negative regulation of neuron death; IMP:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 3.
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; 3.
DR   SMART; SM00409; IG; 3.
DR   SUPFAM; SSF48726; SSF48726; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..455
FT                   /note="Killer cell immunoglobulin-like receptor 3DL2"
FT                   /id="PRO_0000015090"
FT   TOPO_DOM        22..340
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        341..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        361..455
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          42..102
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          137..202
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          237..300
FT                   /note="Ig-like C2-type 3"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..95
FT                   /evidence="ECO:0000305"
FT   DISULFID        144..195
FT                   /evidence="ECO:0000250|UniProtKB:Q8NHL6"
FT   DISULFID        244..293
FT                   /evidence="ECO:0000250|UniProtKB:Q8NHL6"
FT   VAR_SEQ         318..334
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8760804"
FT                   /id="VSP_047374"
FT   VARIANT         40
FT                   /note="P -> A"
FT                   /evidence="ECO:0000269|PubMed:8760804,
FT                   ECO:0000269|PubMed:9430221"
FT                   /id="VAR_010325"
FT   VARIANT         113
FT                   /note="L -> V (in dbSNP:rs3188286)"
FT                   /evidence="ECO:0000269|PubMed:8760804,
FT                   ECO:0000269|PubMed:9430221"
FT                   /id="VAR_010326"
FT   VARIANT         158
FT                   /note="E -> D (in dbSNP:rs633870)"
FT                   /evidence="ECO:0000269|PubMed:8760804,
FT                   ECO:0000269|PubMed:9430221, ECO:0000269|Ref.5"
FT                   /id="VAR_010327"
FT   VARIANT         166
FT                   /note="R -> H (in dbSNP:rs1048271)"
FT                   /evidence="ECO:0000269|PubMed:8760804,
FT                   ECO:0000269|PubMed:9430221"
FT                   /id="VAR_010328"
FT   VARIANT         228
FT                   /note="A -> P (in dbSNP:rs1377032475)"
FT                   /evidence="ECO:0000269|PubMed:9430221"
FT                   /id="VAR_010329"
FT   VARIANT         252
FT                   /note="I -> T"
FT                   /evidence="ECO:0000269|PubMed:9430221"
FT                   /id="VAR_010330"
FT   VARIANT         397
FT                   /note="T -> M (in dbSNP:rs3745902)"
FT                   /id="VAR_049992"
FT   VARIANT         439
FT                   /note="K -> Q (in dbSNP:rs3745903)"
FT                   /id="VAR_049993"
SQ   SEQUENCE   455 AA;  50230 MW;  DB4BA6BB6B3C2945 CRC64;
     MSLTVVSMAC VGFFLLQGAW PLMGGQDKPF LSARPSTVVP RGGHVALQCH YRRGFNNFML
     YKEDRSHVPI FHGRIFQESF IMGPVTPAHA GTYRCRGSRP HSLTGWSAPS NPLVIMVTGN
     HRKPSLLAHP GPLLKSGETV ILQCWSDVMF EHFFLHREGI SEDPSRLVGQ IHDGVSKANF
     SIGPLMPVLA GTYRCYGSVP HSPYQLSAPS DPLDIVITGL YEKPSLSAQP GPTVQAGENV
     TLSCSSWSSY DIYHLSREGE AHERRLRAVP KVNRTFQADF PLGPATHGGT YRCFGSFRAL
     PCVWSNSSDP LLVSVTGNPS SSWPSPTEPS SKSGICRHLH VLIGTSVVIF LFILLLFFLL
     YRWCSNKKNA AVMDQEPAGD RTVNRQDSDE QDPQEVTYAQ LDHCVFIQRK ISRPSQRPKT
     PLTDTSVYTE LPNAEPRSKV VSCPRAPQSG LEGVF
 
 
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