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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //