KI3L1_HUMAN
ID KI3L1_HUMAN Reviewed; 444 AA.
AC P43629; O43473; Q14946; Q16541;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Killer cell immunoglobulin-like receptor 3DL1 {ECO:0000305};
DE AltName: Full=CD158 antigen-like family member E;
DE AltName: Full=HLA-BW4-specific inhibitory NK cell receptor;
DE AltName: Full=Natural killer-associated transcript 3;
DE Short=NKAT-3;
DE AltName: Full=p70 natural killer cell receptor clones CL-2/CL-11;
DE Short=p70 NK receptor CL-2/CL-11;
DE AltName: CD_antigen=CD158e;
DE Flags: Precursor;
GN Name=KIR3DL1 {ECO:0000312|HGNC:HGNC:6338}; Synonyms=CD158E, NKAT3, NKB1;
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] (ISOFORM 1).
RC TISSUE=Peripheral blood lymphocyte;
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).
RC TISSUE=Blood;
RX PubMed=7650366;
RA D'Andrea A., Chang C., Franz-Bacon K., McClanahan T., Phillips J.H.,
RA Lanier L.L.;
RT "Molecular cloning of NKB1. A natural killer cell receptor for HLA-B
RT allotypes.";
RL J. Immunol. 155:2306-2310(1995).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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 [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-320 IN COMPLEX WITH
RP PEPTIDE-LOADED HLA-B, FUNCTION, GLYCOSYLATION AT ASN-92; ASN-179 AND
RP ASN-273, AND DISULFIDE BONDS.
RX PubMed=22020283; DOI=10.1038/nature10517;
RA Vivian J.P., Duncan R.C., Berry R., O'Connor G.M., Reid H.H., Beddoe T.,
RA Gras S., Saunders P.M., Olshina M.A., Widjaja J.M., Harpur C.M., Lin J.,
RA Maloveste S.M., Price D.A., Lafont B.A., McVicar D.W., Clements C.S.,
RA Brooks A.G., Rossjohn J.;
RT "Killer cell immunoglobulin-like receptor 3DL1-mediated recognition of
RT human leukocyte antigen B.";
RL Nature 479:401-405(2011).
CC -!- FUNCTION: Receptor on natural killer (NK) cells for HLA Bw4 allele.
CC Inhibits the activity of NK cells thus preventing cell lysis.
CC {ECO:0000269|PubMed:22020283}.
CC -!- INTERACTION:
CC P43629; O95393: BMP10; NbExp=3; IntAct=EBI-3910993, EBI-3922513;
CC P43629; P30511: HLA-F; NbExp=4; IntAct=EBI-3910993, EBI-2811134;
CC P43629; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-3910993, EBI-8640191;
CC P43629; C9JKN6: THSD7B; NbExp=3; IntAct=EBI-3910993, EBI-17192156;
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=P43629-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43629-2; Sequence=VSP_047633;
CC -!- DOMAIN: Ig-like C2-type domain 2 mediates specificity through
CC recognition of the Bw4 epitope. {ECO:0000269|PubMed:22020283}.
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; L41269; AAA69870.1; -; mRNA.
DR EMBL; U30273; AAB52521.1; -; mRNA.
DR EMBL; U30274; AAB52522.1; -; mRNA.
DR EMBL; X94262; CAA63938.1; -; mRNA.
DR EMBL; U31416; AAC23725.1; -; mRNA.
DR EMBL; AF022049; AAB95322.1; -; mRNA.
DR EMBL; L76664; AAB36592.1; -; mRNA.
DR EMBL; AC006293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS42621.1; -. [P43629-1]
DR PIR; G01924; G01924.
DR PIR; G01925; G01925.
DR RefSeq; NP_001309097.1; NM_001322168.1.
DR RefSeq; NP_037421.2; NM_013289.2. [P43629-1]
DR PDB; 3VH8; X-ray; 1.80 A; G/H=22-320.
DR PDB; 3WUW; X-ray; 2.00 A; G=28-313.
DR PDB; 5B38; X-ray; 2.30 A; G=22-320.
DR PDB; 5B39; X-ray; 2.50 A; G=22-320.
DR PDB; 5T6Z; X-ray; 2.00 A; G=22-320.
DR PDB; 5T70; X-ray; 2.10 A; G=22-320.
DR PDB; 6V3J; X-ray; 1.98 A; G=22-320.
DR PDB; 7K80; X-ray; 2.40 A; G/H=22-320.
DR PDB; 7K81; X-ray; 2.00 A; G=27-315.
DR PDBsum; 3VH8; -.
DR PDBsum; 3WUW; -.
DR PDBsum; 5B38; -.
DR PDBsum; 5B39; -.
DR PDBsum; 5T6Z; -.
DR PDBsum; 5T70; -.
DR PDBsum; 6V3J; -.
DR PDBsum; 7K80; -.
DR PDBsum; 7K81; -.
DR AlphaFoldDB; P43629; -.
DR SMR; P43629; -.
DR BioGRID; 110012; 11.
DR IntAct; P43629; 13.
DR STRING; 9606.ENSP00000375608; -.
DR GlyGen; P43629; 3 sites.
DR iPTMnet; P43629; -.
DR PhosphoSitePlus; P43629; -.
DR BioMuta; KIR3DL1; -.
DR DMDM; 1171728; -.
DR jPOST; P43629; -.
DR MassIVE; P43629; -.
DR PaxDb; P43629; -.
DR PeptideAtlas; P43629; -.
DR PRIDE; P43629; -.
DR ProteomicsDB; 55643; -. [P43629-1]
DR ProteomicsDB; 60254; -.
DR Antibodypedia; 34883; 558 antibodies from 33 providers.
DR DNASU; 3811; -.
DR Ensembl; ENST00000358178.4; ENSP00000350901.4; ENSG00000167633.18. [P43629-2]
DR Ensembl; ENST00000391728.8; ENSP00000375608.4; ENSG00000167633.18. [P43629-1]
DR Ensembl; ENST00000612668.4; ENSP00000484488.1; ENSG00000274036.5. [P43629-1]
DR Ensembl; ENST00000616188.4; ENSP00000484036.1; ENSG00000275288.6. [P43629-1]
DR Ensembl; ENST00000621353.4; ENSP00000484972.1; ENSG00000276423.6. [P43629-1]
DR Ensembl; ENST00000639353.2; ENSP00000492794.1; ENSG00000284342.2. [P43629-1]
DR Ensembl; ENST00000639813.1; ENSP00000492173.1; ENSG00000284426.1. [P43629-2]
DR Ensembl; ENST00000640111.2; ENSP00000491437.2; ENSG00000284342.2. [P43629-2]
DR Ensembl; ENST00000640788.1; ENSP00000491550.1; ENSG00000284426.1. [P43629-1]
DR GeneID; 3811; -.
DR KEGG; hsa:3811; -.
DR UCSC; uc010esf.4; human. [P43629-1]
DR CTD; 3811; -.
DR DisGeNET; 3811; -.
DR GeneCards; KIR3DL1; -.
DR HGNC; HGNC:6338; KIR3DL1.
DR HPA; ENSG00000167633; Tissue enhanced (lymphoid).
DR MalaCards; KIR3DL1; -.
DR MIM; 604946; gene.
DR neXtProt; NX_P43629; -.
DR OpenTargets; ENSG00000167633; -.
DR PharmGKB; PA30123; -.
DR VEuPathDB; HostDB:ENSG00000167633; -.
DR eggNOG; ENOG502RU21; Eukaryota.
DR GeneTree; ENSGT01000000214458; -.
DR InParanoid; P43629; -.
DR OMA; PMEERTV; -.
DR OrthoDB; 1055520at2759; -.
DR PhylomeDB; P43629; -.
DR TreeFam; TF352669; -.
DR PathwayCommons; P43629; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; P43629; -.
DR SIGNOR; P43629; -.
DR BioGRID-ORCS; 3811; 13 hits in 1066 CRISPR screens.
DR GeneWiki; KIR3DL1; -.
DR GenomeRNAi; 3811; -.
DR Pharos; P43629; Tbio.
DR PRO; PR:P43629; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P43629; protein.
DR Bgee; ENSG00000167633; Expressed in granulocyte and 34 other tissues.
DR ExpressionAtlas; P43629; baseline and differential.
DR Genevisible; P43629; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030109; F:HLA-B specific inhibitory MHC class I receptor activity; NAS:UniProtKB.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:UniProtKB.
DR DisProt; DP02552; -.
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 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..444
FT /note="Killer cell immunoglobulin-like receptor 3DL1"
FT /id="PRO_0000015087"
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..444
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 REGION 315..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22020283"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22020283"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22020283"
FT DISULFID 49..95
FT /evidence="ECO:0000269|PubMed:22020283"
FT DISULFID 144..195
FT /evidence="ECO:0000269|PubMed:22020283"
FT DISULFID 244..293
FT /evidence="ECO:0000269|PubMed:22020283"
FT VAR_SEQ 25..119
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8662091"
FT /id="VSP_047633"
FT VARIANT 2
FT /note="S -> L (in dbSNP:rs605219)"
FT /id="VAR_010319"
FT VARIANT 13
FT /note="L -> F (in dbSNP:rs1142881)"
FT /id="VAR_010320"
FT VARIANT 23
FT /note="M -> V (in dbSNP:rs1142882)"
FT /id="VAR_010321"
FT VARIANT 68
FT /note="I -> V (in dbSNP:rs643347)"
FT /id="VAR_010322"
FT VARIANT 75
FT /note="I -> L (in dbSNP:rs1049150)"
FT /id="VAR_010323"
FT VARIANT 203
FT /note="P -> S (in dbSNP:rs2273731)"
FT /id="VAR_049987"
FT VARIANT 220
FT /note="P -> L (in dbSNP:rs680891)"
FT /id="VAR_049988"
FT VARIANT 259
FT /note="G -> R (in dbSNP:rs1049215)"
FT /id="VAR_010336"
FT VARIANT 333
FT /note="S -> C"
FT /id="VAR_010324"
FT VARIANT 362
FT /note="L -> R (in dbSNP:rs1130468)"
FT /id="VAR_049989"
FT VARIANT 394
FT /note="E -> Q (in dbSNP:rs1130513)"
FT /id="VAR_049990"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:7K81"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3VH8"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3VH8"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:3VH8"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:3VH8"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:7K81"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:7K80"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:3VH8"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3WUW"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:7K80"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:3VH8"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:7K80"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:3VH8"
SQ SEQUENCE 444 AA; 49098 MW; 47DEA12BBAFDEC53 CRC64;
MSLMVVSMAC VGLFLVQRAG PHMGGQDKPF LSAWPSAVVP RGGHVTLRCH YRHRFNNFML
YKEDRIHIPI FHGRIFQESF NMSPVTTAHA GNYTCRGSHP HSPTGWSAPS NPVVIMVTGN
HRKPSLLAHP GPLVKSGERV ILQCWSDIMF EHFFLHKEGI SKDPSRLVGQ IHDGVSKANF
SIGPMMLALA GTYRCYGSVT HTPYQLSAPS DPLDIVVTGP YEKPSLSAQP GPKVQAGESV
TLSCSSRSSY DMYHLSREGG AHERRLPAVR KVNRTFQADF PLGPATHGGT YRCFGSFRHS
PYEWSDPSDP LLVSVTGNPS SSWPSPTEPS SKSGNPRHLH ILIGTSVVII LFILLLFFLL
HLWCSNKKNA AVMDQEPAGN RTANSEDSDE QDPEEVTYAQ LDHCVFTQRK ITRPSQRPKT
PPTDTILYTE LPNAKPRSKV VSCP
