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   24-JAN-2024, entry version 205.
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};
GN   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; P01889: HLA-B; NbExp=3; IntAct=EBI-3910993, EBI-1046513;
CC       P43629; P30511: HLA-F; NbExp=3; IntAct=EBI-3910993, EBI-2811134;
CC       P43629; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-3910993, EBI-8640191;
CC       P43629; Q9C0I4: THSD7B; NbExp=3; IntAct=EBI-3910993, EBI-311394;
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}.
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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   GlyCosmos; P43629; 3 sites, No reported glycans.
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; 9606-ENSP00000375608; -.
DR   PeptideAtlas; P43629; -.
DR   ProteomicsDB; 55643; -. [P43629-1]
DR   ProteomicsDB; 60254; -.
DR   Antibodypedia; 34883; 617 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   MANE-Select; ENST00000391728.8; ENSP00000375608.4; NM_013289.4; NP_037421.2.
DR   UCSC; uc010esf.4; human. [P43629-1]
DR   AGR; HGNC:6338; -.
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; ENSGT01100000263478; -.
DR   InParanoid; P43629; -.
DR   OMA; YEELNIN; -.
DR   OrthoDB; 4802839at2759; -.
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 1144 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 cell types or tissues.
DR   ExpressionAtlas; P43629; baseline and differential.
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:0060090; F:molecular adaptor activity; EXP:DisProt.
DR   GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR   GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:UniProtKB.
DR   CDD; cd05711; IgC2_D2_LILR_KIR_like; 2.
DR   DisProt; DP02552; -.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013151; Immunoglobulin.
DR   PANTHER; PTHR11738:SF166; KILLER CELL IMMUNOGLOBULIN-LIKE RECEPTOR 3DL1-RELATED; 1.
DR   PANTHER; PTHR11738; MHC CLASS I NK CELL RECEPTOR; 1.
DR   Pfam; PF00047; ig; 3.
DR   SMART; SM00409; IG; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   Genevisible; P43629; HS.
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
//