ID   KI2S2_HUMAN             Reviewed;         304 AA.
AC   P43631; Q14955; Q6H2G9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Killer cell immunoglobulin-like receptor 2DS2 {ECO:0000305};
DE   AltName: Full=CD158 antigen-like family member J;
DE   AltName: Full=NK receptor 183 ActI;
DE   AltName: Full=Natural killer-associated transcript 5;
DE            Short=NKAT-5;
DE   AltName: Full=p58 natural killer cell receptor clone CL-49;
DE            Short=p58 NK receptor CL-49;
DE   AltName: CD_antigen=CD158j;
DE   Flags: Precursor;
GN   Name=KIR2DS2 {ECO:0000312|HGNC:HGNC:6334}; Synonyms=CD158J, NKAT5;
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] OF 2-304.
RC   TISSUE=Natural killer cell;
RX   PubMed=7749980; DOI=10.1016/1074-7613(95)90025-x;
RA   Wagtmann N., Biassoni R., Cantoni C., Verdiani S., Malnati M.S., Vitale M.,
RA   Bottino C., Moretta L., Moretta A., Long E.O.;
RT   "Molecular clones of the p58 NK cell receptor reveal immunoglobulin-related
RT   molecules with diversity in both the extra- and intracellular domains.";
RL   Immunity 2:439-449(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lymphoid tissue;
RX   PubMed=8627176; DOI=10.1084/jem.183.2.645;
RA   Biassoni R., Cantoni C., Falco M., Verdiani S., Bottino C., Vitale M.,
RA   Conte R., Poggi A., Moretta A., Moretta L.;
RT   "The human leukocyte antigen (HLA)-C-specific 'activatory' or 'inhibitory'
RT   natural killer cell receptors display highly homologous extracellular
RT   domains but differ in their transmembrane and intracytoplasmic portions.";
RL   J. Exp. Med. 183:645-650(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=14607943; DOI=10.4049/jimmunol.171.10.5396;
RA   Artavanis-Tsakonas K., Eleme K., McQueen K.L., Cheng N.W., Parham P.,
RA   Davis D.M., Riley E.M.;
RT   "Activation of a subset of human NK cells upon contact with Plasmodium
RT   falciparum-infected erythrocytes.";
RL   J. Immunol. 171:5396-5405(2003).
RN   [5]
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   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-221, AND DISULFIDE BONDS.
RX   PubMed=12668644; DOI=10.1084/jem.20021624;
RA   Saulquin X., Gastinel L.N., Vivier E.;
RT   "Crystal structure of the human natural killer cell activating receptor
RT   KIR2DS2 (CD158j).";
RL   J. Exp. Med. 197:933-938(2003).
CC   -!- FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles. Does
CC       not inhibit the activity of NK cells.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC50338.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U24079; AAC50338.1; ALT_INIT; mRNA.
DR   EMBL; L41347; AAA65225.1; -; mRNA.
DR   EMBL; X89893; CAA61983.1; -; mRNA.
DR   EMBL; AY366243; AAR16201.1; -; mRNA.
DR   EMBL; AL133414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001278624.1; NM_001291695.1.
DR   RefSeq; NP_001278625.1; NM_001291696.1.
DR   RefSeq; NP_001278629.1; NM_001291700.1.
DR   RefSeq; NP_001278630.1; NM_001291701.1.
DR   RefSeq; NP_036444.1; NM_012312.4.
DR   RefSeq; XP_016885764.1; XM_017030275.1.
DR   PDB; 1M4K; X-ray; 2.30 A; A=22-221.
DR   PDB; 4N8V; X-ray; 2.50 A; G/I=22-221.
DR   PDB; 7DUU; X-ray; 2.51 A; D=22-221.
DR   PDBsum; 1M4K; -.
DR   PDBsum; 4N8V; -.
DR   PDBsum; 7DUU; -.
DR   AlphaFoldDB; P43631; -.
DR   SMR; P43631; -.
DR   BioGRID; 110005; 63.
DR   BioGRID; 110008; 41.
DR   BioGRID; 125444; 50.
DR   IntAct; P43631; 22.
DR   GlyCosmos; P43631; 3 sites, No reported glycans.
DR   GlyGen; P43631; 3 sites.
DR   iPTMnet; P43631; -.
DR   PhosphoSitePlus; P43631; -.
DR   BioMuta; KIR2DS2; -.
DR   DMDM; 13124793; -.
DR   jPOST; P43631; -.
DR   MassIVE; P43631; -.
DR   PeptideAtlas; P43631; -.
DR   DNASU; 100132285; -.
DR   Ensembl; ENST00000610441.1; ENSP00000484281.1; ENSG00000277885.1.
DR   Ensembl; ENST00000611495.1; ENSP00000484082.1; ENSG00000276425.1.
DR   Ensembl; ENST00000612182.1; ENSP00000478509.1; ENSG00000274438.1.
DR   Ensembl; ENST00000613378.1; ENSP00000482725.1; ENSG00000274518.1.
DR   Ensembl; ENST00000614231.1; ENSP00000482770.1; ENSG00000275253.1.
DR   Ensembl; ENST00000614727.4; ENSP00000483792.1; ENSG00000276139.4.
DR   Ensembl; ENST00000616472.1; ENSP00000482637.1; ENSG00000275452.2.
DR   Ensembl; ENST00000616541.4; ENSP00000484771.1; ENSG00000278300.4.
DR   Ensembl; ENST00000617284.4; ENSP00000478014.1; ENSG00000278300.4.
DR   Ensembl; ENST00000617984.1; ENSP00000477892.1; ENSG00000275737.1.
DR   Ensembl; ENST00000618364.1; ENSP00000483804.1; ENSG00000275735.1.
DR   Ensembl; ENST00000619473.1; ENSP00000484400.1; ENSG00000276258.1.
DR   Ensembl; ENST00000622127.1; ENSP00000481307.1; ENSG00000278152.2.
DR   GeneID; 100132285; -.
DR   KEGG; hsa:100132285; -.
DR   MANE-Select; ENST00000617284.5; ENSP00000478014.1; NM_012312.5; NP_036444.1.
DR   UCSC; uc032izx.2; human.
DR   AGR; HGNC:6334; -.
DR   CTD; 100132285; -.
DR   DisGeNET; 100132285; -.
DR   GeneCards; KIR2DS2; -.
DR   HGNC; HGNC:6334; KIR2DS2.
DR   MIM; 604953; gene.
DR   neXtProt; NX_P43631; -.
DR   PharmGKB; PA30119; -.
DR   InParanoid; P43631; -.
DR   PathwayCommons; P43631; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-2172127; DAP12 interactions.
DR   SignaLink; P43631; -.
DR   BioGRID-ORCS; 100132285; 0 hits in 35 CRISPR screens.
DR   EvolutionaryTrace; P43631; -.
DR   GenomeRNAi; 100132285; -.
DR   Pharos; P43631; Tdark.
DR   PRO; PR:P43631; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; P43631; Protein.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:UniProtKB.
DR   GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR   GO; GO:0002222; P:stimulatory killer cell immunoglobulin-like receptor signaling pathway; IDA:UniProtKB.
DR   CDD; cd05711; IgC2_D2_LILR_KIR_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
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:SF168; KILLER CELL IMMUNOGLOBULIN-LIKE RECEPTOR 2DL2-RELATED; 1.
DR   PANTHER; PTHR11738; MHC CLASS I NK CELL RECEPTOR; 1.
DR   Pfam; PF00047; ig; 2.
DR   SMART; SM00409; IG; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
PE   1: Evidence at protein level;
KW   3D-structure; 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..304
FT                   /note="Killer cell immunoglobulin-like receptor 2DS2"
FT                   /id="PRO_0000015083"
FT   TOPO_DOM        22..245
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..304
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          42..107
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          142..205
FT                   /note="Ig-like C2-type 2"
FT   REGION          220..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        49..100
FT                   /evidence="ECO:0000269|PubMed:12668644"
FT   DISULFID        149..198
FT                   /evidence="ECO:0000269|PubMed:12668644"
FT   VARIANT         9
FT                   /note="A -> V (in dbSNP:rs189739973)"
FT                   /id="VAR_059420"
FT   VARIANT         66
FT                   /note="Y -> F (in dbSNP:rs1049626616)"
FT                   /id="VAR_059421"
FT   VARIANT         237
FT                   /note="K -> E (in dbSNP:rs2262065)"
FT                   /id="VAR_020090"
FT   VARIANT         254
FT                   /note="K -> N (in dbSNP:rs1063326)"
FT                   /id="VAR_059422"
FT   CONFLICT        20
FT                   /note="W -> G (in Ref. 3; CAA61983)"
FT                   /evidence="ECO:0000305"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          45..53
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          56..62
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          75..79
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          81..87
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          96..103
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          105..108
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          118..123
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          130..135
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          143..162
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          169..172
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:7DUU"
FT   STRAND          180..189
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          194..201
FT                   /evidence="ECO:0007829|PDB:1M4K"
FT   STRAND          205..209
FT                   /evidence="ECO:0007829|PDB:4N8V"
FT   STRAND          216..220
FT                   /evidence="ECO:0007829|PDB:1M4K"
SQ   SEQUENCE   304 AA;  33502 MW;  186C77DD9E86BA28 CRC64;
     MSLMVVSMAC VGFFLLQGAW PHEGVHRKPS LLAHPGPLVK SEETVILQCW SDVRFEHFLL
     HREGKYKDTL HLIGEHHDGV SKANFSIGPM MQDLAGTYRC YGSVTHSPYQ LSAPSDPLDI
     VITGLYEKPS LSAQPGPTVL AGESVTLSCS SRSSYDMYHL SREGEAHERR FSAGPKVNGT
     FQADFPLGPA THGGTYRCFG SFRDSPYEWS NSSDPLLVSV TGNPSNSWPS PTEPSSKTGN
     PRHLHVLIGT SVVKIPFTIL LFFLLHRWCS NKKNAAVMDQ EPAGNRTVNS EDSDEQDHQE
     VSYA
//