KI2S4_HUMAN
ID KI2S4_HUMAN Reviewed; 304 AA.
AC P43632; Q6H2G7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 166.
DE RecName: Full=Killer cell immunoglobulin-like receptor 2DS4 {ECO:0000305};
DE AltName: Full=CD158 antigen-like family member I;
DE AltName: Full=Natural killer-associated transcript 8;
DE Short=NKAT-8;
DE AltName: Full=P58 natural killer cell receptor clones CL-39/CL-17;
DE Short=p58 NK receptor CL-39/CL-17;
DE AltName: CD_antigen=CD158i;
DE Flags: Precursor;
GN Name=KIR2DS4 {ECO:0000303|PubMed:24018270, ECO:0000312|HGNC:HGNC:6336};
GN Synonyms=CD158I, KKA3, NKAT8;
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].
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=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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoid tissue;
RX PubMed=8765026; DOI=10.1002/eji.1830260823;
RA Bottino C., Sivori S., Vitale M., Cantoni C., Falco M., Pende D.,
RA Morelli L., Augugliaro R., Semenzato G., Biassoni R., Moretta L.,
RA Moretta A.;
RT "A novel surface molecule homologous to the p58/p50 family of receptors is
RT selectively expressed on a subset of human natural killer cells and induces
RT both triggering of cell functions and proliferation.";
RL Eur. J. Immunol. 26:1816-1824(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 [MRNA].
RA Chan H.W., Salter R.D.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP 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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-221, FUNCTION, AND DISULFIDE
RP BONDS.
RX PubMed=19858347; DOI=10.1084/jem.20091010;
RA Graef T., Moesta A.K., Norman P.J., Abi-Rached L., Vago L.,
RA Older Aguilar A.M., Gleimer M., Hammond J.A., Guethlein L.A.,
RA Bushnell D.A., Robinson P.J., Parham P.;
RT "KIR2DS4 is a product of gene conversion with KIR3DL2 that introduced
RT specificity for HLA-A*11 while diminishing avidity for HLA-C.";
RL J. Exp. Med. 206:2557-2572(2009).
CC -!- FUNCTION: Receptor on natural killer (NK) cells for HLA-C alleles. Does
CC not inhibit the activity of NK cells. {ECO:0000269|PubMed:19858347}.
CC -!- SUBUNIT: Interacts with HLA-F; this interaction is direct.
CC {ECO:0000269|PubMed:24018270}.
CC -!- INTERACTION:
CC P43632; P01889: HLA-B; NbExp=2; IntAct=EBI-13916812, EBI-1046513;
CC P43632; P10321: HLA-C; NbExp=8; IntAct=EBI-13916812, EBI-1051396;
CC P43632; P30511: HLA-F; NbExp=4; IntAct=EBI-13916812, EBI-2811134;
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=AAC50336.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U24077; AAC50336.1; ALT_INIT; mRNA.
DR EMBL; L76671; AAB36599.1; -; mRNA.
DR EMBL; X94609; CAA64317.1; -; mRNA.
DR EMBL; AY366245; AAR16203.1; -; mRNA.
DR EMBL; AF002255; AAB61281.1; -; mRNA.
DR EMBL; BC101977; AAI01978.1; -; mRNA.
DR EMBL; BC103693; AAI03694.1; -; mRNA.
DR RefSeq; NP_001268900.1; NM_001281971.1.
DR RefSeq; NP_001268901.1; NM_001281972.1.
DR RefSeq; NP_036446.3; NM_012314.5.
DR PDB; 3H8N; X-ray; 2.50 A; A=27-221.
DR PDBsum; 3H8N; -.
DR AlphaFoldDB; P43632; -.
DR SMR; P43632; -.
DR IntAct; P43632; 8.
DR GlyGen; P43632; 5 sites.
DR BioMuta; KIR2DS4; -.
DR DMDM; 2828511; -.
DR jPOST; P43632; -.
DR MassIVE; P43632; -.
DR PeptideAtlas; P43632; -.
DR PRIDE; P43632; -.
DR DNASU; 3809; -.
DR Ensembl; ENST00000611311.1; ENSP00000484123.1; ENSG00000276885.1.
DR Ensembl; ENST00000612783.1; ENSP00000481753.1; ENSG00000274957.1.
DR Ensembl; ENST00000613654.1; ENSP00000483112.1; ENSG00000276634.1.
DR Ensembl; ENST00000614639.1; ENSP00000481319.1; ENSG00000275731.1.
DR Ensembl; ENST00000617469.1; ENSP00000477744.1; ENSG00000276395.1.
DR Ensembl; ENST00000617825.1; ENSP00000483274.1; ENSG00000275353.1.
DR Ensembl; ENST00000619771.1; ENSP00000478241.1; ENSG00000274947.1.
DR Ensembl; ENST00000620669.1; ENSP00000480062.1; ENSG00000274406.1.
DR Ensembl; ENST00000621436.1; ENSP00000479843.1; ENSG00000276154.1.
DR Ensembl; ENST00000638566.2; ENSP00000492248.1; ENSG00000284264.3.
DR Ensembl; ENST00000640817.2; ENSP00000491676.1; ENSG00000283870.3.
DR Ensembl; ENST00000640941.2; ENSP00000492546.1; ENSG00000283882.3.
DR Ensembl; ENST00000642862.2; ENSP00000494622.1; ENSG00000283882.3.
DR Ensembl; ENST00000644051.2; ENSP00000494670.1; ENSG00000283870.3.
DR Ensembl; ENST00000644154.2; ENSP00000495680.1; ENSG00000284264.3.
DR GeneID; 3809; -.
DR KEGG; hsa:3809; -.
DR UCSC; uc061emp.1; human.
DR CTD; 3809; -.
DR DisGeNET; 3809; -.
DR GeneCards; KIR2DS4; -.
DR HGNC; HGNC:6336; KIR2DS4.
DR MIM; 604955; gene.
DR neXtProt; NX_P43632; -.
DR PharmGKB; PA30121; -.
DR InParanoid; P43632; -.
DR OrthoDB; 1000446at2759; -.
DR PhylomeDB; P43632; -.
DR PathwayCommons; P43632; -.
DR Reactome; R-HSA-2172127; DAP12 interactions.
DR SignaLink; P43632; -.
DR BioGRID-ORCS; 3809; 2 hits in 155 CRISPR screens.
DR EvolutionaryTrace; P43632; -.
DR GeneWiki; KIR2DS4; -.
DR GenomeRNAi; 3809; -.
DR Pharos; P43632; Tdark.
DR PRO; PR:P43632; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P43632; protein.
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 Gene3D; 2.60.40.10; -; 2.
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; 2.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 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 2DS4"
FT /id="PRO_0000015085"
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 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
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:19858347"
FT DISULFID 149..198
FT /evidence="ECO:0000269|PubMed:19858347"
FT VARIANT 65
FT /note="K -> M (in dbSNP:rs1130480)"
FT /id="VAR_049980"
FT VARIANT 68
FT /note="N -> D (in dbSNP:rs1130481)"
FT /id="VAR_049981"
FT VARIANT 71
FT /note="H -> R (in dbSNP:rs1130482)"
FT /id="VAR_049982"
FT VARIANT 89
FT /note="P -> R (in dbSNP:rs1130487)"
FT /id="VAR_049983"
FT VARIANT 92
FT /note="P -> H (in dbSNP:rs1143508)"
FT /id="VAR_049984"
FT VARIANT 93
FT /note="V -> D (in dbSNP:rs1130491)"
FT /id="VAR_049985"
FT VARIANT 103
FT /note="S -> C (in dbSNP:rs10406301)"
FT /id="VAR_049986"
FT VARIANT 178
FT /note="N -> H (in dbSNP:rs4806591)"
FT /id="VAR_059423"
FT VARIANT 205
FT /note="A -> S (in dbSNP:rs1049290)"
FT /id="VAR_059424"
FT VARIANT 254
FT /note="K -> N (in dbSNP:rs1063326)"
FT /id="VAR_059425"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 96..106
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:3H8N"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:3H8N"
SQ SEQUENCE 304 AA; 33583 MW; CEFDAFF3FD679A3F CRC64;
MSLMVIIMAC VGFFLLQGAW PQEGVHRKPS FLALPGHLVK SEETVILQCW SDVMFEHFLL
HREGKFNNTL HLIGEHHDGV SKANFSIGPM MPVLAGTYRC YGSVPHSPYQ LSAPSDPLDM
VIIGLYEKPS LSAQPGPTVQ AGENVTLSCS SRSSYDMYHL SREGEAHERR LPAVRSINGT
FQADFPLGPA THGGTYRCFG SFRDAPYEWS NSSDPLLVSV TGNPSNSWPS PTEPSSKTGN
PRHLHVLIGT SVVKIPFTIL LFFLLHRWCS DKKNAAVMDQ EPAGNRTVNS EDSDEQDHQE
VSYA
