KI2L2_HUMAN
ID KI2L2_HUMAN Reviewed; 348 AA.
AC P43627; C6EVR8; Q14951;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 180.
DE RecName: Full=Killer cell immunoglobulin-like receptor 2DL2 {ECO:0000305};
DE AltName: Full=CD158 antigen-like family member B1;
DE AltName: Full=Natural killer-associated transcript 6;
DE Short=NKAT-6;
DE AltName: Full=p58 natural killer cell receptor clone CL-43;
DE Short=p58 NK receptor CL-43;
DE AltName: CD_antigen=CD158b1;
DE Flags: Precursor;
GN Name=KIR2DL2 {ECO:0000312|HGNC:HGNC:6330}; Synonyms=CD158B1, NKAT6;
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 [GENOMIC DNA].
RA Hou L., Hurley C.K., Steiner N.K., Belle I.;
RT "Highly homologous KIR genes require additional strategies to obtain
RT complete coding sequences of KIR2DL2/3 alleles from genomic DNA.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 25-221, FUNCTION, AND DISULFIDE
RP BONDS.
RX PubMed=10097129; DOI=10.1073/pnas.96.7.3864;
RA Snyder G.A., Brooks A.G., Sun P.D.;
RT "Crystal structure of the HLA-Cw3 allotype-specific killer cell inhibitory
RT receptor KIR2DL2.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3864-3869(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-221 IN COMPLEX WITH HLA-CW3,
RP AND DISULFIDE BONDS.
RX PubMed=10850706; DOI=10.1038/35014520;
RA Boyington J.C., Motyka S.A., Schuck P., Brooks A.G., Sun P.D.;
RT "Crystal structure of an NK cell immunoglobulin-like receptor in complex
RT with its class I MHC ligand.";
RL Nature 405:537-543(2000).
CC -!- FUNCTION: Receptor on natural killer (NK) cells for HLA-Cw1, 3, 7, and
CC 8 allotypes. Inhibits the activity of NK cells thus preventing cell
CC lysis. {ECO:0000269|PubMed:10097129}.
CC -!- INTERACTION:
CC P43627; P10321: HLA-C; NbExp=4; IntAct=EBI-13941368, EBI-1051396;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; U24075; AAC50334.1; -; mRNA.
DR EMBL; L76669; AAB36597.1; -; mRNA.
DR EMBL; EU791544; ACI49715.1; -; Genomic_DNA.
DR RefSeq; NP_055034.2; NM_014219.2.
DR PDB; 1EFX; X-ray; 3.00 A; D/E=22-221.
DR PDB; 2DL2; X-ray; 3.00 A; A=26-221.
DR PDB; 2DLI; X-ray; 2.90 A; A=25-221.
DR PDB; 6PA1; X-ray; 3.01 A; D/H=22-225.
DR PDBsum; 1EFX; -.
DR PDBsum; 2DL2; -.
DR PDBsum; 2DLI; -.
DR PDBsum; 6PA1; -.
DR AlphaFoldDB; P43627; -.
DR SMR; P43627; -.
DR BioGRID; 110004; 21.
DR IntAct; P43627; 13.
DR ChEMBL; CHEMBL3833441; -.
DR GlyGen; P43627; 3 sites.
DR iPTMnet; P43627; -.
DR PhosphoSitePlus; P43627; -.
DR BioMuta; KIR2DL2; -.
DR DMDM; 1171725; -.
DR jPOST; P43627; -.
DR MassIVE; P43627; -.
DR PeptideAtlas; P43627; -.
DR PRIDE; P43627; -.
DR ABCD; P43627; 1 sequenced antibody.
DR DNASU; 3803; -.
DR Ensembl; ENST00000611724.4; ENSP00000482519.1; ENSG00000275546.5.
DR Ensembl; ENST00000613410.1; ENSP00000483373.1; ENSG00000276731.1.
DR Ensembl; ENST00000616831.4; ENSP00000482201.1; ENSG00000278731.5.
DR Ensembl; ENST00000618388.4; ENSP00000480161.1; ENSG00000275914.5.
DR Ensembl; ENST00000618796.1; ENSP00000481907.1; ENSG00000275407.1.
DR Ensembl; ENST00000619621.1; ENSP00000483052.1; ENSG00000276011.1.
DR GeneID; 3803; -.
DR KEGG; hsa:3803; -.
DR UCSC; uc032lsh.2; human.
DR CTD; 3803; -.
DR DisGeNET; 3803; -.
DR GeneCards; KIR2DL2; -.
DR HGNC; HGNC:6330; KIR2DL2.
DR MIM; 604937; gene.
DR neXtProt; NX_P43627; -.
DR PharmGKB; PA30115; -.
DR InParanoid; P43627; -.
DR OrthoDB; 1055520at2759; -.
DR PathwayCommons; P43627; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; P43627; -.
DR BioGRID-ORCS; 3803; 1 hit in 35 CRISPR screens.
DR EvolutionaryTrace; P43627; -.
DR GenomeRNAi; 3803; -.
DR Pharos; P43627; Tdark.
DR PRO; PR:P43627; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P43627; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR IDEAL; IID00628; -.
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..348
FT /note="Killer cell immunoglobulin-like receptor 2DL2"
FT /id="PRO_0000015079"
FT TOPO_DOM 22..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..348
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 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:10097129,
FT ECO:0000269|PubMed:10850706, ECO:0007744|PDB:1EFX,
FT ECO:0007744|PDB:2DL2, ECO:0007744|PDB:2DLI"
FT DISULFID 149..198
FT /evidence="ECO:0000269|PubMed:10097129,
FT ECO:0000269|PubMed:10850706, ECO:0007744|PDB:1EFX,
FT ECO:0007744|PDB:2DL2, ECO:0007744|PDB:2DLI"
FT VARIANT 9
FT /note="A -> V (in dbSNP:rs3810343)"
FT /id="VAR_059417"
FT VARIANT 37
FT /note="R -> P (in dbSNP:rs1555897648)"
FT /id="VAR_021929"
FT VARIANT 66
FT /note="F -> Y (in dbSNP:rs78713511)"
FT /id="VAR_059418"
FT CONFLICT 289..290
FT /note="SE -> RQ (in Ref. 2; AAB36597)"
FT /evidence="ECO:0000305"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 77..87
FT /evidence="ECO:0007829|PDB:2DLI"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1EFX"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:2DL2"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1EFX"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:2DLI"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1EFX"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:2DLI"
SQ SEQUENCE 348 AA; 38472 MW; 5B54C548F5CF3FBF CRC64;
MSLMVVSMAC VGFFLLQGAW PHEGVHRKPS LLAHPGRLVK SEETVILQCW SDVRFEHFLL
HREGKFKDTL HLIGEHHDGV SKANFSIGPM MQDLAGTYRC YGSVTHSPYQ LSAPSDPLDI
VITGLYEKPS LSAQPGPTVL AGESVTLSCS SRSSYDMYHL SREGEAHECR FSAGPKVNGT
FQADFPLGPA THGGTYRCFG SFRDSPYEWS NSSDPLLVSV IGNPSNSWPS PTEPSSKTGN
PRHLHILIGT SVVIILFILL FFLLHRWCSN KKNAAVMDQE SAGNRTANSE DSDEQDPQEV
TYTQLNHCVF TQRKITRPSQ RPKTPPTDII VYAELPNAES RSKVVSCP
