RAE1B_MOUSE
ID RAE1B_MOUSE Reviewed; 253 AA.
AC O08603; A2RS95;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Retinoic acid early-inducible protein 1-beta;
DE Short=RAE-1-beta;
DE Flags: Precursor;
GN Name=Raet1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:BAA19485.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=8882725; DOI=10.1093/oxfordjournals.jbchem.a021242;
RA Zou Z., Nomura M., Takihara Y., Yasunaga T., Shimada K.;
RT "Isolation and characterization of retinoic acid-inducible cDNA clones in
RT F9 cells: a novel cDNA family encodes cell surface proteins sharing partial
RT homology with MHC class I molecules.";
RL J. Biochem. 119:319-328(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=ddY; TISSUE=Lung;
RX PubMed=10894171; DOI=10.1016/s1074-7613(00)80222-8;
RA Cerwenka A., Bakker A.B., McClanahan T., Wagner J., Wu J., Phillips J.H.,
RA Lanier L.L.;
RT "Retinoic acid early inducible genes define a ligand family for the
RT activating NKG2D receptor in mice.";
RL Immunity 12:721-727(2000).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=8982867; DOI=10.1093/oxfordjournals.jbchem.a021517;
RA Nomura M., Zou Z., Joh T., Takihara Y., Matsuda Y., Shimada K.;
RT "Genomic structures and characterization of Rae1 family members encoding
RT GPI-anchored cell surface proteins and expressed predominantly in embryonic
RT mouse brain.";
RL J. Biochem. 120:987-995(1996).
RN [5]
RP FUNCTION AS A LIGAND FOR KLRK1.
RX PubMed=11248803; DOI=10.1038/77793;
RA Diefenbach A., Jamieson A.M., Liu S.D., Shastri N., Raulet D.H.;
RT "Ligands for the murine NKG2D receptor: expression by tumor cells and
RT activation of NK cells and macrophages.";
RL Nat. Immunol. 1:119-126(2000).
RN [6]
RP FUNCTION AS A LIGAND FOR KLRK1.
RX PubMed=11557981; DOI=10.1038/35093109;
RA Diefenbach A., Jensen E.R., Jamieson A.M., Raulet D.H.;
RT "Rae1 and H60 ligands of the NKG2D receptor stimulate tumour immunity.";
RL Nature 413:165-171(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 30-204, AND X-RAY CRYSTALLOGRAPHY
RP (1.95 ANGSTROMS) OF 30-204 IN COMPLEX WITH KLRK1.
RX PubMed=11825567; DOI=10.1016/s1074-7613(02)00258-3;
RA Li P., McDermott G., Strong R.K.;
RT "Crystal structures of RAE-1beta and its complex with the activating
RT immunoreceptor NKG2D.";
RL Immunity 16:77-86(2002).
CC -!- FUNCTION: Acts as a ligand for KLRK1. {ECO:0000269|PubMed:10894171,
CC ECO:0000269|PubMed:11248803, ECO:0000269|PubMed:11557981}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10894171,
CC ECO:0000269|PubMed:8982867}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in embryonic brain.
CC {ECO:0000269|PubMed:8982867}.
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly during early
CC embryogenesis. Detected at high levels in 7, 11 and 14-day-old embryos
CC but not in 18-day-old embryos. Very low levels detected in adults.
CC {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8882725}.
CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:8882725}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:8982867}.
CC -!- SIMILARITY: Belongs to the NKG2D ligand family. {ECO:0000305}.
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DR EMBL; D64161; BAA19485.1; -; mRNA.
DR EMBL; BC132022; AAI32023.1; -; mRNA.
DR EMBL; BC132024; AAI32025.1; -; mRNA.
DR RefSeq; NP_033043.1; NM_009017.1.
DR PDB; 1JFM; X-ray; 2.85 A; A/B/C/D/E=31-204.
DR PDB; 4PP8; X-ray; 1.95 A; C/D=31-204.
DR PDBsum; 1JFM; -.
DR PDBsum; 4PP8; -.
DR AlphaFoldDB; O08603; -.
DR SMR; O08603; -.
DR IntAct; O08603; 1.
DR GlyGen; O08603; 5 sites.
DR iPTMnet; O08603; -.
DR PhosphoSitePlus; O08603; -.
DR SwissPalm; O08603; -.
DR MaxQB; O08603; -.
DR PeptideAtlas; O08603; -.
DR PRIDE; O08603; -.
DR ProteomicsDB; 253165; -.
DR DNASU; 19369; -.
DR GeneID; 19369; -.
DR KEGG; mmu:19369; -.
DR CTD; 19369; -.
DR MGI; MGI:109432; Raet1b.
DR InParanoid; O08603; -.
DR BioGRID-ORCS; 19369; 0 hits in 16 CRISPR screens.
DR EvolutionaryTrace; O08603; -.
DR PRO; PR:O08603; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O08603; protein.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:MGI.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; IDA:UniProtKB.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IDA:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IDA:MGI.
DR GO; GO:0002839; P:positive regulation of immune response to tumor cell; IDA:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:MGI.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IDA:MGI.
DR GO; GO:0032816; P:positive regulation of natural killer cell activation; IDA:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:MGI.
DR GO; GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; IDA:MGI.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR029287; RAE-1.
DR Pfam; PF14586; MHC_I_2; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..229
FT /note="Retinoic acid early-inducible protein 1-beta"
FT /id="PRO_0000019729"
FT PROPEP 230..253
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019730"
FT REGION 198..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 229
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..56
FT DISULFID 90..190
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:4PP8"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:4PP8"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:4PP8"
FT HELIX 85..107
FT /evidence="ECO:0007829|PDB:4PP8"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:4PP8"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1JFM"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:4PP8"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:4PP8"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:4PP8"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:4PP8"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:4PP8"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:4PP8"
FT HELIX 177..199
FT /evidence="ECO:0007829|PDB:4PP8"
SQ SEQUENCE 253 AA; 28625 MW; 33842B4EF9566867 CRC64;
MAKAAVTKRH HFMIQKLLIL LSYGYTNGLD DAHSLRCNLT IKDPTPADPL WYEAKCFVGE
ILILHLSNIN KTMTSGDPGE TANATEVKKC LTQPLKNLCQ KLRNKVSNTK VDTHKTNGYP
HLQVTMIYPQ SQGRTPSATW EFNISDSYFF TFYTENMSWR SANDESGVIM NKWKDDGEFV
KQLKFLIHEC SQKMDEFLKQ SKEKPRSTSR SPSITQLTST SPLPPPSHST SKKGFISVGL
IFISLLFAFA FAM
