RAE1D_MOUSE
ID RAE1D_MOUSE Reviewed; 249 AA.
AC Q9JI58; Q3KQI0;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Retinoic acid early-inducible protein 1-delta;
DE Short=RAE-1-delta;
DE Flags: Precursor;
GN Name=Raet1d;
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:AAF97631.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS A LIGAND FOR KLRK1, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
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 [2]
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).
CC -!- FUNCTION: Acts as a ligand for KLRK1. {ECO:0000269|PubMed:10894171}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10894171};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10894171}.
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}.
CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:10894171}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:10894171}.
CC -!- SIMILARITY: Belongs to the NKG2D ligand family. {ECO:0000305}.
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DR EMBL; AF257520; AAF97631.1; -; mRNA.
DR EMBL; BC106190; AAI06191.1; -; mRNA.
DR CCDS; CCDS35866.1; -.
DR RefSeq; NP_064414.1; NM_020030.2.
DR RefSeq; XP_006512871.1; XM_006512808.2.
DR AlphaFoldDB; Q9JI58; -.
DR SMR; Q9JI58; -.
DR STRING; 10090.ENSMUSP00000093471; -.
DR GlyGen; Q9JI58; 4 sites.
DR iPTMnet; Q9JI58; -.
DR PhosphoSitePlus; Q9JI58; -.
DR MaxQB; Q9JI58; -.
DR PaxDb; Q9JI58; -.
DR PRIDE; Q9JI58; -.
DR ProteomicsDB; 255076; -.
DR DNASU; 56554; -.
DR Ensembl; ENSMUST00000095795; ENSMUSP00000093471; ENSMUSG00000078452.
DR Ensembl; ENSMUST00000182677; ENSMUSP00000138328; ENSMUSG00000078452.
DR GeneID; 56554; -.
DR KEGG; mmu:56554; -.
DR UCSC; uc007epm.1; mouse.
DR CTD; 56554; -.
DR MGI; MGI:1861032; Raet1d.
DR VEuPathDB; HostDB:ENSMUSG00000078452; -.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_1115463_0_0_1; -.
DR InParanoid; Q9JI58; -.
DR OrthoDB; 1092787at2759; -.
DR PhylomeDB; Q9JI58; -.
DR TreeFam; TF339658; -.
DR BioGRID-ORCS; 56554; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Raet1d; mouse.
DR PRO; PR:Q9JI58; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9JI58; protein.
DR Bgee; ENSMUSG00000078452; Expressed in primary oocyte and 33 other tissues.
DR Genevisible; Q9JI58; MM.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; IDA:UniProtKB.
DR GO; GO:0042267; P: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 Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..225
FT /note="Retinoic acid early-inducible protein 1-delta"
FT /id="PRO_0000019733"
FT PROPEP 226..249
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019734"
FT REGION 194..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 225
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 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..52
FT /evidence="ECO:0000250"
FT DISULFID 86..186
FT /evidence="ECO:0000250"
SQ SEQUENCE 249 AA; 27884 MW; A9E51BD08983175E CRC64;
MAKAAVTKRH HFMIQKLLIL LSYGYTNGLD DAHSLRCNLT IKAPTPADEV KCFVGEILIL
HLSNINKTMT SGDPGETANA TEVGECLTQP LKDLCQKLRD KVSNTKVDTH KTNGYPHLQV
TMIYPQSQGQ TPSATWEFNI SDSYFFTFYT EIMSWRSAND ESGVIMNKWK DDGEFVKQLK
FLIHGCSQKM DEFLKQSKEK PRSTSRSPSI TQLTSTSPLP PTSHSTSKKG FISVGLIFIS
LLFAFAFAM
