RAE1C_MOUSE
ID RAE1C_MOUSE Reviewed; 253 AA.
AC O08604; A2RSA1;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Retinoic acid early-inducible protein 1-gamma;
DE Short=RAE-1-gamma;
DE Flags: Precursor;
GN Name=Raet1c;
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:BAA19486.1};
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 AS A LIGAND FOR KLRK1, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=ddY {ECO:0000269|PubMed:10894171};
RC TISSUE=Lung {ECO:0000269|PubMed:10894171};
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).
CC -!- FUNCTION: Acts as a ligand for KLRK1. {ECO:0000269|PubMed:10894171}.
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; D64162; BAA19486.1; -; mRNA.
DR EMBL; BC132028; AAI32029.1; -; mRNA.
DR EMBL; BC132032; AAI32033.1; -; mRNA.
DR RefSeq; NP_033044.1; NM_009018.1.
DR PDB; 4G59; X-ray; 2.44 A; A/B=29-232.
DR PDBsum; 4G59; -.
DR AlphaFoldDB; O08604; -.
DR SMR; O08604; -.
DR GlyGen; O08604; 5 sites.
DR iPTMnet; O08604; -.
DR PhosphoSitePlus; O08604; -.
DR SwissPalm; O08604; -.
DR MaxQB; O08604; -.
DR PRIDE; O08604; -.
DR ProteomicsDB; 254976; -.
DR DNASU; 19370; -.
DR GeneID; 19370; -.
DR KEGG; mmu:19370; -.
DR UCSC; uc033fov.1; mouse.
DR CTD; 19370; -.
DR MGI; MGI:109431; Raet1c.
DR InParanoid; O08604; -.
DR PhylomeDB; O08604; -.
DR BioGRID-ORCS; 19370; 0 hits in 16 CRISPR screens.
DR PRO; PR:O08604; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O08604; protein.
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: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 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..227
FT /note="Retinoic acid early-inducible protein 1-gamma"
FT /id="PRO_0000019731"
FT PROPEP 228..253
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019732"
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 227
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 /evidence="ECO:0000250"
FT DISULFID 90..190
FT /evidence="ECO:0000250"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:4G59"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:4G59"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:4G59"
FT HELIX 83..107
FT /evidence="ECO:0007829|PDB:4G59"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:4G59"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:4G59"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:4G59"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:4G59"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:4G59"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:4G59"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:4G59"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:4G59"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:4G59"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4G59"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:4G59"
SQ SEQUENCE 253 AA; 28508 MW; 2EFDD89ED8A25B18 CRC64;
MAKAAVTKRH HFMIQKLLIL LSYGYTNGLD DAHSLRCNLT IKAPTPADPL WYEAKCLVDE
ILILHLSNIN KTMTSGDPGE TANATEVGEC LTQPVNDLCQ KLRDKVSNTK VDTHKTNGYP
HLQVTMIYPQ SQGQTPSATW EFNISDSYFF TFYTENMSWR SANDESGVIM NKWNDDGDLV
QRLKYFIPEC RQKIDEFLKQ SKEKPRSTSR SPSITQLTST SPLPPPSHST SKKGFISVGL
IFISLLFAFA FAM
