RAE1E_MOUSE
ID RAE1E_MOUSE Reviewed; 251 AA.
AC Q9CZQ6; A2RSZ5;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Retinoic acid early-inducible protein 1-epsilon;
DE Short=RAE-1-epsilon;
DE Flags: Precursor;
GN Name=Raet1e;
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:BAB28147.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=C57BL/10 {ECO:0000312|EMBL:AAL17719.1};
RC TISSUE=Squamous cell carcinoma {ECO:0000312|EMBL:AAL17719.1};
RX PubMed=11567106; DOI=10.1126/science.1063916;
RA Girardi M., Oppenheim D.E., Steele C.R., Lewis J.M., Glusac E., Filler R.,
RA Hobby P., Sutton B., Tigelaar R.E., Hayday A.C.;
RT "Regulation of cutaneous malignancy by gammadelta T cells.";
RL Science 294:605-609(2001).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAL11004.1};
RC TISSUE=Lung {ECO:0000312|EMBL:AAL11004.1};
RA Lanier L.L.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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 [5]
RP FUNCTION AS A LIGAND FOR KLRK1.
RX PubMed=16086018; DOI=10.1038/ni1236;
RA Ogasawara K., Benjamin J., Takaki R., Phillips J.H., Lanier L.L.;
RT "Function of NKG2D in natural killer cell-mediated rejection of mouse bone
RT marrow grafts.";
RL Nat. Immunol. 6:938-945(2005).
CC -!- FUNCTION: Acts as a ligand for KLRK1. {ECO:0000269|PubMed:11567106,
CC ECO:0000269|PubMed:16086018}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- INDUCTION: By retinoic acid. {ECO:0000250|UniProtKB:O08603}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:O08603}.
CC -!- SIMILARITY: Belongs to the NKG2D ligand family. {ECO:0000305}.
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DR EMBL; AY056835; AAL17719.1; -; mRNA.
DR EMBL; AY054973; AAL11004.1; -; mRNA.
DR EMBL; AK012289; BAB28147.1; -; mRNA.
DR EMBL; BC132308; AAI32309.1; -; mRNA.
DR CCDS; CCDS35865.1; -.
DR RefSeq; NP_937836.1; NM_198193.2.
DR RefSeq; XP_006512840.1; XM_006512777.2.
DR RefSeq; XP_006512842.1; XM_006512779.2.
DR RefSeq; XP_006512843.1; XM_006512780.2.
DR RefSeq; XP_006512845.1; XM_006512782.2.
DR RefSeq; XP_011241480.1; XM_011243178.2.
DR RefSeq; XP_011241481.1; XM_011243179.1.
DR AlphaFoldDB; Q9CZQ6; -.
DR SMR; Q9CZQ6; -.
DR STRING; 10090.ENSMUSP00000138022; -.
DR GlyGen; Q9CZQ6; 5 sites.
DR iPTMnet; Q9CZQ6; -.
DR PhosphoSitePlus; Q9CZQ6; -.
DR MaxQB; Q9CZQ6; -.
DR PaxDb; Q9CZQ6; -.
DR PeptideAtlas; Q9CZQ6; -.
DR PRIDE; Q9CZQ6; -.
DR ProteomicsDB; 253166; -.
DR DNASU; 379043; -.
DR Ensembl; ENSMUST00000065527; ENSMUSP00000066627; ENSMUSG00000053219.
DR Ensembl; ENSMUST00000178026; ENSMUSP00000136032; ENSMUSG00000053219.
DR Ensembl; ENSMUST00000181645; ENSMUSP00000138022; ENSMUSG00000053219.
DR GeneID; 379043; -.
DR KEGG; mmu:379043; -.
DR UCSC; uc007epd.1; mouse.
DR CTD; 135250; -.
DR MGI; MGI:2675273; Raet1e.
DR VEuPathDB; HostDB:ENSMUSG00000053219; -.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_1115463_0_0_1; -.
DR InParanoid; Q9CZQ6; -.
DR OrthoDB; 1092787at2759; -.
DR PhylomeDB; Q9CZQ6; -.
DR TreeFam; TF339658; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 379043; 0 hits in 70 CRISPR screens.
DR ChiTaRS; Raet1e; mouse.
DR PRO; PR:Q9CZQ6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CZQ6; protein.
DR Bgee; ENSMUSG00000053219; Expressed in secondary oocyte and 51 other tissues.
DR ExpressionAtlas; Q9CZQ6; baseline and differential.
DR Genevisible; Q9CZQ6; MM.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0001913; P:T 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-epsilon"
FT /id="PRO_0000019735"
FT PROPEP 226..251
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019736"
FT REGION 196..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..228
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 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 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..56
FT /evidence="ECO:0000250"
FT DISULFID 88..188
FT /evidence="ECO:0000250"
SQ SEQUENCE 251 AA; 28284 MW; DAE96B471A8B07C4 CRC64;
MAKAAVTKRH HFMIQKLLIL LSYGYTNGLD DAHSLRCNLT IKDPTSADLP WCDVKCSVDE
ITILHLNNIN KTMTSGDPGK MANATGKCLT QPLNDLCQEL RDKVSNTKVD THKTNGYPHL
QVTMIYPQSQ GQTPSATWEF NISDSYFFTF YTENMSWRSA NDESGVIMNK WKDDGDLVQQ
LKYFIPQCRQ KIDEFLKQSK EKPRSTSRSP SITQLTSTSP LPPPSHSTSK KGFISVGLIF
ISLLFAFAFA M
