REEP1_MOUSE
ID REEP1_MOUSE Reviewed; 201 AA.
AC Q8BGH4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Receptor expression-enhancing protein 1;
GN Name=Reep1; Synonyms=D6Ertd253e;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH OLFR992, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Olfactory epithelium;
RX PubMed=15550249; DOI=10.1016/j.cell.2004.11.021;
RA Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H.;
RT "RTP family members induce functional expression of mammalian odorant
RT receptors.";
RL Cell 119:679-691(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Embryo, Lung, and Urinary bladder;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ZFYVE27.
RX PubMed=24668814; DOI=10.1074/jbc.m113.528687;
RA Hashimoto Y., Shirane M., Matsuzaki F., Saita S., Ohnishi T.,
RA Nakayama K.I.;
RT "Protrudin regulates endoplasmic reticulum morphology and function
RT associated with the pathogenesis of hereditary spastic paraplegia.";
RL J. Biol. Chem. 289:12946-12961(2014).
CC -!- FUNCTION: Required for endoplasmic reticulum (ER) network formation,
CC shaping and remodeling; it links ER tubules to the cytoskeleton. May
CC also enhance the cell surface expression of odorant receptors (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:15550249}.
CC -!- SUBUNIT: Interacts with OLFR992 (PubMed:15550249). Interacts with SPAST
CC and ATL1. Interacts (via C-terminus) with microtubules (By similarity).
CC Interacts with ZFYVE27 (PubMed:24668814).
CC {ECO:0000250|UniProtKB:Q9H902, ECO:0000269|PubMed:15550249,
CC ECO:0000269|PubMed:24668814}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q9H902}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:24668814}.
CC Note=A small proportion is detected at the cell surface. Localizes to
CC endoplasmic reticulum tubular network. {ECO:0000269|PubMed:15550249,
CC ECO:0000269|PubMed:24668814}.
CC -!- TISSUE SPECIFICITY: Detected in olfactory sensory neurons of the
CC olfactory epithelium, and in total brain.
CC {ECO:0000269|PubMed:15550249}.
CC -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY562229; AAT70674.1; -; mRNA.
DR EMBL; AK035238; BAC28995.1; -; mRNA.
DR EMBL; AK045056; BAC32200.1; -; mRNA.
DR EMBL; AK053158; BAC35288.1; -; mRNA.
DR EMBL; AK136916; BAE23168.1; -; mRNA.
DR EMBL; BC046826; AAH46826.1; -; mRNA.
DR CCDS; CCDS51807.1; -.
DR RefSeq; NP_848723.1; NM_178608.4.
DR AlphaFoldDB; Q8BGH4; -.
DR BioGRID; 206478; 9.
DR CORUM; Q8BGH4; -.
DR STRING; 10090.ENSMUSP00000112662; -.
DR iPTMnet; Q8BGH4; -.
DR PhosphoSitePlus; Q8BGH4; -.
DR SwissPalm; Q8BGH4; -.
DR jPOST; Q8BGH4; -.
DR MaxQB; Q8BGH4; -.
DR PaxDb; Q8BGH4; -.
DR PeptideAtlas; Q8BGH4; -.
DR PRIDE; Q8BGH4; -.
DR ProteomicsDB; 254912; -.
DR ABCD; Q8BGH4; 1 sequenced antibody.
DR Antibodypedia; 32091; 252 antibodies from 27 providers.
DR DNASU; 52250; -.
DR Ensembl; ENSMUST00000121469; ENSMUSP00000112662; ENSMUSG00000052852.
DR GeneID; 52250; -.
DR KEGG; mmu:52250; -.
DR UCSC; uc009chc.2; mouse.
DR CTD; 65055; -.
DR MGI; MGI:1098827; Reep1.
DR VEuPathDB; HostDB:ENSMUSG00000052852; -.
DR eggNOG; KOG1726; Eukaryota.
DR GeneTree; ENSGT00940000159532; -.
DR HOGENOM; CLU_028431_0_2_1; -.
DR InParanoid; Q8BGH4; -.
DR OMA; YDTLLHF; -.
DR OrthoDB; 1473891at2759; -.
DR PhylomeDB; Q8BGH4; -.
DR TreeFam; TF314177; -.
DR BioGRID-ORCS; 52250; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8BGH4; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8BGH4; protein.
DR Bgee; ENSMUSG00000052852; Expressed in indifferent gonad and 241 other tissues.
DR ExpressionAtlas; Q8BGH4; baseline and differential.
DR Genevisible; Q8BGH4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0031849; F:olfactory receptor binding; ISO:MGI.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; ISS:UniProtKB.
DR GO; GO:0051205; P:protein insertion into membrane; ISO:MGI.
DR GO; GO:0032386; P:regulation of intracellular transport; IDA:UniProtKB.
DR InterPro; IPR004345; TB2_DP1_HVA22.
DR PANTHER; PTHR12300; PTHR12300; 1.
DR Pfam; PF03134; TB2_DP1_HVA22; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..201
FT /note="Receptor expression-enhancing protein 1"
FT /id="PRO_0000101822"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 158..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 201 AA; 22285 MW; 99C33D74A71FB6B7 CRC64;
MVSWIISRLV VLIFGTLYPA YYSYKAVKSK DIKEYVKWMM YWIIFALFTT AETFTDIFLC
WFPFYYELKI AFVAWLLSPY TKGSSLLYRK FVHPTLSSKE KEIDDCLVQA KDRSYDALVH
FGKRGLNVAA TAAVMAASKG QGALSERLRS FSMQDLTTIR GDGAPAPSGP PPPGTGRSSG
KHSQPKMSRS ASESAGSSGT A
