REEP3_MOUSE
ID REEP3_MOUSE Reviewed; 254 AA.
AC Q99KK1; Q9CZM8; Q9D8G3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Receptor expression-enhancing protein 3;
GN Name=Reep3; Synonyms=D10Ucla1;
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].
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;
RC TISSUE=Corpus striatum, Embryo, Small intestine, and Spinal cord;
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=FVB/N; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-200 AND SER-209, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
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).
CC -!- FUNCTION: Microtubule-binding protein required to ensure proper cell
CC division and nuclear envelope reassembly by sequestering the
CC endoplasmic reticulum away from chromosomes during mitosis. Probably
CC acts by clearing the endoplasmic reticulum membrane from metaphase
CC chromosomes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB25434.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY562231; AAT70676.1; -; mRNA.
DR EMBL; AK008058; BAB25434.1; ALT_SEQ; mRNA.
DR EMBL; AK012403; BAB28218.1; -; mRNA.
DR EMBL; AK047728; BAC33141.1; -; mRNA.
DR EMBL; AK079649; BAC37714.1; -; mRNA.
DR EMBL; BC004607; AAH04607.1; -; mRNA.
DR CCDS; CCDS35926.1; -.
DR RefSeq; NP_848721.1; NM_178606.5.
DR AlphaFoldDB; Q99KK1; -.
DR IntAct; Q99KK1; 1.
DR MINT; Q99KK1; -.
DR STRING; 10090.ENSMUSP00000020023; -.
DR iPTMnet; Q99KK1; -.
DR PhosphoSitePlus; Q99KK1; -.
DR EPD; Q99KK1; -.
DR jPOST; Q99KK1; -.
DR MaxQB; Q99KK1; -.
DR PaxDb; Q99KK1; -.
DR PeptideAtlas; Q99KK1; -.
DR PRIDE; Q99KK1; -.
DR ProteomicsDB; 255007; -.
DR Antibodypedia; 45181; 82 antibodies from 21 providers.
DR DNASU; 28193; -.
DR Ensembl; ENSMUST00000020023; ENSMUSP00000020023; ENSMUSG00000019873.
DR GeneID; 28193; -.
DR KEGG; mmu:28193; -.
DR UCSC; uc007flq.2; mouse.
DR CTD; 221035; -.
DR MGI; MGI:88930; Reep3.
DR VEuPathDB; HostDB:ENSMUSG00000019873; -.
DR eggNOG; KOG1726; Eukaryota.
DR GeneTree; ENSGT00940000158794; -.
DR HOGENOM; CLU_028431_0_1_1; -.
DR InParanoid; Q99KK1; -.
DR OMA; DLTISWF; -.
DR PhylomeDB; Q99KK1; -.
DR TreeFam; TF314177; -.
DR BioGRID-ORCS; 28193; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Reep3; mouse.
DR PRO; PR:Q99KK1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q99KK1; protein.
DR Bgee; ENSMUSG00000019873; Expressed in rostral migratory stream and 259 other tissues.
DR ExpressionAtlas; Q99KK1; baseline and differential.
DR Genevisible; Q99KK1; MM.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IBA:GO_Central.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; ISS:UniProtKB.
DR GO; GO:0006998; P:nuclear envelope organization; ISS: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 Cell cycle; Cell division; Endoplasmic reticulum; Membrane; Microtubule;
KW Mitosis; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..254
FT /note="Receptor expression-enhancing protein 3"
FT /id="PRO_0000101827"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 162..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 50
FT /note="V -> I (in Ref. 2; BAB28218)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="K -> E (in Ref. 2; BAB28218)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="S -> F (in Ref. 2; BAB28218)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..235
FT /note="RK -> PQ (in Ref. 2; BAB28218)"
FT /evidence="ECO:0000305"
FT CONFLICT 249..250
FT /note="RP -> TT (in Ref. 2; BAB28218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 29214 MW; 2F211016F4256EA2 CRC64;
MVSWMISRAV VLVFGMLYPA YYSYKAVKTK NVKEYVRWMM YWIVFALYTV IETVADQTLA
WFPLYYELKI AFVIWLLSPY TRGASLIYRK FLHPLLSSKE REIDDYIVQA KERGYETMVN
FGRQGLNLAA AAAVTAAVKS QGAITERLRS FSMHDLTAIQ GDEPVGHRPY QTLPEAKRKG
KQATESPAYG IPLKDGSEQT DEEAEGPFSD DEMVTHKALR RSQSMKSVKT IKGRKEVRYG
SLKYKVKKRP QVYF
