ID   REEP4_RAT               Reviewed;         257 AA.
AC   Q4QQW1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Receptor expression-enhancing protein 4;
GN   Name=Reep4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16396499; DOI=10.1021/pr0503073;
RA   Moser K., White F.M.;
RT   "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT   MS/MS.";
RL   J. Proteome Res. 5:98-104(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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}.
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DR   EMBL; BC097957; AAH97957.1; -; mRNA.
DR   RefSeq; NP_001020450.1; NM_001025279.1.
DR   AlphaFoldDB; Q4QQW1; -.
DR   STRING; 10116.ENSRNOP00000015169; -.
DR   iPTMnet; Q4QQW1; -.
DR   PhosphoSitePlus; Q4QQW1; -.
DR   jPOST; Q4QQW1; -.
DR   PaxDb; Q4QQW1; -.
DR   PRIDE; Q4QQW1; -.
DR   Ensembl; ENSRNOT00000015169; ENSRNOP00000015169; ENSRNOG00000011373.
DR   GeneID; 306014; -.
DR   KEGG; rno:306014; -.
DR   UCSC; RGD:1306561; rat.
DR   CTD; 80346; -.
DR   RGD; 1306561; Reep4.
DR   eggNOG; KOG1726; Eukaryota.
DR   GeneTree; ENSGT00940000161674; -.
DR   HOGENOM; CLU_028431_0_1_1; -.
DR   InParanoid; Q4QQW1; -.
DR   OMA; DTEDGCW; -.
DR   OrthoDB; 1473891at2759; -.
DR   PhylomeDB; Q4QQW1; -.
DR   TreeFam; TF314177; -.
DR   PRO; PR:Q4QQW1; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000011373; Expressed in colon and 20 other tissues.
DR   Genevisible; Q4QQW1; RN.
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; 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; ISS:UniProtKB.
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..257
FT                   /note="Receptor expression-enhancing protein 4"
FT                   /id="PRO_0000101833"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          159..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6H4"
FT   MOD_RES         196
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6H4"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6H4"
FT   MOD_RES         250
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6H4"
FT   MOD_RES         253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6H4"
SQ   SEQUENCE   257 AA;  29660 MW;  4F7A370129800F13 CRC64;
     MVSWMICRLV VLIFGMLYPA YASYKAVKSK NIREYVRWMM YWIVFAIFMA AETFTDIFIS
     WFPFYYEIKM AFVLWLLSPY TKGASLLYRK FVHPSLSRHE KEIDACIVQA KERSYETMLS
     FGKRSLNMAA SAAVQAATKS QGALAGRLRS FSMQDLRSIP DTSAPTYQDP LYLEDQAPRR
     RPPIGYRPGG LQDSDTEDEC WSDNEIAPQP PVRPREKPLS RSQSLRVVKR KPLVREGTSR
     SLKVRTRKKT IPSDLDS