REEP5_MOUSE
ID REEP5_MOUSE Reviewed; 185 AA.
AC Q60870;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Receptor expression-enhancing protein 5;
DE AltName: Full=GP106;
DE AltName: Full=Polyposis locus protein 1 homolog;
DE AltName: Full=Protein TB2 homolog;
GN Name=Reep5; Synonyms=Dp1;
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=8647449; DOI=10.1016/0378-1119(95)00827-6;
RA Prieschl E.E., Pendl G.G., Harrer N.E., Baumruker T.;
RT "The murine homolog of TB2/DP1, a gene of the familial adenomatous
RT polyposis (FAP) locus.";
RL Gene 169:215-218(1996).
RN [2]
RP PROTEIN SEQUENCE OF 13-21 AND 144-153, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP INTERACTION WITH ATL1 AND ATL2.
RX PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA Rapoport T.A., Blackstone C.;
RT "A class of dynamin-like GTPases involved in the generation of the tubular
RT ER network.";
RL Cell 138:549-561(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen,
RC and 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 [5]
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).
RN [6]
RP FUNCTION, SUBUNIT, INTERACTION WITH ATL3; CKAP4 AND RTN4, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=32075961; DOI=10.1038/s41467-019-14143-9;
RA Lee S.H., Hadipour-Lakmehsari S., Murthy H.R., Gibb N., Miyake T.,
RA Teng A.C.T., Cosme J., Yu J.C., Moon M., Lim S., Wong V., Liu P.,
RA Billia F., Fernandez-Gonzalez R., Stagljar I., Sharma P., Kislinger T.,
RA Scott I.C., Gramolini A.O.;
RT "REEP5 depletion causes sarco-endoplasmic reticulum vacuolization and
RT cardiac functional defects.";
RL Nat. Commun. 11:965-965(2020).
CC -!- FUNCTION: Plays an essential role in heart function and development by
CC regulating the organization and function of the sarcoplasmic reticulum
CC in cardiomyocytes. {ECO:0000269|PubMed:32075961}.
CC -!- SUBUNIT: Monomer (heart including ventricles) (PubMed:32075961).
CC Homodimer (atria, kidney, intestine); maybe disulfide-linked
CC (PubMed:32075961). Homotrimer (heart, ventricle, skeletal muscle,
CC liver) (PubMed:32075961). Interacts with ATL1 (PubMed:19665976).
CC Interacts with ATL2 (PubMed:19665976). Interacts with ATL3
CC (PubMed:32075961). Interacts with CKAP4 (PubMed:32075961). Interacts
CC with RTN4 (isoforms A and B) (PubMed:32075961). Interacts with ZFYVE27
CC (PubMed:24668814). {ECO:0000269|PubMed:19665976,
CC ECO:0000269|PubMed:24668814, ECO:0000269|PubMed:32075961}.
CC -!- INTERACTION:
CC Q60870; Q8WXF7: ATL1; Xeno; NbExp=2; IntAct=EBI-2410304, EBI-2410266;
CC Q60870; Q8NHH9: ATL2; Xeno; NbExp=2; IntAct=EBI-2410304, EBI-2410430;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24668814}; Multi-pass membrane protein
CC {ECO:0000255}. Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:32075961}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to endoplasmic reticulum tubular network
CC (PubMed:24668814). In cardiomyocytes, localizes to the junctional
CC sarcoplasmic reticulum membrane which is closely tethered to the cell
CC membrane and contractile machinery (PubMed:32075961).
CC {ECO:0000269|PubMed:24668814, ECO:0000269|PubMed:32075961}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart including ventricles (at
CC protein level). Expressed in cardiomyocytes (at protein level)
CC (PubMed:32075961). Also, expressed in skeletal muscle and kidney and to
CC a lesser extend in brain, liver and intestine (at protein level)
CC (PubMed:32075961). {ECO:0000269|PubMed:32075961}.
CC -!- DOMAIN: The short lumenal loops between transmembrane domains 1 and 2
CC and between transmembrane domains 3 and 4 may impart a wedge-like
CC configuration, thus deforming membranes.
CC {ECO:0000250|UniProtKB:Q00765}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the heart of P10
CC neonatal mice causes lethal cardiac dysfunction at 4 weeks
CC (PubMed:19665976). Myocardium is disorganized with greater fibrotic
CC regions with significant collagen deposition in the ventricular
CC myocardium (PubMed:19665976). Mice show significant myocardial
CC dilatation and cardiac contractile dysfunction (PubMed:19665976). Also,
CC sarcomere organization is disordered and the sarcoplasmic reticulum
CC membrane forms vacuoles (PubMed:19665976). Myocardium has elevated
CC expression levels of ER stress marker Hspa5/Grp78, cleaved Casp12,
CC Rtn4, Atl3 and Ckap4 (PubMed:19665976). {ECO:0000269|PubMed:19665976}.
CC -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000305}.
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DR EMBL; U28168; AAB07994.1; -; mRNA.
DR PIR; JC4667; JC4667.
DR AlphaFoldDB; Q60870; -.
DR IntAct; Q60870; 2.
DR STRING; 10090.ENSMUSP00000006027; -.
DR iPTMnet; Q60870; -.
DR PhosphoSitePlus; Q60870; -.
DR SwissPalm; Q60870; -.
DR EPD; Q60870; -.
DR jPOST; Q60870; -.
DR MaxQB; Q60870; -.
DR PaxDb; Q60870; -.
DR PeptideAtlas; Q60870; -.
DR PRIDE; Q60870; -.
DR ProteomicsDB; 253201; -.
DR MGI; MGI:1270152; Reep5.
DR eggNOG; KOG1725; Eukaryota.
DR InParanoid; Q60870; -.
DR PhylomeDB; Q60870; -.
DR ChiTaRS; Reep5; mouse.
DR PRO; PR:Q60870; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60870; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
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:0014701; C:junctional sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IMP: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 Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Sarcoplasmic reticulum; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..185
FT /note="Receptor expression-enhancing protein 5"
FT /id="PRO_0000101816"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TRANSMEM 31..47
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TOPO_DOM 48..49
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TOPO_DOM 71..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TRANSMEM 81..99
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TOPO_DOM 100..101
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TRANSMEM 102..119
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TOPO_DOM 120..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT REGION 110..181
FT /note="Required for dimerization and maintaining
FT endoplasmic reticulum morphology"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
SQ SEQUENCE 185 AA; 21051 MW; 706F03AB257D7D0C CRC64;
MRERFDRFLH EKNCMTDLLA KLEAKTGVNR SFIALGVIGL VALYLVFGYG ASLLCNLIGF
GYPAYISMKA IESPNKDDDT QWLTYWVVYG VFSIAEFFSD LFLSWLPFYY MLKCGFLLWC
MAPSPANGAE MLYRRIIRPI FLRHESQVDS VVKDVKDKAK ETADAISKEV KKATVNLLGD
VKKST
