REEP5_RAT
ID REEP5_RAT Reviewed; 189 AA.
AC B2RZ37;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Receptor expression-enhancing protein 5;
DE AltName: Full=Polyposis locus protein 1 homolog;
GN Name=Reep5; Synonyms=Dp1;
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=Heart;
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 INTERACTION WITH ATL1.
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 [3]
RP IDENTIFICATION BY 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: Plays an essential role in heart function and development by
CC regulating the organization and function of the sarcoplasmic reticulum
CC in cardiomyocytes. {ECO:0000250|UniProtKB:Q60870}.
CC -!- SUBUNIT: Monomer (By similarity). Homodimer; maybe disulfide-linked (By
CC similarity). Homotrimer (By similarity). Interacts with ATL1
CC (PubMed:19665976). Interacts with ATL2 (By similarity). Interacts with
CC ATL3 (By similarity). Interacts with CKAP4 (By similarity). Interacts
CC with RTN4 (isoforms A and B) (By similarity). Interacts with ZFYVE27
CC (By similarity). {ECO:0000250|UniProtKB:Q60870,
CC ECO:0000269|PubMed:19665976}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q60870}; Multi-pass membrane protein
CC {ECO:0000255}. Sarcoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q60870}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to endoplasmic reticulum tubular network.
CC In cardiomyocytes, localizes to the junctional sarcoplasmic reticulum
CC membrane which is closely tethered to the cell membrane and contractile
CC machinery. {ECO:0000250|UniProtKB:Q60870}.
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 -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000305}.
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DR EMBL; BC167013; AAI67013.1; -; mRNA.
DR RefSeq; NP_001102358.2; NM_001108888.2.
DR AlphaFoldDB; B2RZ37; -.
DR SMR; B2RZ37; -.
DR STRING; 10116.ENSRNOP00000027345; -.
DR iPTMnet; B2RZ37; -.
DR PhosphoSitePlus; B2RZ37; -.
DR SwissPalm; B2RZ37; -.
DR jPOST; B2RZ37; -.
DR PaxDb; B2RZ37; -.
DR PeptideAtlas; B2RZ37; -.
DR PRIDE; B2RZ37; -.
DR GeneID; 364838; -.
DR KEGG; rno:364838; -.
DR UCSC; RGD:1306047; rat.
DR CTD; 7905; -.
DR RGD; 1306047; Reep5.
DR VEuPathDB; HostDB:ENSRNOG00000020167; -.
DR eggNOG; KOG1725; Eukaryota.
DR HOGENOM; CLU_028431_2_0_1; -.
DR InParanoid; B2RZ37; -.
DR OMA; FILVLWM; -.
DR OrthoDB; 1473891at2759; -.
DR PhylomeDB; B2RZ37; -.
DR TreeFam; TF314913; -.
DR PRO; PR:B2RZ37; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000020167; Expressed in pancreas and 20 other tissues.
DR Genevisible; B2RZ37; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0090158; P:endoplasmic reticulum membrane 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 Endoplasmic reticulum; Membrane; Reference proteome;
KW Sarcoplasmic reticulum; Transmembrane; Transmembrane helix.
FT CHAIN 1..189
FT /note="Receptor expression-enhancing protein 5"
FT /id="PRO_0000384816"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TRANSMEM 35..51
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TOPO_DOM 52..53
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TOPO_DOM 75..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TOPO_DOM 104..105
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TRANSMEM 106..123
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT TOPO_DOM 124..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
FT REGION 114..185
FT /note="Required for dimerization and maintaining
FT endoplasmic reticulum morphology"
FT /evidence="ECO:0000250|UniProtKB:Q00765"
SQ SEQUENCE 189 AA; 21431 MW; 27FA9236172A8D41 CRC64;
MSAAMRERFD RFLHEKNCMT DLLAKLEAKT GVNRSFIALG VIGLVALYLV FGYGASLLCN
LIGFGYPAYI SMKAIESPNK DDDTQWLTYW VVYGVFSIAE FFSDLFLSWF PFYYMLKCGF
LLWCMAPSPS NGAELLYRRV IRPIFLKHES QVDSVVKDVK DKAKETADAI SKEVKKATVN
LLGDEKKST
