ID   REEP5_PONAB             Reviewed;         189 AA.
AC   Q5RE33;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Receptor expression-enhancing protein 5;
DE   AltName: Full=Polyposis locus protein 1 homolog;
GN   Name=REEP5; Synonyms=DP1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (heart, ventricle). Homodimer (atria, kidney,
CC       intestine); maybe disulfide-linked. Homotrimer (heart, ventricle,
CC       skeletal muscle, liver). Interacts with ATL1. Interacts with ATL2.
CC       Interacts with ATL3. Interacts with CKAP4. Interacts with RTN4.
CC       Interacts with ZFYVE27. {ECO:0000250|UniProtKB:Q60870}.
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; CR857705; CAH89974.1; -; mRNA.
DR   RefSeq; NP_001127218.1; NM_001133746.1.
DR   AlphaFoldDB; Q5RE33; -.
DR   SMR; Q5RE33; -.
DR   STRING; 9601.ENSPPYP00000017541; -.
DR   Ensembl; ENSPPYT00000018250; ENSPPYP00000017541; ENSPPYG00000015687.
DR   GeneID; 100174273; -.
DR   KEGG; pon:100174273; -.
DR   CTD; 7905; -.
DR   eggNOG; KOG1725; Eukaryota.
DR   GeneTree; ENSGT00940000157873; -.
DR   InParanoid; Q5RE33; -.
DR   OrthoDB; 1473891at2759; -.
DR   Proteomes; UP000001595; Chromosome 5.
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:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript 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_0000101817"
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;  21461 MW;  83E57E500CA2DC60 CRC64;
     MSAAMRERFD RFLHEKNCMT DLLAKLEAKT GVNRSFIALG VIGLVALYLV FGYGASLLCN
     LIGFGYPAYI SIKAIESPNK EDDTQWLTYW VVYGVFSIAE FFSDIFLSWF PFYYMLKCGF
     LLWCMAPSPS NGAELLYKRI IRPFFLKHES QVDSVVKDLK DKAKETADAI TKEAKKATVN
     LLGEEKKST