REEP6_RAT
ID REEP6_RAT Reviewed; 211 AA.
AC Q5XI60;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Receptor expression-enhancing protein 6;
DE AltName: Full=Polyposis locus protein 1-like 1;
GN Name=Reep6; Synonyms=Dp1l1;
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=Testis;
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 TISSUE SPECIFICITY.
RX PubMed=15728532; DOI=10.1167/iovs.04-0867;
RA Sato H., Tomita H., Nakazawa T., Wakana S., Tamai M.;
RT "Deleted in polyposis 1-like 1 gene (Dp1l1): a novel gene richly expressed
RT in retinal ganglion cells.";
RL Invest. Ophthalmol. Vis. Sci. 46:791-796(2005).
CC -!- FUNCTION: Required for correct function and survival of retinal
CC photoreceptors (By similarity). Required for retinal development (By
CC similarity). In rod photoreceptors, facilitates stability and/or
CC trafficking of guanylate cyclases and is required to maintain
CC endoplasmic reticulum and mitochondrial homeostasis (By similarity).
CC May play a role in clathrin-coated intracellular vesicle trafficking of
CC proteins from the endoplasmic reticulum to the retinal rod plasma
CC membrane (By similarity). {ECO:0000250|UniProtKB:Q9JM62}.
CC -!- SUBUNIT: Interacts with STX3 (By similarity). Interacts with clathrin
CC (By similarity). {ECO:0000250|UniProtKB:Q9JM62}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9JM62}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000250|UniProtKB:Q9JM62}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in retina. {ECO:0000269|PubMed:15728532}.
CC -!- SIMILARITY: Belongs to the DP1 family. {ECO:0000305}.
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DR EMBL; BC083830; AAH83830.1; -; mRNA.
DR RefSeq; NP_001013236.1; NM_001013218.1.
DR AlphaFoldDB; Q5XI60; -.
DR SMR; Q5XI60; -.
DR IntAct; Q5XI60; 8.
DR STRING; 10116.ENSRNOP00000039493; -.
DR iPTMnet; Q5XI60; -.
DR PhosphoSitePlus; Q5XI60; -.
DR jPOST; Q5XI60; -.
DR PaxDb; Q5XI60; -.
DR PRIDE; Q5XI60; -.
DR Ensembl; ENSRNOT00000044030; ENSRNOP00000039493; ENSRNOG00000033262.
DR GeneID; 362835; -.
DR KEGG; rno:362835; -.
DR UCSC; RGD:1309508; rat.
DR CTD; 92840; -.
DR RGD; 1309508; Reep6.
DR eggNOG; KOG1725; Eukaryota.
DR GeneTree; ENSGT00940000161493; -.
DR HOGENOM; CLU_028431_2_0_1; -.
DR InParanoid; Q5XI60; -.
DR OMA; HQATMDS; -.
DR OrthoDB; 1473891at2759; -.
DR PhylomeDB; Q5XI60; -.
DR TreeFam; TF314913; -.
DR PRO; PR:Q5XI60; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000033262; Expressed in testis and 19 other tissues.
DR Genevisible; Q5XI60; RN.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0044317; C:rod spherule; ISO:RGD.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISS:UniProtKB.
DR GO; GO:0032386; P:regulation of intracellular transport; ISO:RGD.
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 Cytoplasmic vesicle; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..211
FT /note="Receptor expression-enhancing protein 6"
FT /id="PRO_0000101820"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 188..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 211 AA; 23313 MW; D51FFD3C617C59B6 CRC64;
MDGLRQRFER FLEQKNVATD ALGALEARTG VEKRYLAAGA LTLLGLYLLF GYGASLLCNV
IGFVYPAYAS VKAIESPNKE DDTVWLTYWV VYALFGLVEF FSDLLLFWFP FYYAGKCAFL
LFCMTPGPWN GALLLYHRVI RPLFLKHHVA LDSAASQLSG RALDIAAGIT RDVLQALARG
RTLVTPASAS ESPAALEPDP KSSQTTLLKH K