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Database: UniProt
Entry: A0A1V6R7P5_9EURO
LinkDB: A0A1V6R7P5_9EURO
Original site: A0A1V6R7P5_9EURO 
ID   A0A1V6R7P5_9EURO        Unreviewed;       189 AA.
AC   A0A1V6R7P5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   22-FEB-2023, entry version 13.
DE   RecName: Full=Protein RER1 {ECO:0000256|PIRNR:PIRNR016013};
GN   ORFNames=PENSOL_c013G02965 {ECO:0000313|EMBL:OQD97212.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD97212.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane
CC       proteins from the early Golgi compartment.
CC       {ECO:0000256|PIRNR:PIRNR016013}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the RER1 family. {ECO:0000256|ARBA:ARBA00006070,
CC       ECO:0000256|PIRNR:PIRNR016013}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQD97212.1}.
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DR   EMBL; MDYO01000013; OQD97212.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6R7P5; -.
DR   STRING; 60172.A0A1V6R7P5; -.
DR   OrthoDB; 415184at2759; -.
DR   Proteomes; UP000191612; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051179; P:localization; IEA:UniProt.
DR   InterPro; IPR004932; Rer1.
DR   PANTHER; PTHR10743; PROTEIN RER1; 1.
DR   PANTHER; PTHR10743:SF0; PROTEIN RER1; 1.
DR   Pfam; PF03248; Rer1; 1.
DR   PIRSF; PIRSF016013; AtER_Rer1p; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR016013};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191612};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   189 AA;  22121 MW;  9903C125C2E448A3 CRC64;
     MDVPEPDQSP FTAVSAHTSR LTRHYQAYLD ASTPYTTYRW VGSGVLLFLF FLRIFLAQGW
     YIVAYTLGIY LLNLFLAFLT PKFDPSLTQD EGLEDGDAGS PSLPTKKDEE FRPFIRRLPE
     FKFWHSATRA ITIGFVCSWL AVFDIPVFWP VLVVYWMILF VLTMRRQIQH MIKYRYVPFS
     FGKTRYGRS
//
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