ID W6QDV2_PENRF Unreviewed; 215 AA.
AC W6QDV2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Endoplasmic reticulum transmembrane protein {ECO:0000256|RuleBase:RU367026};
GN ORFNames=PROQFM164_S03g001405 {ECO:0000313|EMBL:CDM34680.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM34680.1};
RN [1] {ECO:0000313|EMBL:CDM34680.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM34680.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- FUNCTION: May play a role in anterograde transport of membrane proteins
CC from the endoplasmic reticulum to the Golgi.
CC {ECO:0000256|RuleBase:RU367026}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367026}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367026}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family.
CC {ECO:0000256|ARBA:ARBA00007956, ECO:0000256|RuleBase:RU367026}.
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DR EMBL; HG792017; CDM34680.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QDV2; -.
DR STRING; 1365484.W6QDV2; -.
DR OMA; PYRWNRL; -.
DR OrthoDB; 1332764at2759; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IEA:UniProtKB-UniRule.
DR InterPro; IPR008417; BAP29/BAP31.
DR InterPro; IPR040463; BAP29/BAP31_N.
DR InterPro; IPR041672; Bap31/Bap29_C.
DR PANTHER; PTHR12701; BCR-ASSOCIATED PROTEIN, BAP; 1.
DR PANTHER; PTHR12701:SF18; ENDOPLASMIC RETICULUM TRANSMEMBRANE PROTEIN; 1.
DR Pfam; PF05529; Bap31; 1.
DR Pfam; PF18035; Bap31_Bap29_C; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367026};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU367026};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367026};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU367026}; Receptor {ECO:0000313|EMBL:CDM34680.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367026};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367026};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367026}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367026"
FT TRANSMEM 47..63
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367026"
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367026"
FT DOMAIN 1..139
FT /note="BAP29/BAP31 transmembrane"
FT /evidence="ECO:0000259|Pfam:PF05529"
FT DOMAIN 163..214
FT /note="Bap31/Bap29 cytoplasmic coiled-coil"
FT /evidence="ECO:0000259|Pfam:PF18035"
FT COILED 165..199
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 215 AA; 24475 MW; 56FF18BA3F2A93A7 CRC64;
MTLYYSLVFL LLVFEMGVFL ALVIPLPHVV KRKLFAFISE SPIIAKLQYG LKITFIFILI
LFIDSVNRVY RVQQELSAFA KDGPGMGAAH LGTDRMEVQA RKFYSQRNMY LCGFTLFLSL
ILNRTYTMIL ETLRLEDRVR LIEGDKKAGG KDSARIAEAG SVGEIGRLKE IIATKNRDIE
TLKKQCEGLT REYHSLGDQI SNEKGDKNEK DKKDL
//
