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Database: UniProt
Entry: A0A1V6V7M6_9EURO
LinkDB: A0A1V6V7M6_9EURO
Original site: A0A1V6V7M6_9EURO 
ID   A0A1V6V7M6_9EURO        Unreviewed;       216 AA.
AC   A0A1V6V7M6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Endoplasmic reticulum transmembrane protein {ECO:0000256|RuleBase:RU367026};
GN   ORFNames=PENCOP_c001G08864 {ECO:0000313|EMBL:OQE46646.1};
OS   Penicillium coprophilum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE46646.1, ECO:0000313|Proteomes:UP000191500};
RN   [1] {ECO:0000313|Proteomes:UP000191500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
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: 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}.
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:OQE46646.1}.
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DR   EMBL; MDDG01000001; OQE46646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6V7M6; -.
DR   STRING; 36646.A0A1V6V7M6; -.
DR   OrthoDB; 1332764at2759; -.
DR   Proteomes; UP000191500; Unassembled WGS sequence.
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};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191500};
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..140
FT                   /note="BAP29/BAP31 transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF05529"
FT   DOMAIN          163..215
FT                   /note="Bap31/Bap29 cytoplasmic coiled-coil"
FT                   /evidence="ECO:0000259|Pfam:PF18035"
FT   REGION          195..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   216 AA;  24708 MW;  EF2E886D93F2E476 CRC64;
     MTLYYSLVFL LLVFEMAVFL ALVIPLPHTI KRKLFAFISE SPIIAKLQYG LKITFIFILI
     LFLDSVNRVY RVQQELSAFT KDGPGMGAAH LGTDRMEVQA RKFYSQRNMY LCGFTLFLSL
     ILNRTYTMIL ETLRLEDRVR LLEGDKKAGG KDSARIAEAG SVGEIGRLKE LVETKDRDIE
     TLKKQCEGLT REYHSLGDQI SNEKGDKNEK KDKKDL
//
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