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Database: UniProt
Entry: B6QAV1_TALMQ
LinkDB: B6QAV1_TALMQ
Original site: B6QAV1_TALMQ 
ID   B6QAV1_TALMQ            Unreviewed;       211 AA.
AC   B6QAV1;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Endoplasmic reticulum transmembrane protein {ECO:0000256|RuleBase:RU367026};
GN   ORFNames=PMAA_074020 {ECO:0000313|EMBL:EEA26329.1};
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA26329.1, ECO:0000313|Proteomes:UP000001294};
RN   [1] {ECO:0000313|Proteomes:UP000001294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC   {ECO:0000313|Proteomes:UP000001294};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; DS995900; EEA26329.1; -; Genomic_DNA.
DR   RefSeq; XP_002146876.1; XM_002146840.1.
DR   AlphaFoldDB; B6QAV1; -.
DR   VEuPathDB; FungiDB:PMAA_074020; -.
DR   HOGENOM; CLU_087648_0_1_1; -.
DR   OrthoDB; 1332764at2759; -.
DR   Proteomes; UP000001294; 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   Gene3D; 1.20.5.110; -; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001294};
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..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367026"
FT   TRANSMEM        49..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367026"
FT   TRANSMEM        108..130
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..210
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   211 AA;  24181 MW;  A392A604DCCB28F0 CRC64;
     MTLYYTLVFM LLVFEMLVFL ALIVPLPYTF KRKLFAFISE SPVVAKLQYG LRITFIFILI
     LFIDSVNRVY RVQLEMSAFS KDSTGIGAAA LGTERMEVQA RKFYSQRNMY LCGFTLFLSL
     ILNRTYIMIV EVLRLEDRIK LLEGDKKAGG KDAARIAEAG SVGEIGRLKK ELEAKDRDIE
     TLKKQAEGLQ REYHNLGDKL TESDKAPKKD R
//
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