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Database: UniProt
Entry: A0A1V6S0R6_9EURO
LinkDB: A0A1V6S0R6_9EURO
Original site: A0A1V6S0R6_9EURO 
ID   A0A1V6S0R6_9EURO        Unreviewed;       336 AA.
AC   A0A1V6S0R6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Bax inhibitor 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENVUL_c013G04063 {ECO:0000313|EMBL:OQE07448.1};
OS   Penicillium vulpinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE07448.1, ECO:0000313|Proteomes:UP000191518};
RN   [1] {ECO:0000313|Proteomes:UP000191518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the BI1 family. {ECO:0000256|RuleBase:RU004379}.
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:OQE07448.1}.
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DR   EMBL; MDYP01000013; OQE07448.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6S0R6; -.
DR   STRING; 29845.A0A1V6S0R6; -.
DR   OrthoDB; 1703953at2759; -.
DR   Proteomes; UP000191518; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006214; Bax_inhibitor_1-related.
DR   PANTHER; PTHR23291; BAX INHIBITOR-RELATED; 1.
DR   PANTHER; PTHR23291:SF129; GROWTH HORMONE-INDUCIBLE TRANSMEMBRANE PROTEIN-RELATED; 1.
DR   Pfam; PF01027; Bax1-I; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004379};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191518};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU004379};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU004379}.
FT   TRANSMEM        81..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
FT   TRANSMEM        120..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
FT   TRANSMEM        150..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
FT   TRANSMEM        233..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
FT   TRANSMEM        271..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
SQ   SEQUENCE   336 AA;  36987 MW;  FDCD3EDBAC3C5FFE CRC64;
     MAFFLRRPFA VSSALRQVPK ITNTARFIHN SPIKPTQATK PQGVSSSIFA KSRQNFQNAF
     RRTYMQQSAN PAQGGNMTQK LVYGAAIIGG TVMATNFIFN RETREDGGMP AYERSFLNET
     FMHTGLGIGI IGVAARALHM SGWSYRLMAM NPWLVMGVGL VGSIGSMYGT FYTSPDNYVV
     KYGCWTLFNL TQAALLSPLM FMNPAILARA GLYTVGMMGS IAFVGATAKQ EKYLYLGGPL
     LAGVTIVALS GFAPMVLPAT AVRTLMWSER LWLYGGLAVF GGFTLYDVQK ILHHARLAER
     GLIKRDVVNE SVSLELDFIN IFIRMVQILG MGNNRR
//
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