ID A0A1V6TI59_9EURO Unreviewed; 1119 AA.
AC A0A1V6TI59;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|ARBA:ARBA00015856, ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=PENFLA_c007G02279 {ECO:0000313|EMBL:OQE26038.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE26038.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
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 inositol deacylation of GPI-anchored proteins
CC which plays important roles in the quality control and ER-associated
CC degradation of GPI-anchored proteins. {ECO:0000256|ARBA:ARBA00003496,
CC ECO:0000256|RuleBase:RU365011}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000256|ARBA:ARBA00006931, ECO:0000256|RuleBase:RU365011}.
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:OQE26038.1}.
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DR EMBL; MLQL01000007; OQE26038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6TI59; -.
DR STRING; 254877.A0A1V6TI59; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000191342; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR039529; PGAP1/BST1.
DR PANTHER; PTHR15495:SF7; GPI INOSITOL-DEACYLASE; 1.
DR PANTHER; PTHR15495; NEGATIVE REGULATOR OF VESICLE FORMATION-RELATED; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365011};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365011};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365011};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365011};
KW Reference proteome {ECO:0000313|Proteomes:UP000191342};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365011};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365011};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365011}.
FT TRANSMEM 101..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 863..882
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 927..958
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 979..1002
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1051..1070
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1076..1093
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1119 AA; 124814 MW; 391A1825885E79FA CRC64;
MHRRSSGSPV EDEDSSVSRT DDGTAIDEKS RSQIARRGTS FDLRRDGSAT PRSRNSSMWR
TPSSQPSNDT KPMPLGSPRL PMEAPAPDGR RARQSRQRSP WSCSILTAFT TCVAVAFLVS
IVSSFTGRQH GGDGCGVPMM SPTFIRMLEF DTEHTRFASK YNLFVYREEG VDPYTQDNIG
LNGVPVLFLP GNAGSYRQVR SLAAEASRHY YDVVRHDESR HAAGTRSLDF FMVDFNEDMA
AFHGQTLLDQ AEYVNEAISY ILSLYHDPRR TRRDPGLPDP SAVILVGHSM GGIVARTALT
MANYQANSVN TIITMSAPHA KPPVSFDSDI VHTYKQINDY WRDAYAQTWA NNNPLWHVTL
ISIAGGARDT VVPSDYASIS SLVPETHGFT VFTSSIPDVW IGMDHLSITW CDQFRKAIIK
SLFEIVDARR PTQTKPRAER MRVLKRWYLT GLESVAERTL PQKEANTLLT LEDNANTILA
QGQRLILREL GLQHGPDVRL LPIPPQGVSG KKFTLLTDQS LDKNGNIEVL FCSVFPLSNG
RSTNFPLNLD FSGGTVGSTR LACKSAAEDT IHLPASTRSS KHAHDRTPPF SYLQYDLEAL
AEHQFVAVVD KANVRTSGFL VAEFSDSSDA MIRAKVGLGG LLSAGLKMRL PASRPMLMEV
QIPALYSSLL DYRLKITRHP QKEELFAPLL RQSVSDPHES KFFVNVNEVS VNLHGVAPYM
PPAISEQAAL GGVSFHLWTD PTSDSTVDIS LQVDLASSLG ELVMRYRTVF AAFPLLVVAL
VLRKQFQVYD ESGYFIPFTD GLDRALRSSF PLLLVAMSLL ATSLATSKTL PQTDETLHWR
SNSTETPVDF TKNDLLLGSQ DGFFWFLVPA FGLISVGVCV LVNYLALVLV NIFSLVYGVL
HSKSGYIRRE DRGNLPIFHT PTPRRRIIHT AILLILVSTA IPYQFAYMVA CIVQLATCVR
AQWHAKETRS TSHLNFDNYA HSILILMLWI LPINVLVLLV WAHNLVVHWF MPFSSHHNVL
SIMPFLILVE TMTSGAMIPR ITTRFRHVTS MIFFCIAIYS AIYGVSYAYL LHHLTNLLAA
WFVGIYLVGN NFSPRRLWRI IDGDELPSET GSSHVKKKP
//
