ID B5VI04_YEAS6 Unreviewed; 808 AA.
AC B5VI04;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 22-FEB-2023, entry version 42.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
DE Flags: Fragment;
GN ORFNames=AWRI1631_60360 {ECO:0000313|EMBL:EDZ72445.1};
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124 {ECO:0000313|EMBL:EDZ72445.1, ECO:0000313|Proteomes:UP000008988};
RN [1] {ECO:0000313|EMBL:EDZ72445.1, ECO:0000313|Proteomes:UP000008988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631 {ECO:0000313|EMBL:EDZ72445.1,
RC ECO:0000313|Proteomes:UP000008988};
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
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|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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:EDZ72445.1}.
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DR EMBL; ABSV01000759; EDZ72445.1; -; Genomic_DNA.
DR AlphaFoldDB; B5VI04; -.
DR ESTHER; yeast-BST1; PGAP1.
DR Proteomes; UP000008988; 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: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 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 487..508
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 587..618
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 693..720
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 732..751
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 763..782
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDZ72445.1"
SQ SEQUENCE 808 AA; 92400 MW; DAA90E3BC009B7B6 CRC64;
YPHPKPQSVI IVGHSMGGIV SRVMLTLKNH VPGSISTILT LSSPHAASPV TFDGDILKLY
KNTNEYWRKQ LSQNDSFFSK NISLVSITGG ILDTTLPADY ASVEDLVSLE NGFTSFTTTI
PDVWTPIDHL AIVWCKQLRE VLARLLLESI DASKPEKVKP LNQRLQIARK LLLSGFEDYS
WMNSKLNYPQ ENLQEFSDNF FSDYATLEMN DVLDFEMFNL EKWHNNYTKI NIPSNISSTE
HLHFTLLTSL DMPMIYFCTE SRVNLSCITA VDSILTVPRS SKDTLFAADS SFGEGKNPFK
AVSVGKNILQ KYDYLMISKP TYGEFSEQEG MEDNQGFLLA LLRNVSNVQI VNTTPSQILL
FGEQLHLDGK DIEQVISFSN LWDSLLSYRL ETKIEASNEG IASEETLFQP FIRQWVYEPF
ESKWHLNIIN KSLDINMHNV APFIPLNESE PRSLQLSFFI PPGMSLEAKM TINWSLTLKM
LFIRYRLALA SFPVAFIALV LSYQFYWYNK TSEFPSFDST LGYILRKHGI LMFFTLFLAS
PVVNNKLVQR ILYLLDPVGL NYPFLLSERN MHANFYYLGI RDWFMSTIGI LFGVMTVGLL
ALVSKIFGSL EILVIFLQRK LSKKNTEVKE AFDTIEHKAY GKGRLMASVL LLLLVFFHIP
YQMAFVISLV IQIATCIRVA LLKLSNSEQK LNLLNYNMTL LLLLLFVSAI NIPIIIVFLH
NVAIKWETSF RSHHNILAVA PIIFLVGNNS IFKMPNSVPL DTWDGKVTII LFVYLTVFSF
IYGIRNLYWI HHLVNIICAW LLFFETIH
//
