ID G8JMH4_ERECY Unreviewed; 1037 AA.
AC G8JMH4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 03-MAY-2023, entry version 43.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN OrderedLocusNames=Ecym_1465 {ECO:0000313|EMBL:AET37691.1};
OS Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS NRRL Y-17582) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=931890 {ECO:0000313|EMBL:AET37691.1, ECO:0000313|Proteomes:UP000006790};
RN [1] {ECO:0000313|Proteomes:UP000006790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC {ECO:0000313|Proteomes:UP000006790};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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}.
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DR EMBL; CP002497; AET37691.1; -; Genomic_DNA.
DR RefSeq; XP_003644508.1; XM_003644460.1.
DR AlphaFoldDB; G8JMH4; -.
DR STRING; 931890.G8JMH4; -.
DR GeneID; 11470414; -.
DR KEGG; erc:Ecym_1465; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_006103_0_0_1; -.
DR InParanoid; G8JMH4; -.
DR OMA; WVRNLAV; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000006790; Chromosome 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000006790};
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 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 708..729
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 749..776
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 820..839
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 867..884
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 890..907
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 919..944
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 956..976
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 988..1007
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
SQ SEQUENCE 1037 AA; 118019 MW; DF12261F6FF4A29C CRC64;
MKRKFRSTCQ KGAALVKRGI PIYSMVATSD DHTVDALQGP YPYVEMASTG PILRYRSKLN
FLITLGLFFI LLTTFTTMYK PFQGSNSPKC RPVMMAPSYA LIKGFDKEFH RLAQKYHLYL
YREQGRDKGP SIDNEIHLDG IPVLFIPGNA GSFKQMRSLA ASAANLYYGE SRSSIVNDDA
KNLDFFGADF NEDYTAFHGR TMLDQAEYCN AAIDYILELY KRSSAYKKSG EPLPQSVIVV
GHSMGGVVAR VMTTLKNHIP ESINTIFTLS SPHSTAPATF DGDILKIYEQ LNSFWRNKFN
TGDYFYVNNM SVVSITGGIL DSILPADYTS ISSIIPEQNG FTTYSTTIPG VWTPVDHLAI
VWCDQLRTVL AKLLIEMVDS KSASKTHPLA KRMELARRYL LSGLEDSYEQ GFNAWGPLIA
ENVKPIQIDN FKEIEMNVPL TINKSNHDAI SEYSVFKIHE STGNKTFSIL TSFSNTEVFF
CKTVKLQNDI TYQIGNRMYN CTSMSEYMIS VPRSFKGSLY PTESSVGSGN NPFKLLHTND
TILSSYNLVV VQKPPLNDIR ESDFIVAELS TRKSVETFNK NLFQLLFSPL KINHVASDFS
FIFAIRFPRM TSSLVSYVMS IEYDNKNLVF EPLLSQSVAK TFETKWHLDL QHPVDISFYS
DAPFIPSLAT SDKSLRITLL VPPLTDLKIR LRINWFMTLK LLFTRYRLAI LTLPTVLISL
VLCCQFFIYN KSGDFMSFDL ALHFLVRKYW GYLMTVSIFL TPLMNVSMVQ KLLLLLDPIR
YSHQLQLSNK QIISSIYYLG VNEVFMCWLG PMLLTMSLTL VYLLYALIAV VDFVLNKGYN
KIIQRSLRDG VKKFLMVDDE INKKFEIRHY IGFIIVTFSV LFYIPYQVAY VLLTLLQVTT
CIRLSQIDRG LKKYANLKNY NLSLLLLLLL VLPVNIPVVV VFLHNLAVDW ETPFTSHHNF
LAILPLIFLI AANTSFRMPA RYKANSRGLI TVGGLLYLSI FTLIYGIRTL YWVHHLVNAF
AGWLFLISLD NISPSDR
//
