ID G8JMM1_ERECY Unreviewed; 412 AA.
AC G8JMM1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 03-MAY-2023, entry version 40.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN OrderedLocusNames=Ecym_1122 {ECO:0000313|EMBL:AET37376.1};
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:AET37376.1, 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|RuleBase:RU365011}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000256|RuleBase:RU365011}.
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DR EMBL; CP002497; AET37376.1; -; Genomic_DNA.
DR RefSeq; XP_003644193.1; XM_003644145.1.
DR AlphaFoldDB; G8JMM1; -.
DR STRING; 931890.G8JMM1; -.
DR GeneID; 11472560; -.
DR KEGG; erc:Ecym_1122; -.
DR eggNOG; ENOG502QQNH; Eukaryota.
DR HOGENOM; CLU_015737_1_2_1; -.
DR InParanoid; G8JMM1; -.
DR OMA; FWSVFRL; -.
DR OrthoDB; 2718971at2759; -.
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 PANTHER; PTHR11440:SF97; BCDNA.GH02384; 1.
DR PANTHER; PTHR11440; LECITHIN-CHOLESTEROL ACYLTRANSFERASE-RELATED; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU365011};
KW Hydrolase {ECO:0000256|RuleBase:RU365011};
KW Membrane {ECO:0000256|RuleBase:RU365011};
KW Protein transport {ECO:0000256|RuleBase:RU365011};
KW Reference proteome {ECO:0000313|Proteomes:UP000006790};
KW Transport {ECO:0000256|RuleBase:RU365011}.
SQ SEQUENCE 412 AA; 46585 MW; A56133E0A6F882E4 CRC64;
MLPQDLKPLC HEQLTSKEGA NGKMAAALEY IGYFSPISAY LSFHKHAITT IKSFWSVQDE
QEILYNGSYD GALSQPNEQE LILDSFPPLK DYTAPKYPIV LCHGLSGFDK LILIPSIRQL
LGLLQITVKE QNSDTFMQEA TNDSGLLALD YWVGVQKFLE SKGCTVITAK VPSFGSIEER
AAVLNDFIEK GVEKLVEKGD TGNNNDRMTA DKKVKVNLIA HSMGGLDCRY LISKKANKGY
QVMSLTTINT PHHGSEMADF VVEKFDLLKQ TAKLDELPLF LPPAFYQLTT YHMKYFNSMT
SNDPNVSYFS YGSYFYPKWY NVFYPSWNVI LNRSNGEPND GLVTVKSAKW GQYMGALKNI
DHLDIINWRN KLQLESLTSL DKTYKRKAVS TSKLDVLEFY LAITDMLTRK GL
//
