ID Q6BPC6_DEBHA Unreviewed; 391 AA.
AC Q6BPC6;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN OrderedLocusNames=DEHA2E14718g {ECO:0000313|EMBL:CAG88190.1};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88190.1, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAG88190.1, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382137; CAG88190.1; -; Genomic_DNA.
DR RefSeq; XP_459944.1; XM_459944.1.
DR AlphaFoldDB; Q6BPC6; -.
DR STRING; 284592.Q6BPC6; -.
DR ESTHER; debha-q6bpc6; PGAP1.
DR GeneID; 2902239; -.
DR KEGG; dha:DEHA2E14718g; -.
DR VEuPathDB; FungiDB:DEHA2E14718g; -.
DR eggNOG; ENOG502QQNH; Eukaryota.
DR HOGENOM; CLU_015737_1_2_1; -.
DR InParanoid; Q6BPC6; -.
DR OMA; FWSVFRL; -.
DR OrthoDB; 2718971at2759; -.
DR Proteomes; UP000000599; Chromosome E.
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:UP000000599};
KW Transport {ECO:0000256|RuleBase:RU365011}.
SQ SEQUENCE 391 AA; 45189 MW; 5FC297668E45585C CRC64;
MRIRYSCLRR PNSHAIGIIR FKPKFAIRFY SEPPKKTDHG GNKVIDLQEK KKEPIISDKF
STLKEKYEIP RYPIVLCHGF SGFDKLTFMH KPKFHNRLHQ ASEKVKKTID DGLLNIDYWY
GIKEALENIG STVLIAKVPP FGTIKERANH LNDFINRECD ELRKSESKSS IYSNMSNKSK
DDVSENATFE ETNKPIKVNL IAHSMGGLDS RYLISKLKHT NYQVVSLTTI STPHHGSECA
DFIVKFLKNR NHLSRVCPKS VHELTTKSLV EFNQKVKDDP NVSYFSYGAR FNPKWFSVFK
LTWEIMKYEM QLRDKTKPGL DRIDNDGIVS VESAKWGKYI GTLDDVDHLD LINWTNKLRN
AIDSTFFHPT SKFNAIALYL DIAENLSKRG F
//