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Database: UniProt
Entry: A0A0J0XFA4_9TREE
LinkDB: A0A0J0XFA4_9TREE
Original site: A0A0J0XFA4_9TREE 
ID   A0A0J0XFA4_9TREE        Unreviewed;       468 AA.
AC   A0A0J0XFA4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   RecName: Full=GPI inositol-deacylase {ECO:0000256|RuleBase:RU365011};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN   ORFNames=CC85DRAFT_323215 {ECO:0000313|EMBL:KLT39747.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT39747.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT39747.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT39747.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KQ087250; KLT39747.1; -; Genomic_DNA.
DR   RefSeq; XP_018276238.1; XM_018426225.1.
DR   AlphaFoldDB; A0A0J0XFA4; -.
DR   STRING; 879819.A0A0J0XFA4; -.
DR   GeneID; 28986828; -.
DR   OrthoDB; 5477082at2759; -.
DR   Proteomes; UP000053611; 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   Reference proteome {ECO:0000313|Proteomes:UP000053611};
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        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365011"
SQ   SEQUENCE   468 AA;  51623 MW;  AE07D0CA63D0793D CRC64;
     MGDPNKYRKS RSFQRRLTLL TSIALCALLT WVGYWSYSTD QAMSGLWGCE MAYMYPSFSP
     LEGVDTAGSR YALFLYREGG MDPPVPSGHP VIFIPGNAGS YKQARSIGAS VAAQFHKGRD
     TTWTKSVDLF TVDFNEDLSA LHAPTLRSQA QFLVKAIARV YRAYEHLPAD ERPAKVILLG
     HSMGGIVARL ASTMAQPTMW QPSPVDVILT MSTPHLQPPA PLDPEMERIY AEINSVRYSD
     PSPLLISICG GTSDVQIVSD ACALTNSLIG RDDGFAVFTT GIPGVWTGVE HQAMVWCDQV
     RYRVARTLLD MGEAASRQGK LSAAQRWLLG ISETQPALPT LDTTTRVEVV ASRMAILLKL
     TYPTEVSLVS PPVTAQFCEE EGVCSDQTFF SYSVPWLPVS ERPFPLLGEG SRPEESVFVL
     DFDLPEVNRG WLEIRHPLGA SVHSGPLVDQ TVVGSRWSEW HHRTRLNA
//
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