ID A0A074XWZ1_AURPU Unreviewed; 1034 AA.
AC A0A074XWZ1;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|ARBA:ARBA00015856, ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=M438DRAFT_269048 {ECO:0000313|EMBL:KEQ86472.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ86472.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ86472.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ86472.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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|ARBA:ARBA00003496,
CC 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; KL584978; KEQ86472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XWZ1; -.
DR STRING; 1043002.A0A074XWZ1; -.
DR HOGENOM; CLU_006103_0_0_1; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000030706; 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:UP000030706};
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 677..696
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 717..738
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 776..809
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 829..850
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 856..874
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 895..914
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 934..951
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 963..980
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 986..1003
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 1010..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 115289 MW; 451AF94B92624B6D CRC64;
MEDFYRKQRQ RARLRSPWAC SLVTMVCTAL SLLLLATIAQ SFLGRQLDPK GCNMSYMLSA
FAKYTDFDTE HTRFATKYSL YLYREAGIDQ DTRVKGIPVL FIPGNAGSYK QVRSLAAEAA
NYYHDVLQHD AQAQQDGKRP FDFFSVDFNE DITAFHGQTL LDQAEYLNEA VAYILSLYHN
PHRSLRDESL PDPKSVMLVG HSMGGIVART MFTMHNYQPN TINTIITLSA PHARAPVSFD
QDIVDTYQNI NEYWRNSYAL DQSPLDHVTL VSIVGGGLDT VVPSDYASLT SLMPESHGFT
VFTSTIPHVW TGMDHLAIIW CDQLRKAVIK ALFDVADVKQ PTQTIPREER MRHFRRRFLT
GLEPSVKKAL PEQEAKMLLS LDDQSSAILS IGERLSLRQL GSSAKTEAHV LPVPSLIEKD
TRKLSVLTNQ RIDEHGPVQV FLCSSHIPQA GAGGNAYAIN LDLSGGSSGF MRLSCKDAAS
DAIALPASTS GSAFAFDDAS PFTYIEYTLK DLSDYQYVAV IDKASELTDG WVVAEFSDSA
KSTITVKRSL RSLMLSGMHR ILPATRAMVN EIRIPRVHSS LLAYTLHIRQ KCKSEPLFQP
LLRQYISEPY ESKFFPNVRG DVNINLHGVS PYVPPPANAA HTKDGLSLQI WSDPTCNAEM
EVALDIDILG SLGKLYMRYR TVFAAFPLVV VALVLRKQFK VYDATGIFMS FSEGMDQCIR
TSLPVLFIAL SFLSLALANH ATAAVGEEIL GPQHEATESF LAFTKNDLLL GSNDPFFFWL
VPLFGVISVG VCIVINYIAL AVTQIFTFCY TKIRNVRLRN DEGRRTTTAF AVTSPLQRVI
TTSILLIMVA TIIPYQFAYL VLCLVQLATS VRALRLAQET RSGNNYNFYN YVHSLLVLML
WILPINLPVL VVWIHNLAVH WLTPFSSHHN ILSIMPYILI VETMSTGHII PRLSSPWKLV
NNIMLFALAL YAAIYGVSYA YVLHHLVNGV CAWLVIVHFA PVLRKRGSGM EAEQRGAGSP
PPGPPQDGHV KKIP
//
