ID L8G9A0_PSED2 Unreviewed; 1174 AA.
AC L8G9A0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 22-FEB-2023, entry version 31.
DE RecName: Full=GPI inositol-deacylase {ECO:0000256|ARBA:ARBA00015856, ECO:0000256|RuleBase:RU365011};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU365011};
GN ORFNames=GMDG_03792 {ECO:0000313|EMBL:ELR09218.1};
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR09218.1, ECO:0000313|Proteomes:UP000011064};
RN [1] {ECO:0000313|Proteomes:UP000011064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) 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|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; GL573232; ELR09218.1; -; Genomic_DNA.
DR RefSeq; XP_012742210.1; XM_012886756.1.
DR AlphaFoldDB; L8G9A0; -.
DR STRING; 658429.L8G9A0; -.
DR VEuPathDB; FungiDB:GMDG_03792; -.
DR HOGENOM; CLU_006103_1_0_1; -.
DR InParanoid; L8G9A0; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000011064; 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:UP000011064};
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 153..172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 863..882
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 918..937
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 984..1012
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1033..1057
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1109..1129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT TRANSMEM 1135..1159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365011"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 130563 MW; 47BFE0C7489293C1 CRC64;
MRPRSPASAA EDDGDDDSDP STLAALVAPD NIITSAWEGT EVNGSGNGFR PPSRRDNGES
LDAPSRLGVN QHIRRSFESR NSIDVPDTAR SRRPSNTIWK PGEIRNGSVT KNGSAKSGLV
AVPPSEIIND GKMPPHFVAR RTKFRSPWSN SPTTFAVTLL AILSMGMIFY SFTTRQMDSK
GCRMSYMRPA FAKLKDFDTE HTRFASKYSV YLYREATVDE DTKVKGVPIL FIPGNAGSYK
QVRPIAAEAA NYFHDVLRHD ETVLKTGTRN LDFFTVDFNE EFTAFHGQAI LDQAEYLNEA
VAYILSLYHD PRQSQRDPDL PDPTSVIILG HSMGGIVART MLVMPNYQSN SINTIITMSA
PHARPPVSFD SQIVEIYENV NRYWREAYSQ QWANNNPLWH VTLISIAGGG LDTMVPSDYA
SLESLVPETH GFTVFTTTVP TVWTGMDHQA ILWCDQFRKV VIKSLYDVVD VNRAAQTKPR
AERMRMFKKR LLTGMEAFAE RTLPRKEPST LLTLEDGSNS ILQQGKSLTL RKFGRSRKPQ
AYLLPIPTNL AGTRFTLLSD QKPDEDGGNG KLEVLFCSVF PLKAGQSATL LSMNIDLSGD
KPGSARLACK NAAADVIQLP ASTRESKHPF IGQDDEPITP FSYLQYELAD IADHQFVAIV
DKATEPAPGW VVAEFSDKVV SKRVGSLSLK KLLAFGMKTK LPDTRPMVME VNIPALHSSL
LSYNLNVGNQ ACGDEGQLFT PLVRQYLSKP YESKYFVNVK QARINLHGVA PFMPPPLEPR
QGHEGISLQI WTDPTCGSSV DVSLTVDVFG SFGKLYMRYR TIIAAFPLLI VALVIGKQLS
IYNDTGIFVS FTEGMDACLR RTIPLVMLCL TIVSWVLSSS SASPVSANSS PWSWNGNVTS
PLVDFKQNEL LLGSRDPFFW FLVPLTGVIS VGICIIINYG FLLLIQICSI VYGLVHTSPA
WLGKNDKRLS SSAAFYPSST RRRLIITGIL LLLVATFIPY QFAYLVACLV QITTCTRAWR
LASDTRSAAN HHFYNYAHSV FTLMLWTIPA INLPILVVWA NNIVVQWLTP FSSHHNVLSI
MPFILLVETL TSGKMIPRVS NRLRYAMPSF FFFIAMYAAV YGVTYVYMLH HLVNIATFGL
FVIHSSCGTW SVAAVSDIFD SESSMERRKR GKTP
//
