ID   BST1_ASPFU              Reviewed;        1156 AA.
AC   Q4WGM4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=GPI inositol-deacylase;
DE            EC=3.1.-.-;
GN   Name=bst1; ORFNames=AFUA_7G05540;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC       {ECO:0000305}.
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DR   EMBL; AAHF01000009; EAL86917.1; -; Genomic_DNA.
DR   RefSeq; XP_748955.1; XM_743862.1.
DR   AlphaFoldDB; Q4WGM4; -.
DR   STRING; 746128.CADAFUBP00008859; -.
DR   ESTHER; aspfu-q4wgm4; PGAP1.
DR   EnsemblFungi; EAL86917; EAL86917; AFUA_7G05540.
DR   GeneID; 3506265; -.
DR   KEGG; afm:AFUA_7G05540; -.
DR   VEuPathDB; FungiDB:Afu7g05540; -.
DR   eggNOG; KOG3724; Eukaryota.
DR   HOGENOM; CLU_006103_1_0_1; -.
DR   InParanoid; Q4WGM4; -.
DR   OMA; LLVWAHN; -.
DR   OrthoDB; 438490at2759; -.
DR   Proteomes; UP000002530; Chromosome 7.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050185; F:phosphatidylinositol deacylase activity; IBA:GO_Central.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006505; P:GPI anchor metabolic process; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR012908; PGAP1-like.
DR   InterPro; IPR039529; PGAP1/BST1.
DR   PANTHER; PTHR15495; PTHR15495; 1.
DR   Pfam; PF07819; PGAP1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW   Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..1156
FT                   /note="GPI inositol-deacylase"
FT                   /id="PRO_0000277629"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        797..817
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        845..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        897..917
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        966..986
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1016..1036
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1053..1073
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1081..1101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1102..1122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        877
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1009
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1156 AA;  128763 MW;  0D7B77632C5AA415 CRC64;
     MHRRSSGSPV EDDAEDSPLV SRSPTESTAH GPNNNAFETA EKSRSQIAKR GTSFDLRRDN
     GASTPRSRNS GLWRTPSSSS TSSTTAMATA STETKSSSAS FLMPLASQRL PMGTSPESSR
     FRSSRLRSPW TCSILTALTT LVASVFLFFI VRSFSARQAG EDGCGIPVMS PTFLHMVGFD
     TEHTRFASKY NLYLYREEGV DFYNQENLGL NGAPVLFLPG NAGSYRQVRS LAAEASRHFH
     DVVRHDQERI KAGTRSLDFF MIDFNEDMAA FHGQTLLDQA EYVNEAIAYI LSLYHDPKRS
     RRDPELPDPS SVILIGHSMG GIVARTALTM SNYQANSVNT IVTMSAPHAK PPVSFDSDIV
     HTYKQINDYW REAYSQTWAN NNPLWHVTLI SIAGGSRDTV VPSDYASISS LVPETHGFTV
     FTSSIPDVWI GVDHLSITWC DQFRKAIIKS LFDIIDVRRA SQTKPRAERM RIFKKWYLTG
     LEPVAERTLS QKEPNTLLTL EDKSNSILPQ GQRLILRELG HRSGPKVYLL PVPPQGVSGK
     KFTLLTDQRF DKTGEHGNLE VLFCSVFPLQ NGKFATVFSM NMDFSGGNTG STRLACKNAA
     EDGIHLPAST PASKYPFDRV QPFSYLQYEL EDLSEHQFVA IVDKADSPTK GWVLAEFSDS
     SDAVIRVRGG LGGLLSAGLK MRLPANRPML TEIKIPALHS SLLDYKLQIV RHNHDKRQEL
     FAPLLRQSIS DPHESKFFVN VDKVDVNLHG VAPFMPPPLR EQATLGGVSF QLWTDPSCGS
     TVDVSLKVDI AGSLGELVMR YRTVFAAFPL LVVALVLRKQ FQMYDETGYF ITFAEGLDTA
     LRSSFPILLL AMSLLASSLA TSAQIPPSDE PFQWPVNATE TPIDFTKNDL LLGSQDAFFW
     FLVPVFGLIS VGVCVILNYI ALILLSVLSF IYGCLRTRSG YIKRNEKGTP IFSAPTARRR
     MINTAILLVL VSTLIPYQFA YMVACIVQLA TCVRAQWHAK ETRSTAHYNF SNYAHSIFIL
     MLWILPINIL VLLVWAHNLV VHWFMPFSSH HNVLSIMPFI LLVETMTSGA MIPRVTTRLK
     HVTSMILFAI AVYSAVYGVS YAYLLHHLAN ILAAWFVVIY FFSSGFSLRR LWLILEGDDA
     TQGKSEPGGS HQKKKP