ID   BST1_PHANO              Reviewed;        1049 AA.
AC   Q0UQV6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=GPI inositol-deacylase;
DE            EC=3.1.-.-;
GN   Name=BST1; ORFNames=SNOG_05858;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445332; EAT86922.2; -; Genomic_DNA.
DR   RefSeq; XP_001796254.1; XM_001796202.1.
DR   AlphaFoldDB; Q0UQV6; -.
DR   STRING; 13684.SNOT_05858; -.
DR   ESTHER; phano-bst1; PGAP1.
DR   EnsemblFungi; SNOT_05858; SNOT_05858; SNOG_05858.
DR   GeneID; 5973131; -.
DR   KEGG; pno:SNOG_05858; -.
DR   eggNOG; KOG3724; Eukaryota.
DR   HOGENOM; CLU_006103_0_0_1; -.
DR   InParanoid; Q0UQV6; -.
DR   OrthoDB; 438490at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
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; Hydrolase; Membrane; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1049
FT                   /note="GPI inositol-deacylase"
FT                   /id="PRO_0000277641"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        699..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        742..762
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        798..818
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        867..887
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        917..937
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        944..964
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        986..1006
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1009..1029
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1049 AA;  116830 MW;  2AAAFA3EEE5AC279 CRC64;
     MVREKAQVTM GSTTMDMLED EVVKAQDRRW RLRLRNPWAC SAYTLVTTAL GFAAFFLMLQ
     SFLTKQLDTK GCEMVYMRPM YSKFDDFDTE HTRFASKYSL YLYREWGIDE EFTVKGAPVL
     FIPGNAGSYK QVRSLAAESA YHYHNSVQHE SNAGKGERRP LDFFAVDFNE DFTAFHGQTV
     LDQAEYLNDA ITFILSLYHT PGRSRRDPHL PDPTSVIIVG HSMGGVVART LFTMPNYQAN
     SINTIVTIAA PHARPPVSFD GDIVRTQNAV NSYWRSAYAQ DSAKDNPLQH VTLVSIAGGG
     LDNIVSSDYA SIASIVPETH GFTVFSSSIP NCWTGADHLA ITWCDQVRKS IVRALYDVVD
     VSQAMQTLPV TNRMRFFKKW FLTGLEDIAE KTLPMTTEAT LLTVDVDTAI LPQEEQLVLR
     SLGRSSPNIK AFLLPVPPRD RGEKIFTLLT NERLDGPGEH GRLEVLFCSM SSAQSTQSYL
     THLDFAGESP TATKLACKNA ASDVIILPES TSHSNFPFRP DQAPFSYLQY DVRDLAQHQF
     VAVLDKVAHH SAGWVVAAFS ASSEATVKVN PSLQRLLYTG ISLQLPPRRP LTTEISIPAL
     HSSLLAYDVH ISRQKCSQGE LFAPLLRQYI SDLYESKFFV NVEDAMINVH GRGRPTCRAA
     LSSKSPSNGL SLQIWADPTC DSSIDVTLKV DFLGSLGKLW MRYRIVFAAF PLLVVALVLC
     QQFRTYDATG VFISFAQSLN ECMYSSLPLA ITALTFLSIT LATAQMQSKK LQALGGPASI
     IGAFFDNDNE LLLGSEDPFF WFLVPLFGIM CTAICVMVNY VVLILTYLFA TLYALVRSNR
     LLDASGQRTP DAFAVTSTRR RIINTLILLS LISTAIPYHF AYVVLCIVQL ATCIRGFRLA
     KEAQLDTNYN FYNYAHSIFI LMLWILPINL PVLVVWIRNL AIQWLTPFSS HHNVLSITPF
     ILLVETLSTG RMVPRVRPGI SLFTNVFLFA IGAYAAVYGV TYAYVLHHLA NILCAWLVAI
     HFDTLGLAFE DSSKGVAVVG GRSEGKKRP