ID   BST1_CANAL              Reviewed;         390 AA.
AC   Q59VP0; A0A1D8PD71;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=GPI inositol-deacylase;
DE            EC=3.1.-.-;
GN   Name=BST1; OrderedLocusNames=CAALFM_C104190CA;
GN   ORFNames=CaO19.1053, CaO19.8655;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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   -!- MISCELLANEOUS: Lacks the C-terminal half of the classical GPI inositol-
CC       deacylases.
CC   -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC       {ECO:0000305}.
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DR   EMBL; CP017623; AOW26094.1; -; Genomic_DNA.
DR   RefSeq; XP_713657.2; XM_708564.2.
DR   AlphaFoldDB; Q59VP0; -.
DR   SMR; Q59VP0; -.
DR   STRING; 237561.Q59VP0; -.
DR   ESTHER; canal-q59vp0; PGAP1.
DR   GeneID; 3644717; -.
DR   KEGG; cal:CAALFM_C104190CA; -.
DR   CGD; CAL0000175277; BST1.
DR   VEuPathDB; FungiDB:C1_04190C_A; -.
DR   eggNOG; KOG3724; Eukaryota.
DR   HOGENOM; CLU_058462_0_0_1; -.
DR   InParanoid; Q59VP0; -.
DR   OMA; NIDFFTA; -.
DR   OrthoDB; 1057033at2759; -.
DR   PRO; PR:Q59VP0; -.
DR   Proteomes; UP000000559; Chromosome 1.
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; IMP:CGD.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0042783; P:evasion of host immune response; IMP:CGD.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:CGD.
DR   GO; GO:0006505; P:GPI anchor metabolic process; IMP:CGD.
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..390
FT                   /note="GPI inositol-deacylase"
FT                   /id="PRO_0000277632"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   390 AA;  44366 MW;  785F6E0DCE00B552 CRC64;
     MLSKRLFPYS NLFPRSRKYK FIVYFIICLT IIISALGVYL YSIPIVSPNQ PQCDMVWMSP
     SYARIRAFDE THTKYASKYN LYLYREQDVD KMPNENENED GNEGFTSLDG IPALFIHGNA
     GSFEQVRSIA ARCSEMYYND GRFKEKYPHA RNIDFFTADF NEELSAFKGL RDQVEYVTQA
     ISFIVDLYPQ NPNRNIILIG HSMGGLVARI AASRQQHESN VDIILTLATP HSDPFPWLPK
     TSDFPDEVGL ISIYSSVDLM VPPSVVTPKS KSDHFFSVDA AKLLGVPIDH QGIVWCGQLR
     EKLSEALIGI SGLNTLQDRM KVFKKIFSGD RKELGPTPIF GLAKLKLKLL QSWVHLLSLT
     IFALKWTIIV LAIIQLRKVY TKFNNPPPTH