ID   BST1_CRYNB              Reviewed;         768 AA.
AC   P0CM51; Q55R18; Q5KF48;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=GPI inositol-deacylase;
DE            EC=3.1.-.-;
GN   Name=BST1; OrderedLocusNames=CNBF1710;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(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; AAEY01000030; EAL20361.1; -; Genomic_DNA.
DR   RefSeq; XP_775008.1; XM_769915.1.
DR   AlphaFoldDB; P0CM51; -.
DR   ESTHER; cryne-q5kf48; PGAP1.
DR   EnsemblFungi; EAL20361; EAL20361; CNBF1710.
DR   GeneID; 4936723; -.
DR   KEGG; cnb:CNBF1710; -.
DR   VEuPathDB; FungiDB:CNBF1710; -.
DR   HOGENOM; CLU_020685_0_0_1; -.
DR   Proteomes; UP000001435; Chromosome 6.
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: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; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR012908; PGAP1-like.
DR   InterPro; IPR039529; PGAP1/BST1.
DR   PANTHER; PTHR15495; PTHR15495; 2.
DR   Pfam; PF07819; PGAP1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..768
FT                   /note="GPI inositol-deacylase"
FT                   /id="PRO_0000410027"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        604..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        642..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        663..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        700..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        725..745
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        748..768
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        206
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        448
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   768 AA;  86618 MW;  2D2C21DED814F74D CRC64;
     MPAWPRFMSL RRQYLYKALD KNHQKHPIKH PHTRFLSRLF CALAVLFSYS IYQSFRTDLK
     QSGSWGCEMS WMSPSYRRLE WTEFISTRYA LYLYREQGLD SEDTLSGHPV LFVPGNAGSY
     QQVRSIASSA SKQYYEQVKA RERNVVTGKK IDFFTADLKE EFSAFHARTV REQAVFIQHC
     IKGILQEYTH LPQEKRPTQV TLLAHSMGGV VARLAMDPIT SISVDIIVTL STPHILPPLA
     LERDMDSIYS LIRWRRQHIS THPPLISICG GISDTQIVSD SCALPFFQAG NNSDIAVFTT
     GIPGVWTAVE HQAIIWCHQI RWRIARMLLD MSSRANTTAK LVTAKEWLLD YQEDETLKEP
     RSERQHDYSV SSRNMTFIGL HQPSKAFVAQ QCNGLERCRT VPSVMSLLPF PNNPSDPFPL
     PGEGIKPSEV MLVAEISLSS TNTVVKINAS QYGQTIAGSR EHHLVKGNSW SEFTITMRYR
     YIRIQLLFCI RPTHTSTFSF YCGTLLTLPR QSWHLSGDIS IALMSCTTGV AQKKLLQRTG
     QICDSVPYGR SCMASRVGCC GSSVSIIRFY QHRSVRTCKG FKLILVGEIL SWNSALERIA
     RRRMPICIVL LLLGATIQSQ LPDFPMLHTF FLGVNQLEMV PLVGILGVWT FGLLCVVSFH
     LISTCAIFTT LLIPFKILHV AIWSRNIWTG SAALVSTDNN FYYAIPPALL VKCASCGGTI
     QKRHVCLKAC RIALIILIMS SFSVGARWTW ILSPIANAVL ILFVASII