BST1_CRYNJ
ID BST1_CRYNJ Reviewed; 768 AA.
AC P0CM50; Q55R18; Q5KF48;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
GN Name=BST1; OrderedLocusNames=CNF03000;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
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; AE017346; AAW44289.1; -; Genomic_DNA.
DR RefSeq; XP_571596.1; XM_571596.1.
DR AlphaFoldDB; P0CM50; -.
DR SMR; P0CM50; -.
DR STRING; 5207.AAW44289; -.
DR ESTHER; cryne-q5kf48; PGAP1.
DR PaxDb; P0CM50; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_020685_0_0_1; -.
DR InParanoid; P0CM50; -.
DR OMA; ISTCAIF; -.
DR OrthoDB; 438490at2759; -.
DR Proteomes; UP000002149; Chromosome 6.
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.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..768
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277636"
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; 86716 MW; 1097BBB9338D92C8 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 SCMASRVGYC GSSVSIIRFY QHRSVRTCKG FKLILVGEIL PWNSALERIA
RRRMPICIVL LLLGATIQSQ LPDFPMLHTF FLGVNQLEMV PLVGILGVWT FGLLCVVSFH
LISTCAIFTT LLIPFKILHV AIWSRNIWTG SAALVSTDNN FYYAIPPVLL VKCASCGGTI
QKRHVCLKAC RIALIILIMS SFSVGARWTW ILSPIANAVL ILFVASII
