BST1_SCHPO
ID BST1_SCHPO Reviewed; 1142 AA.
AC Q9UT41;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
GN Name=bst1; ORFNames=SPAC824.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329670; CAB57332.1; -; Genomic_DNA.
DR PIR; T39103; T39103.
DR RefSeq; NP_593441.1; NM_001018874.2.
DR AlphaFoldDB; Q9UT41; -.
DR BioGRID; 279419; 57.
DR STRING; 4896.SPAC824.02.1; -.
DR ESTHER; schpo-BST1; PGAP1.
DR MaxQB; Q9UT41; -.
DR PaxDb; Q9UT41; -.
DR EnsemblFungi; SPAC824.02.1; SPAC824.02.1:pep; SPAC824.02.
DR GeneID; 2542981; -.
DR KEGG; spo:SPAC824.02; -.
DR PomBase; SPAC824.02; bst1.
DR VEuPathDB; FungiDB:SPAC824.02; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_006103_0_0_1; -.
DR InParanoid; Q9UT41; -.
DR OMA; LLVWAHN; -.
DR PhylomeDB; Q9UT41; -.
DR PRO; PR:Q9UT41; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050185; F:phosphatidylinositol deacylase activity; ISO:PomBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:PomBase.
DR GO; GO:0006505; P:GPI anchor metabolic process; ISO:PomBase.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IC:PomBase.
DR GO; GO:0006621; P:protein retention in ER lumen; ISO:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016050; P:vesicle organization; ISO:PomBase.
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..1142
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277642"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 741..761
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 781..801
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 849..869
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 946..966
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1006..1026
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1035..1055
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1097..1117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 24..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 264
FT /evidence="ECO:0000250"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1002
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1028
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1142 AA; 129413 MW; A550AB2916DA8C89 CRC64;
MKDDKGRSDT VNGYYISNSK LSSGFYKRNN ANTASNDEKP NLEQNDIPSV TSSGSSTPSS
ISIEKEIKIS KGNVIVKAIR SWSLYVAIIA ILLLLVILHS FQGRPQDNGC GKSYVWPSYV
RFVDFDERYT RFANKYSLYL YREKSVEESD EPSGIPILFI PGNAGSYKQV RAFAAQAAHV
YANAYAEDAD GTLNAGKLVP DFFVVDFNED FSAFHGQTLL DQAEYVNDAI PYILSLYRQN
RKISSEYDNE AFPPPTSVIL LGHSMGGIVA QATFTMKNYV DGSVNTLITL ATPHAMAPLP
FDRHLVEFYE SIKNFWSQSF LLSPEENSLD DVLLVSIAGG GLDTHVVPEY SSISTFVPPS
NGLMVFTSGI PSVWAEIDHQ AMAWCENFRR VLIRGIFAIM DARTSKCTVS LNLRKELLSR
AYIQGSSFQN DITQISKPIA QYKALDLDLT YVYSEMPGQL LFLNQLGVSY IRHHIFPIPK
PTSSIDRFEL LTDQPIDLSS SNIKVLACRL DPKIDNTISA LLENGNNKVI NANCHLLREL
VTLLPASTAY TSSPYGGDSF YNYVLPKEKM DDYHFILVSD DSKAPASGFV VGGFSNVSLD
PKTIKGSQIE LFKSGRKFQF DTKGSISKRF RFPGIQSSIM AYTISVTYEL YPGAVPQKEF
TPMLKQSIES PFETKYHVNM SNTELSVHGI SPFMEFFGKE SEKSLTLEFF LNPAIYKSVY
VSIQPSYYRS AGRLLMRYRT LLASFPVVVI SLAAYNQFRY FHYGSAYLSM SAALEVMIRK
GLIKLLFLVS ILSIAFSYLI SRVELIVADG ADPVASWKIF AMMVPKSFWK QNHLLFGLQT
AQFWFLAPLL TLMFVGLVIT ASVIILCVMH LLAFIYGIYL RYKGLTFTGV CQAVKFSFQC
LRTRNTRKLD HGEFKKLSSF LSQRNMYYAN PSLCYVYGKK HMQARIIGIM LLLLMAMTVV
PFQLVYGVAL CTQTVTTAKA LHLARFCTKS SHYRKKLWDF YNFSCTITIL MLLLAPLDFP
VLIVWARNLS MHWSIPFPTH HNFFSIIPFI LLTEILRTGK MLPRLNDVEY YINNVFLFLL
SFYSLIYGAE KPYLIHNVVG LYFFWLLFLY AKNGFFVQNI SKWPIIPRMK YFIKHKFLRS
IS
