BST1_ASHGO
ID BST1_ASHGO Reviewed; 1028 AA.
AC Q752Q2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
GN Name=BST1; OrderedLocusNames=AFR521W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 81.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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 -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000305}.
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DR EMBL; AE016819; AAS53892.2; -; Genomic_DNA.
DR RefSeq; NP_986068.2; NM_212204.2.
DR AlphaFoldDB; Q752Q2; -.
DR STRING; 33169.AAS53892; -.
DR ESTHER; ashgo-BST1; PGAP1.
DR EnsemblFungi; AAS53892; AAS53892; AGOS_AFR521W.
DR GeneID; 4622347; -.
DR KEGG; ago:AGOS_AFR521W; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_006103_0_0_1; -.
DR InParanoid; Q752Q2; -.
DR OMA; LLVWAHN; -.
DR Proteomes; UP000000591; Chromosome VI.
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:0006621; P:protein retention in ER lumen; IEA:EnsemblFungi.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0034368; P:protein-lipid complex remodeling; IEA:EnsemblFungi.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR GO; GO:0016050; P:vesicle organization; IEA:EnsemblFungi.
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..1028
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277628"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 799..819
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 867..887
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 915..935
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 948..968
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 979..999
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 231
FT /evidence="ECO:0000250"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1028 AA; 116993 MW; 2B84380A1DB8BB7B CRC64;
MCSVLRFQRN MASWVKRHVF TFDLGDIQEK RGSDSGSGQS RSTADRYFNA VFGLGLLLFC
IVCMAYLSPF LGSDLPQCRS VTMYPSYALV QGFDRRFSRL GRKYHLYLYR EAGKDNGFSD
DNEIHLDGIP VLFIPGNAGT YKQVRSIAAA TANLYYGEMR DALNNNNTKN LDFFTADFNE
DFTAFHGRTM LDQAEYCNDA IRYILSIYEL SDKYRASGEP LPTSVLVVGH SMGGIVARVM
TTLKNHIPQS INTILTLSSP HSTAPATFDG DILKIYNAMN AFWESKFRDR DKDPFYAENV
SVISITGGVL DSVLPADYTS LEGIIPSDNG FTTYTTTIPW VWTPIDHLAI VWCDQLRIVV
AKLLLELVDR TSASKTRPLP DRMRLARRSL LSGLESSASA DFHLWDNEDY IFQPKVAPGA
LTTAQEMSPI LLNVETYDTL NEYNYLAIPH NEPNLRFSLL TSLENLEELH ILFCQNYNEH
NSNGPIEYSS RCVSPSQDFI HVPRSFENSK YPSESSVGSA SLPFKALHFN QTLLSKYDFI
KFRKPSKSSF KDEDFVLVEL STTDWQTTVN CNPFQLLLSS AKFAHNASSA PFIQTFRFPY
LSSSLVSYKL DVSYTGENLV FEPFIAQSID SPFETKWHLR LRDSVTITIH SEAPFIPFES
HYDKSVKLRL IAPPDCNINL SLSINWYMTL KFLFIRYRLA VAALPLSLVS FVLANQFALY
YSSSFFPDFS TTLRAVTSKF WLKLTLSSIL LTPILNISFI QRLIHSLDPS GVNSPFLIRK
KNIMTAAYYL GIREIFMCWI GPLLSCITLS LVYMLAFGIS TLESCVRRVS CYMSTAISKT
RMKEIWLKDE CEYEEGLVLR RRIGSGIMIL AVVLYVPYQL VFVLLFLVQL NTVIKLNINY
FNTKRHSNLR NYNSSYLLLM LCVLPINAPM VFVFLHNFGR RWVTSFRSHH NCLAILPIIL
LVCDNAGLRI PRSHCIERIS KLITIGSFLY LSLYSVIYGI RNLFWAHHLV NLISGWLLFT
SLDLTSNN
