BST1_YEAST
ID BST1_YEAST Reviewed; 1029 AA.
AC P43571; D6VTK5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
DE AltName: Full=Bypass of SEC30 protein 1;
GN Name=BST1; OrderedLocusNames=YFL025C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND GLYCOSYLATION.
RX PubMed=8862519; DOI=10.1091/mbc.7.7.1043;
RA Elrod-Erickson M.J., Kaiser C.A.;
RT "Genes that control the fidelity of endoplasmic reticulum to Golgi
RT transport identified as suppressors of vesicle budding mutations.";
RL Mol. Biol. Cell 7:1043-1058(1996).
RN [4]
RP FUNCTION.
RX PubMed=11673477; DOI=10.1083/jcb.200106123;
RA Vashist S., Kim W., Belden W.J., Spear E.D., Barlowe C., Ng D.T.W.;
RT "Distinct retrieval and retention mechanisms are required for the quality
RT control of endoplasmic reticulum protein folding.";
RL J. Cell Biol. 155:355-368(2001).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP FUNCTION.
RX PubMed=14734546; DOI=10.1074/jbc.m313755200;
RA Tanaka S., Maeda Y., Tashima Y., Kinoshita T.;
RT "Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is
RT mediated by mammalian PGAP1 and yeast Bst1p.";
RL J. Biol. Chem. 279:14256-14263(2004).
RN [7]
RP FUNCTION.
RX PubMed=16319176; DOI=10.1091/mbc.e05-05-0443;
RA Fujita M., Yoko-o T., Jigami Y.;
RT "Inositol deacylation by Bst1p is required for the quality control of
RT glycosylphosphatidylinositol-anchored proteins.";
RL Mol. Biol. Cell 17:834-850(2006).
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. Required for the transport of
CC misfolded protein to the Golgi, although dipensable for the transport
CC of many normal proteins. {ECO:0000269|PubMed:11673477,
CC ECO:0000269|PubMed:14734546, ECO:0000269|PubMed:16319176,
CC ECO:0000269|PubMed:8862519}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:8862519}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000305}.
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DR EMBL; D50617; BAA09213.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12415.1; -; Genomic_DNA.
DR PIR; S56229; S56229.
DR RefSeq; NP_116628.1; NM_001179941.1.
DR AlphaFoldDB; P43571; -.
DR BioGRID; 31121; 389.
DR DIP; DIP-7407N; -.
DR IntAct; P43571; 4.
DR MINT; P43571; -.
DR STRING; 4932.YFL025C; -.
DR ESTHER; yeast-BST1; PGAP1.
DR iPTMnet; P43571; -.
DR MaxQB; P43571; -.
DR PaxDb; P43571; -.
DR PRIDE; P43571; -.
DR EnsemblFungi; YFL025C_mRNA; YFL025C; YFL025C.
DR GeneID; 850519; -.
DR KEGG; sce:YFL025C; -.
DR SGD; S000001869; BST1.
DR VEuPathDB; FungiDB:YFL025C; -.
DR eggNOG; KOG3724; Eukaryota.
DR GeneTree; ENSGT00940000167854; -.
DR HOGENOM; CLU_006103_0_0_1; -.
DR InParanoid; P43571; -.
DR OMA; LLVWAHN; -.
DR BioCyc; YEAST:G3O-30435-MON; -.
DR PRO; PR:P43571; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43571; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
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; IGI:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0006505; P:GPI anchor metabolic process; IGI:SGD.
DR GO; GO:0006621; P:protein retention in ER lumen; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0034368; P:protein-lipid complex remodeling; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR GO; GO:0016050; P:vesicle organization; IMP:SGD.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1029
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000202676"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 708..728
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 804..824
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 872..892
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 920..940
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 957..977
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 985..1005
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1008..1028
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 236
FT /evidence="ECO:0000250"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 918
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1029 AA; 117755 MW; 10B77B212E5AD686 CRC64;
MGIRRLVSVI TRPIINKVNS SGQYSRVLAT REDQDKASPK YMNNDKIAKK PYTYRLFSIL
GILSICSLLL ISLLKPFNGA DAPQCESIYM FPSYARIDGF DERYTPLAHK YHLYLYREQS
VDREPLNGDE LQLDGIPVLF IPGNAGSFRQ CRSIASACSN IYFDSNTRAT LRNENVRNLD
FFTADFNEDF TAFHGETMLD QAEYLNDAIK YILSLYERTP DYPHPKPQSV IIVGHSMGGI
VSRVMLTLKN HVPGSISTIL TLSSPHAASP VTFDGDILKL YKNTNEYWRK QLSQNDSFFS
KNISLVSITG GILDTTLPAD YASVEDLVSL ENGFTSFTTT IPDVWTPIDH LAIVWCKQLR
EVLARLLLES IDASKPEKVK PLNQRLQIAR KLLLSGFEDY SWMNSKLNYP QENLQEFSDN
FFSDYATLEM NDVLDFEMFN LEKWHNNYTK INIPSNISST EHLHFTLLTS LDMPMIYFCT
ESRVNLSCIT AVDSILTVPR SSKDTQFAAD SSFGEAKNPF KAVSVGKNIL QKYDYLMISK
PTYGEFSEQE GMEDNQGFLL ALLRNVSNVQ IVNTTPSQIL LFGEQLHLDG KDIEQVISFS
NLWDSLLSYK LETKIEASNE GIASEETLFQ PFIRQWVYEP FESKWHLNII NKSLDINMHN
VAPFIPLNES EPRSLQLSFF IPPGMSLEAK MTINWSLTLK MLFIRYRLAL ASFPVAFIAL
VLSYQFYWYN KTSEFPSFDS TLGYILRKHG ILMFFTLFLA SPVVNNKLVQ RILYLLDPVG
LNYPFLLSER NMHANFYYLG IRDWFMSTIG ILFGVMTVGL LALVSKIFGS LEILVIFLQR
KLSKKNTEDK EAFDTIEHKA YGKGRLMASV LLLLLVFFHI PYQMAFVISL VIQIATCIRV
ALLKLSNNEQ KLNLLNYNMT LLLLLLFVSA INIPIIIVFL HNVAIKWETS FRSHHNILAV
APIIFLVGNN SIFKMPNSVP LDTWDGKVTI ILFVYLTVFS FIYGIRNLYW IHHLVNIICA
WLLFFETIH
