BST1_CANGA
ID BST1_CANGA Reviewed; 1011 AA.
AC Q6FLY9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
GN Name=BST1; OrderedLocusNames=CAGL0K12408g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR380957; CAG61718.1; -; Genomic_DNA.
DR RefSeq; XP_448755.1; XM_448755.1.
DR AlphaFoldDB; Q6FLY9; -.
DR STRING; 5478.XP_448755.1; -.
DR ESTHER; canga-q6fly9; PGAP1.
DR PRIDE; Q6FLY9; -.
DR EnsemblFungi; CAG61718; CAG61718; CAGL0K12408g.
DR GeneID; 2889984; -.
DR KEGG; cgr:CAGL0K12408g; -.
DR CGD; CAL0133825; CAGL0K12408g.
DR VEuPathDB; FungiDB:CAGL0K12408g; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_006103_0_0_1; -.
DR InParanoid; Q6FLY9; -.
DR OMA; LLVWAHN; -.
DR Proteomes; UP000002428; Chromosome K.
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; IEA:EnsemblFungi.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR GO; GO:0006505; P:GPI anchor metabolic process; IEA:EnsemblFungi.
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.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1011
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277633"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..737
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 792..812
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 847..867
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 900..920
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 964..984
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 987..1007
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 28..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 250
FT /evidence="ECO:0000250"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 837
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 898
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1011 AA; 115797 MW; 413C16BFF84A8FD5 CRC64;
MSFIRIARSL ARGYYNLPTN IIDRTSINTS RKDDDSDTKA TGSQLDSPDE EWLKDYNSFV
NVRRRNRSVL RTFVFGIGLF LIIAILTLWW PLTGADLPQC HSIYMYPSYA RVDGFNEKFT
SLANKYHLYL YREQGMDKEP LNNGEIQLDG IPVLFIPGNA GSYRQVRSIA AACSELYFKQ
SDILINKNAK NLDFFAADFN EDFTAFHGGT MLDQAEYLND AIRYILSLYD QPDVSTTLAK
PKSVIIVAHS MGGIVARLMP TLKNHIHGSV HSYLTLSSPH AAAPITFDGD VLQLYKRTNE
YWKRELNDKS SFIFNNVSLI SITGGIQDTI LPADYAMIED LIPYSNGFTV HTNTIQDVWT
PIDHLAIVWC KQLREIISRY LVETSNIYLP SKVVPLEERM KIASQLFLSG FEDSYRNYSG
EELRNLTTNS EVSSEMKLND IVKITKDTIP DKPYLSVPVA QFDGNVFLTL FSNSDNIKIL
GCANSYRHDP TIHSCKDLSH FIKKVPRYFD PNKEHKTESN KLLHTSIDEF KKYDFVIVDF
STIVEEHDLL VYATLSREEH TVIDVTPSNL LFMSQKIKVP PGALMNKWEF INLWDSLFAY
KMNVDTTAME QPFEPFVKQH IKEPFETKWH LNVLESTTSI SFHNIAPFIP TNENITRSLF
LTLVGSPEND YFIRISVDYL MTLKLLYIRY RLAIASFPIA VITMVLAYQF YIYDRRGIFL
PFVTALGHLI STYNTIICFS LLGLSFLCDM KLVQNALFAI DPSHLNKPYF NSNKDVRNNF
YLLGLRSKLL GVLVYFFFTI GTALVILLNG ILLTFQKLFT MAINLKRTNM LQNQRTNTTA
IITKWRFLAL FLIIISVSTF IPYQMAFMLA VIIQVINSLK VSSLSARTKN HQNLLNFNMS
LLLLLIFIAI IDFPIIIVFL HNVAIRCGTS FRSQHNCLAI IPILLMVNNN SLLRLPNRTK
GNKGRLVSLL GLIYLSLFSL IYGIRNLFWL HHGVNIFSMW VFYLTIFSKG S
