BST1B_YARLI
ID BST1B_YARLI Reviewed; 955 AA.
AC Q6BZU7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=GPI inositol-deacylase B;
DE EC=3.1.-.-;
GN Name=BST1B; OrderedLocusNames=YALI0F30767g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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}.
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DR EMBL; CR382132; CAG78878.1; -; Genomic_DNA.
DR RefSeq; XP_506065.1; XM_506065.1.
DR AlphaFoldDB; Q6BZU7; -.
DR STRING; 4952.CAG78878; -.
DR ESTHER; yarli-BST1B; PGAP1.
DR EnsemblFungi; CAG78878; CAG78878; YALI0_F30767g.
DR GeneID; 2907924; -.
DR KEGG; yli:YALI0F30767g; -.
DR VEuPathDB; FungiDB:YALI0_F30767g; -.
DR HOGENOM; CLU_006103_0_0_1; -.
DR InParanoid; Q6BZU7; -.
DR Proteomes; UP000001300; Chromosome F.
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.
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..955
FT /note="GPI inositol-deacylase B"
FT /id="PRO_0000277645"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 772..792
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 840..860
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 870..890
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 919..939
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 180
FT /evidence="ECO:0000250"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 753
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 955 AA; 106313 MW; D7EAE83099C3F357 CRC64;
MRRININASV ALWTVFTILT IWISFALHQP DVQTCDIART WISTAHVEGF DSKHSRFGEK
YSLHLIRASQ HAIPQPIRPS GVPVIFVHGN AGGFRQIGPF AGIAQELNDE LRLLTKGDAG
TEFDFFSIDF NEAYSALHGR TLLDQAEYLN DAIAYILDMY KRNQQEGLQV PESVIVLGHS
MGGIVSRVAV TLENYRPQSV NTIITLASPH LIPAATFDAD ITKVYHLVND YWRAAFAEGD
TNDNPLRDIT ILSIAGGKSD TMVPSDYVSL DSLVPATNGL STFTNSIARV WTGIDHDAVM
WCHQLRRQIA SALFHIVDPN VPSQTKPREV RMSTFHRSFS GSQSLSSAMQ DFINIEATPL
QDGVEQRLAP GFYWGRNLQM LTNHVINYDS NIDLYERKSG SLLKVWQCRS RQGSSFRQCK
RIYPLFVPGI NDSVLSHVSV NGILLLDVSK EASESGDWIN IDETSMSAAP FNIYGNIVFS
TSNMVSQDIA FPALTSGLIS YKVLTSGGVG LIRQYMGRNH PSRTYDSKYL IPHYARVDIS
FHGDGAPFVP FKLKTPTKTD LSTKSYKAPL HLQVFGQGKV TISVDYVGSL GNLFMRYRTL
LFSLPTAVLY AVLLLQFWRY YQSGSDAKFL SLRDATGLFI KQYLSWACLV VAGLSFVIKF
EFIRDFLHFI QIPATGSSKS YEIETFYGSL YTHIDLFLGI SGPIGVVLAP AFLALATGIV
VVVTEIVIAV TTLASLAISR GHRKMSLLQT PKNVTIQSSD DPIGDLLHKR TVIIALMALL
VLLFVPYQLA FALATASLLA LTAYFDAEES ASASHDLSTS LYANRQAQEK VGSFINYATT
MSVVMVWTTL VNIPVLAVWV QGMVFGRSTI FSSHHNLLSV LPTLLFIENL SFRRMPERGL
PFVTYIILGY ACFNCTAYGM MHAFMIHHWF NLLAGWLLIT SYKRNKTVIK ESRIE
