BST1C_YARLI
ID BST1C_YARLI Reviewed; 833 AA.
AC Q6CF60;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Putative GPI inositol-deacylase C;
DE EC=3.1.-.-;
GN Name=BST1C; OrderedLocusNames=YALI0B10043g;
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 -!- MISCELLANEOUS: Lacks the C- and N-terminal parts of classical GPI
CC inositol-deacylases and may not have GPI inositol-deacylase activity.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000305}.
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DR EMBL; CR382128; CAG82947.1; -; Genomic_DNA.
DR RefSeq; XP_500702.1; XM_500702.1.
DR AlphaFoldDB; Q6CF60; -.
DR SMR; Q6CF60; -.
DR STRING; 4952.CAG82947; -.
DR ESTHER; yarli-q6cf60; PGAP1.
DR EnsemblFungi; CAG82947; CAG82947; YALI0_B10043g.
DR GeneID; 2906919; -.
DR KEGG; yli:YALI0B10043g; -.
DR VEuPathDB; FungiDB:YALI0_B10043g; -.
DR HOGENOM; CLU_006103_0_0_1; -.
DR InParanoid; Q6CF60; -.
DR OMA; VEVLFCS; -.
DR Proteomes; UP000001300; Chromosome B.
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..833
FT /note="Putative GPI inositol-deacylase C"
FT /id="PRO_0000277646"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 130
FT /evidence="ECO:0000250"
FT CARBOHYD 191
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 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 833 AA; 92665 MW; 18593DA43CE6B385 CRC64;
MWVAYSPIEG LTTEHSRLAE KYSLYLVKST PYDIPLPVRP SGVPVLFVPG NAGSYRQIRS
ISDTCRELNE QYGGSEIDFF ALDFNEAYSA LHGRTLLDQA EYLNDAINYI LQMYRDNGKD
VSSVMLLGHS MGGVVSRLAI SLDNYKPGTV TTIFTLASPH LVPPATFDGD IQKVYNRMND
FWRSNYADSD NNSLSDMTVL SIAGGKRDTM VPSDYISLDS VVPSSHGLST FSNSINRVWT
GIDHDAMMWC HQLRRQIAIA LMNVIDRDVN GRMEVFRKVF SGTQTLSDAE EDFEDVEVTP
VKHGLHQKLE SGWYYGENVQ VMTTHTVNQE SAFESYEMSS GSLLRAFECR SKSGSSFKGC
RKIFPLLVPG SNDAVIAFAE TEHYLLLDVS SSSDWISIDQ VSQKSASFDF VTGATISTSN
TISTDISFPK LTSGLVSYKV SVSKGVQLVR QYVQQNSSRV YDSKYLVPHN GVVDVSFHGD
VPFVPYFQSS PLHLQVFGGG HVTIRVDWIG SLGNLFMRYR ILFISLPSAI LYAIFLVQFH
AGTARFLSLR QSTSIFINRY LLTSCLAGSG IAYLTGLSQV RDFLHLIQIP ITKTFAVDPS
YTKNDLFLGL SGVSGTVLAP IFTVFSTGMV VLITELVMGL TSLLSFCFKS TTTAQSESES
GDPISDLLHK RTVFVAVISV LVLLFFPYQL AFTLATVALL VMTAYFKSNK APQEQSFNNY
ISTICVLMTW TCIINAPVLA VWIQGIVVQR SMTFSSHHNL VSILPTLLFV ENLSFRRIPS
GSSITSLLLA YTSLHCLFYG MMQAFMIHHG FNLLATWLLC MSYKKVFFKS KHE
