BST1A_YARLI
ID BST1A_YARLI Reviewed; 1076 AA.
AC Q6C2Z2;
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 A;
DE EC=3.1.-.-;
GN Name=BST1A; OrderedLocusNames=YALI0F03927g;
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; CAG77777.1; -; Genomic_DNA.
DR RefSeq; XP_504970.1; XM_504970.1.
DR AlphaFoldDB; Q6C2Z2; -.
DR STRING; 4952.CAG77777; -.
DR ESTHER; yarli-q6c2z2; PGAP1.
DR EnsemblFungi; CAG77777; CAG77777; YALI0_F03927g.
DR GeneID; 2907718; -.
DR KEGG; yli:YALI0F03927g; -.
DR VEuPathDB; FungiDB:YALI0_F03927g; -.
DR HOGENOM; CLU_006103_0_0_1; -.
DR InParanoid; Q6C2Z2; -.
DR OMA; LLVWAHN; -.
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..1076
FT /note="GPI inositol-deacylase A"
FT /id="PRO_0000277644"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 765..785
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 815..835
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 855..875
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 910..930
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 970..990
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1006..1026
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1035..1055
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 240
FT /evidence="ECO:0000250"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 849
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 952
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1076 AA; 118703 MW; AE4942AFE6CC8FFB CRC64;
MHIATFPALA ITALALVLWA TVATHSSNTN SCHMSYMKPD MIAMTGFNTT QTPLAHKYSL
HLYRELDVDL SREVGGRPVL FVPGNGGSMR QIRSIAGEAA VQYWHDPRRA GADADTWANG
STARPKSALQ KLNTFAFGDT ESDTEGVRGL GDAVTARDMS GDDRRDAVER PLSNGKLPSQ
WPDDLPLDFF TVNFQEDLTA FDGTTVIDQA EYLNQAIAYI LSLYSSHPNP PTSVIVIGHS
MGGIVARTMV TLDSYIHGSI NTILTLATPH VLPPVSFDKG IVGLYHNVNE FWKTETVPGG
KLEDTLLVSV TGGIRDQMIP AEYSSVDTFL PPTNGFAVAT TSIPDVWMSI DHQAMVWCHQ
LRRVVAETLL VVAGETTEKV STRLDTFQEY FLSGMERVEK KAQNASESSK LTLDTLVSIN
TPLTTTSNII INDHSPNQLV KTKSYFKFPV LKASEINEMS RSFAMPVDKG KSLLVKTNMP
LEDLHILVCR TNTGDVDTNG FSFLRYGSKS KGVRVGTDTL VCANVAGEAV AMPSSIKYAT
GAKIPEEEET GEDNDIPVDS AISSTSLSEY IQLDASSLSG FQYVVVIDNT MSETISSDSY
LLAEMALPSD MAVVAAPTWW EVLKVGRFTI ELPEKRALLT KISLPHFWSS LVAFSIRLST
SDSFSMEYQC EAKKSMGSEH DVLFAPLLMQ YSAQLHEAKF STNLCGGYEQ GTRVAVHGGA
PYMPLAEGRD VSGTELYLWT DSSSRSSESL SLTLEIDLWG SLGRFLGFYR VMFAIFPMFV
FLCLLMIQLR VWTTTELFVS LSDALDVFVD FQLPWILAGS CAIPFVPHVL VSLLYPQMSQ
PGQFFLGLNG THLWFLGPVS LVIATGIVVV LHWLLQILTL WVCQCYYMLG LAPIAPESPF
SVRRIVTISF LLLLVFKIVP HQFAFMVAVL VMAMGAGKAR VGRLMQSEDK DNKSEPCVVI
DRNLINYTHS LLLLLVLLLP INAPTLVVWL HNMANKWHTP LESHHEVSAI LPILLLVLTA
SRGIMIRLPQ SKRAIYATFA FLAYFALFVL FHGVVHSYRL HLLTNGLCLC LLYLSL
