BST1_KLULA
ID BST1_KLULA Reviewed; 975 AA.
AC Q6CIN9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-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=KLLA0F25124g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98908.1; -; Genomic_DNA.
DR RefSeq; XP_456200.1; XM_456200.1.
DR AlphaFoldDB; Q6CIN9; -.
DR STRING; 28985.XP_456200.1; -.
DR ESTHER; klula-q6cin9; PGAP1.
DR EnsemblFungi; CAG98908; CAG98908; KLLA0_F25124g.
DR GeneID; 2895177; -.
DR KEGG; kla:KLLA0_F25124g; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_006103_0_0_1; -.
DR InParanoid; Q6CIN9; -.
DR OMA; LLVWAHN; -.
DR Proteomes; UP000000598; Chromosome F.
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.
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..975
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277639"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 751..771
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 818..838
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 868..888
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 932..952
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 955..975
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 210
FT /evidence="ECO:0000250"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 867
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 975 AA; 111164 MW; E459C5A744BE6202 CRC64;
MVQIDLPAES AVRIRYPTLT KKLRKRSTLV IIVGLLLLCI ITSTHISHNF SGSDTPKCRS
IYMYPSYARI DGFDSRHTKL AKKYHLYLYR EQGKDKEPKH GDEIQLDGIP VLFIPGNAGS
FKQARSIAAA SANLYFDHKS TIQNSNAKNM DYFTADFNED FTAFHGQTML DQAVYLNDAV
RYILSMYAQS AAYKESNRPL PKSVILLGHS MGGIVARLML TLPNHIPESV NTILTLSSPH
STAPVTFDGD ILKLYDRVNS YWTSAMNDMG SYFRNNVSVI SITGGILDDI LPADYTNLQG
IVPESNGFTT FTTTIPELWT PIDHLAIVWC DQLRYLLAKY ILEIVNDDAG GKTATLDIRM
RKGRKFFLSG LERITDADKL IDKNLSAPAV DFSDTESVPE NHLLVLNSSE SMSTGYAFNI
SKSVDYSFEM LTSLVQFDIF FCKDIYGKDC INGFSSFSKV PHSTSLQKFP TDSSWGESVS
PFRFISLNGS LLQGFQIIVF QGSMKKKEDF VLAKYSDDKS IETASDGLWK LSLFPFRMSL
KNKHSFVHGL AFPNLWSSLI SFNLKTTFSD EIDSMFRPMM RQYVNNPYET KWHLLAASSS
HEINMHNISP FIPLDDTIDK SLNLMFFIPP GEEISLRLSI NWKLTLKMLY IRFRLAFASI
PISIIALVLC YQFYYYDSPD SKFISFDTGL MNVLNNHSLL IFLFLSVGPI AINHKAILTL
LHYLDPISLS KPSSDSHMLN NNYMLGLRET FVWWIGPVFF IISVALLFII LRLINVIEFA
VIKISSAITR YTRITFPDPL NDMTHHKLLF NNRQLLGVCF ISLGVMVYVP YQFAFILVSL
IQMWNCMKLA VFTNRNNAKY SNIHNYNVSF LMLTIFMIPI NAPIVVVFLR NFAIRWETAF
RSHHNFLAIA PTLLLTLRNS QCNIPIIKNR MNWLIVVSIL GYLSFYSFMY GIRNLYWVYH
ISNILNGVLF FLTIL
