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BST1_DEBHA
ID   BST1_DEBHA              Reviewed;        1032 AA.
AC   Q6BRG1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=GPI inositol-deacylase;
DE            EC=3.1.-.-;
GN   Name=BST1; OrderedLocusNames=DEHA2D16632g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAG87380.2; -; Genomic_DNA.
DR   RefSeq; XP_459209.2; XM_459209.1.
DR   AlphaFoldDB; Q6BRG1; -.
DR   STRING; 4959.XP_459209.2; -.
DR   ESTHER; debha-q6brg1; PGAP1.
DR   EnsemblFungi; CAG87380; CAG87380; DEHA2D16632g.
DR   GeneID; 2901194; -.
DR   KEGG; dha:DEHA2D16632g; -.
DR   VEuPathDB; FungiDB:DEHA2D16632g; -.
DR   eggNOG; KOG3724; Eukaryota.
DR   HOGENOM; CLU_006103_0_0_1; -.
DR   InParanoid; Q6BRG1; -.
DR   OMA; LLVWAHN; -.
DR   OrthoDB; 438490at2759; -.
DR   Proteomes; UP000000599; Chromosome D.
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:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
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..1032
FT                   /note="GPI inositol-deacylase"
FT                   /id="PRO_0000277637"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        703..723
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        740..760
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        805..825
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        861..880
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        884..903
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        916..936
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        943..963
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        985..1005
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        12
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        520
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        555
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        784
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        907
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        938
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        942
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1032 AA;  117343 MW;  AB5617197B0183C9 CRC64;
     MDSKSRGKSR LNRSILTLVS FFGLVLFYLT WYLYTRGLTG ADSPGCRIVY MGPSYARITA
     FDESHTKFAS KYSLYLYREQ GRDPLPDENE GFKHLGGIPI LFIPGNAGSY RQVRSIAAET
     SDIYFDHYLD QPDGLNPNAK NYDFFTADFN EDFTAFHGRT LLDQAEYLNE AIKFILGLYA
     NSEHPPRSVV VLGHSMGGVV SRVMVSLPNY IPDSINTIIT LASPHAAAPL TFDGDILKIY
     SAVDRFWFQG YDNKETDNTI AKIAKERLSK ISLISITGGL LDSILPADYT TLGYLVPPTN
     GFTVYTTGIP GVWTPIDHLA IVWCAQLRRR VSNALLEIAN FDSPDKTYSL EKRMEIMRKN
     FLSGFEDYTS QDKVAYDKPA DHILLKADSQ QINFVQEGQK LKVTPGKMPS PLNVFRLPSP
     KVSKVQFSLL SSMDIGELKS DNNEGYTQPT LLLCNTMDAI KEDANIIDFT NKETTEIVMF
     KCIDVRDDSN MIPRSAVGTY SLSESSIGGD KSPFYAIQYN STILKQYDTV IVTGSLGMES
     NDNENFLLAE LSDYNSSQFN IHEDLFSLMT RGAKFSLPLD KPLSMNIKIP GAWSSILAYK
     LKVSWPEDRE TTEYIPVFRT FIRQWSNEPY EVKWHVNIEA NNQVLLNMHG IAPYTPFKVK
     SKEEYGLNIE IWTDSIPDKS LTTIRLRIDL LNSLRLLVLR YRLATISFCV SIILLALVFQ
     VKHYKETNKF PTFLYGLSCI CSPWVFGSIL FTLSILTPIM SIKPLQKFLN VIDPVVLQDS
     NEINLSLTDE FKLNSFFLGL EEKSLWFIGP VFFVMGLGIV SLTFYSLLVA GNVIASISRV
     LLKRLKLSQT EKKQPNPGKL WANRRIIGVL FVLLVIPIYM PYQFAYVVSC IIQSIQVIKI
     LVADKTNKSI LNYHLSLLML MLWVLPINVP ILVVFVHNMT INWTTPFSSH HNFLAILPVI
     LLMERYSNSR TLPKMSQTKY KVTQAFLAYY VFYCLVYGIR HTYWIHHLFN LLCCWLLVLH
     YDAQDDTSDH VQ
 
 
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