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 24-JAN-2024, entry version 103.
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; 284592.Q6BRG1; -.
DR ESTHER; debha-q6brg1; PGAP1.
DR GlyCosmos; Q6BRG1; 7 sites, No reported glycans.
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; WVRNLAV; -.
DR OrthoDB; 5477082at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR039529; PGAP1/BST1.
DR PANTHER; PTHR15495:SF7; GPI INOSITOL-DEACYLASE; 1.
DR PANTHER; PTHR15495; NEGATIVE REGULATOR OF VESICLE FORMATION-RELATED; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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
//
