BST1_ASPOR
ID BST1_ASPOR Reviewed; 1102 AA.
AC Q2USI0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
GN Name=bst1; ORFNames=AO090005000419;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE55485.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP007151; BAE55485.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q2USI0; -.
DR STRING; 510516.Q2USI0; -.
DR ESTHER; aspor-q2usi0; PGAP1.
DR PRIDE; Q2USI0; -.
DR EnsemblFungi; BAE55485; BAE55485; AO090005000419.
DR Proteomes; UP000006564; Chromosome 1.
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..1102
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277630"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 744..764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..810
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 867..887
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 914..934
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 964..984
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1001..1021
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1033..1053
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1056..1076
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 308
FT /evidence="ECO:0000250"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 824
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1102 AA; 122758 MW; FB720CED32C8C061 CRC64;
MHRRSSGSPV EDDAEDSLSS RIPPEPSNGP NVVDTPEKSR SQVARTGTSI DLRRDATGAS
TPRSRNSSMW RTPPSSSMTS NPPDCKSSSV MMPLASQRLP IEASPDHQRR YRPSRLRSPW
PCSILTAFTT LVASIFLFFI LRSFALRQTG GDGCGVPVMS PTFIRMVGFD TEHTRFASKY
NLYLYREGGV DPYSQENLGL NGVPVLFLPG NAGSYRQVRS LAAEASRHYY DVVRHDEDRL
NAGTRSLDFF MIDFNEDMAA FHGQTLLDQA EYVNEAVAYI LSLYHDPRRS RRDPELPDPS
AVVLVGHSMG GIVARTALTM TNYQANSVNT IVTMSAPHAK PPVSFDSDIV QTYKQINDYW
REAYSQTWAN DNPLWHVTLI SIAGGSRDTV VPSDYASISS LVPETHGFTV FTSTIPDVWI
GMDHLSITWC DQFRKAIIKS LFEVVDVRRA TQTKPRAERM RIFKKWYLTG METVAERTLP
RKGVSGKKFT LLTNQQFDKS GDHGSLEVLF CSVFPLQNGK PATAFSMNMD FSGGTSGSTR
LACKNAAEDG IHLPASTPSS KRPYDRVQPF SYLQYDLEDL AEHQFVAVVD KANSPTKGFV
LAEFSDSSDS VIRARLGLGS LLSAGLKVRL PANRPMLTEL QIPAVHSSLL DYRLKIIRKN
HGQQQELFAP LLRQSVADPH ESKFFVNVKN VNVNLHGLAP FMPPPLREQA TLGGVSFHLW
TDPSCDSTID ISLSVDIAGS LGELVMRYRT VFAAFPLLVV ALVMRKQFQV YDETGYFITF
AEGLDSALRS SLPMLLLAMS LLASSLATST KLPPTDDPFH WRTNSTESPI DFTKNDLLLG
SQDAFFWFLV PIFGLISVGV CLVINYVALA LIFLLTSIYG FLRSKSGYIR RDEKGNLPIF
SSASPRRRLV NSAILLALVS TVIPYQFAYM VACIVQLATS VRASWHAKEA KSTTHYNFAN
FAYSIFLLML WILPINALVL LVWAHNLVVH WFMPFSSHHN VLSIMPFVLL VEAMTTGTMI
PRVTTRFKHV TSMLFFFIAI YSAIYGVSYA YLLHHLTNIL AAWLVGIYFS ASGFSLSRLW
RVLEGDEAVQ NPASGSHTKK KP
