BST1_ASPTN
ID BST1_ASPTN Reviewed; 1160 AA.
AC Q0CIV4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
GN Name=bst1; ORFNames=ATEG_06380;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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=EAU32924.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476602; EAU32924.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001215558.1; XM_001215558.1.
DR AlphaFoldDB; Q0CIV4; -.
DR STRING; 341663.Q0CIV4; -.
DR ESTHER; asptn-bst1; PGAP1.
DR EnsemblFungi; EAU32924; EAU32924; ATEG_06380.
DR GeneID; 4322443; -.
DR eggNOG; KOG3724; Eukaryota.
DR OrthoDB; 438490at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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..1160
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277631"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 786..806
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 832..852
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 886..906
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 973..993
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1023..1043
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1060..1080
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1092..1112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1115..1135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..92
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 60..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 307
FT /evidence="ECO:0000250"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1019
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1160 AA; 129500 MW; B5906957D6A598CE CRC64;
MHRRSSGSPV EDDAEDPLIS RTPSEPSGPN AVEPSERARP QVARTGTSFD LRRDHTGAST
PRSRNSSTWR MPSSATTTLL PPDPRSSSAA MPLTSQRLLA EASPDAQSRS RPARLRSPWP
CSILTALTSL LASLFLCAIL RSFAARQTGG DGCGIPVMSP AFLHMAGFDT EHTRFASKYN
LYLYREQGVD PFNHENLGLN GAPVLFLPGN AGSYRQVRSL AAEASRHYFE VVRHDQERLR
SGTRSLDFFM IDFNEDMAAF HGQTLLDQAE YVNEAVAYIL SLYHDPKRSR RDPELPDPSS
VIIIGHSMGG IVARTTLTMS NYQANSVNTI ITMSAPHAKP PVSFESDVVH TYKQINDYWR
EAYSQTWANN NPLWHVTLIS IAGGSRDTVV PSDYASISSL VPETHGFTVF TSTIPDVWIG
MDHLSITWCD QFRKAIIKSL FEIVDVRRAS QTKPRAERMR VFKKWYLTGL EPIAERTLSQ
KEPNTLLTLE DQSNTILPQG QRLILRELGH RRSPNVHLLP VPPQGVAGKK FTLLTNQRFD
KSGEQGTLEV LFCSVFPLQN GKFSTVFTMN MDFSGGNVGS TRLACKNAAE DAIHLPASTH
FSKHPYDRAE PFSYLQYDLE DLAEHQFVAV VDKAQSPTKG WLLAEFSDSS DAVIRARLGL
GGLLSAGLKM RLPANRPMLT EVKIPALYSS LLDYNLKIVR RNHGNQQELF TPLLRQSIPD
PHESKFFVNV KDVNVNLHGV APFMPPPLRE QAAVGGVSFQ LWTDPSCDST VDISLHVDIA
SSLGELVMRY RTVFAAFPIL VVALVLRKQF QVYDQTGYFI TFTEGLDSAL RSSLPMLLLA
MSLLASSLAT SSRLPPSDDP FHWPLNSTES PIDFTKNDLL LGSQDAFFWF LVPLFGLICV
GVCVILNYIA LALLSVLAFF YGIFKSKSGY IKRDDKRLVP GFHSTSVTVT NEASNLPIFS
APTPRKRMIN TAILLLLVST TIPYQFAYLV ACIVHLATCV RAQWHAKETK STTHYNFFNY
THSIFILMLW ILPINILVLL VWAHNLVVHW FMPFSSHHNV LSIMPFILLV EAMTTGTMIP
RVTTRFKYIT SLILFSIAIY AAVYGVSYAY LLHHLANIFA AWLVGVYFFS SGFSVRRLWR
VLEGDEGTSN SEPGSMKKKP
