BST1_CHAGB
ID BST1_CHAGB Reviewed; 1147 AA.
AC Q2H102;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
GN Name=BST1; ORFNames=CHGG_04544;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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=EAQ87925.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CH408032; EAQ87925.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001223758.1; XM_001223757.1.
DR AlphaFoldDB; Q2H102; -.
DR STRING; 38033.XP_001223758.1; -.
DR ESTHER; chagb-q2h102; PGAP1.
DR EnsemblFungi; EAQ87925; EAQ87925; CHGG_04544.
DR GeneID; 4392572; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_006103_1_0_1; -.
DR InParanoid; Q2H102; -.
DR OrthoDB; 438490at2759; -.
DR Proteomes; UP000001056; 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..1147
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277634"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 843..863
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 893..913
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 918..938
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 965..985
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1015..1035
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1052..1072
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1084..1104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /evidence="ECO:0000250"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 873
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1147 AA; 127892 MW; 63DB325F56F0F966 CRC64;
MRRHSSGSSE DDDASPVEAP HANSSRFSAK DSRSSAHPTT KLDHNRNADR PPSFSISRRS
SSINWRLPES RNGNGTVEKR PSPERTSPSS PLGLIMTANG ELRTKEVEKT PETVIPARRP
PWRSPWAITF SALVAAIVGI GFLVAVLHSS VTRQLDPKGC RMSYMRPSYA KLNEFDTEHT
RLASKYSLYL YREQDIDRDT KVRGVPVLFI PGNAGSYKQV RPIAAEAANY FHNVLQHDES
AMNAGTRNLD FFTVDFNEDI TAFHGQTLLD QAEYLNEAVR YILSLYLDPR VADRDPDLPD
PTSVIVLGHS MGGIVARTML IMPNFQSHSI NTIITMSAPH ARPPVSFDSQ SVQTYKDIND
YWRRAYSQQW ANDNPLWHVT LVSIAGGGLD TVVPSDYASV ESLVPDTHGF TVFTSTIPNV
WTSMDHQAIL WCDQFRKVVA QAIYDVVDVH RATQTKPRAE RMRVFKKWFL TGMETIAEKA
APRSEPTTLL TVDDNSDSII AEGERLVLRN LGTAGTVRAH LMPIPPSGSP GMKRFTLLTD
TKLDKPGEHG KLEVLFCSVI PSQPSQSWAG FPSQMDLSKG STGSTRLACR SAAPDVVSLP
ASTSSTQFPF YLNGEKEITP FSYLEYGVDD IAEHQFVAVV EKTTAPTPGF VVAEFSDYTQ
SHRTRHISLR SLLTFGMKFH LPAERPMVSE VKVPSLQSSL LAYNLRISHQ DCNGDSELFA
PLVRQYLAEP YESKYFVNAR EATVSLHGVA PYVPPPLTGK LDENGLSFQF WTDPTCSSSI
HIELTADFMG SLGKLYMRYR TVFAAFPLFI VALVLRKQFR VYDTTGMFIP FLEGLDLCLR
QSIPLMLASL TLLTLSTGIM APASNASFWH WRNGTSSIMD FQHNDLLIGT EDPLFLFLIP
LIAIVCVGVC TVFNYMALTL THLLGVLASL VTFHPGWIGN EDRKKTTPAA FFSPSPRRRM
ITTAVLLLLV TTMVPYQFAY LVACLVQLMT TVRAQRIASE LRSTANSNFY NYTHSIFILM
LWILPINLPT FVVWVHNLAV HWLTPFSSHH NVLSVMPFIV LVETLTTGKM IPRMGSRLKH
VTSLLLFGMA VYAAVYGVTY AYTLHYVANF LAFWLAIVHS TSDSWSLAGL THLYSGDAGI
RKRGKEP
