BST1_COCIM
ID BST1_COCIM Reviewed; 1150 AA.
AC Q1DWP9; J3KFS3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
GN Name=BST1; ORFNames=CIMG_05264;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704914; EAS34240.3; -; Genomic_DNA.
DR RefSeq; XP_001245823.1; XM_001245822.2.
DR AlphaFoldDB; Q1DWP9; -.
DR STRING; 246410.Q1DWP9; -.
DR ESTHER; cocim-bst1; PGAP1.
DR EnsemblFungi; EAS34240; EAS34240; CIMG_05264.
DR GeneID; 4565227; -.
DR KEGG; cim:CIMG_05264; -.
DR VEuPathDB; FungiDB:CIMG_05264; -.
DR InParanoid; Q1DWP9; -.
DR OMA; LLVWAHN; -.
DR OrthoDB; 438490at2759; -.
DR Proteomes; UP000001261; 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..1150
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277635"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..810
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 829..849
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 890..910
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 960..980
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1010..1030
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1047..1067
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1079..1099
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1102..1122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 309
FT /evidence="ECO:0000250"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 870
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1150 AA; 127880 MW; CE1455E130B3CE9A CRC64;
MQGRPNGASG DPNPRNDTSV TIDSDSDNGS RHRIAEVRGS SPSQIVPEKA TILNDKVKAG
PCLSTEKDLG IRKQLALSHT ESIIASNPIA VMPLESPKQR LAMESSTESH RLRRARTRNP
WICSGLVLFV TVSALLILSI IVYSYQSLQV DPQGCRTPSM RPTYIKLVGF DSEHTRFASK
YGLYLYRERG VDEYSEEDIG IKGVPVLFLP GNAGSYKQGR SLASEASLYF HDVLQYHQER
LKTGVRGLDF FMADFNEDMA AFHGQTLLDQ AEYVNDALAY ILSLYHDPRR PGRDLNLPDP
TSVILIGHSM GGIVARTVLT MSNYQTNSVN TIITMSTPHA RPPVSFDSDL VHTYKQVNNY
WREAYSQKWA NNNPLWHVTL ISIAGGGGDT IVPSDYTSLS SLVPETHGFT VFTTTIPNVW
TGMDHLSIAW CDSFRKVIIR SLFDVIDVRR SSQTKQRADR MSVFKKWYLT GMEVSAERKL
PRKEHTTLLT LGDDTKSKSI LRQDEKLTLR GFGHRKGPKS HLMPIPPRGG VPEKKLTLLT
DQKLNSMETN RKLDVLFCSD FPLRAGQSAT LPSLNLDLSG GSASSIRLVC KSAAEDVISL
PTSTSSSKFA FDNVPSLSYL QYDLEDLTEY QFVVVIDKAE TRYPGWLHAE FSDSSDSVIP
TRVGLGRLLS AGLNIRLPAE RPMVIDIKVP ALHSSLLAYK LHVESKDCDG TELFKPMVRQ
YISGPYESKF FVNVRDAEIN LHGIAPYMPP HIGDNAAATG ISFQLWSDAS CNGPLQLSLK
VDVLGSMGKL AMRYRTVFAA FPLLVVSLVL RQQFKVYNQT GIFISFMQAL DLCIRSSIPL
LFLGLTFLAS SLATSKNTLS KSASPNAGSN STESVIDFSA NDLLLGSQDA FFWFLVPLFG
IISIGTCVIV NYVAMILIHA LGAIRAILMS RKGYIKHDER GNTSIFWSLS TKNRVINTAV
LLLFVATFIP YQFAYVVACV VQLVTCVQAS WHARETRSAS HSSFYNYVHS IFILMIWILP
INVLVLIVWI HDLAVHWLTP FSSNHNVFSI LPFMLLVETL TCGTMIPRIT THLRHITYVL
FFFLAAYSAI YGVTYAYLLH HITNLVIAWL VGIHFFAGGF SLRNLSRVIN DSDGVPNGSP
ITDGHIKKLP
