BST1_EMENI
ID BST1_EMENI Reviewed; 1140 AA.
AC Q5AYC8; C8V1N9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
GN Name=bst1; ORFNames=AN6702;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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=CBF71281.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAA58520.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AACD01000112; EAA58520.1; ALT_INIT; Genomic_DNA.
DR EMBL; BN001301; CBF71281.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_664306.1; XM_659214.1.
DR AlphaFoldDB; Q5AYC8; -.
DR STRING; 162425.CADANIAP00007489; -.
DR ESTHER; emeni-BST1; PGAP1.
DR EnsemblFungi; EAA58520; EAA58520; AN6702.2.
DR GeneID; 2870486; -.
DR KEGG; ani:AN6702.2; -.
DR VEuPathDB; FungiDB:AN6702; -.
DR eggNOG; KOG3724; Eukaryota.
DR HOGENOM; CLU_006103_1_0_1; -.
DR InParanoid; Q5AYC8; -.
DR OrthoDB; 438490at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0050185; F:phosphatidylinositol deacylase activity; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006505; P:GPI anchor metabolic process; IBA:GO_Central.
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..1140
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277638"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 782..802
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 882..902
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 905..925
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 952..972
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1039..1059
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1070..1090
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1094..1114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 304
FT /evidence="ECO:0000250"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1140 AA; 127346 MW; D9C6E0ABA242EED6 CRC64;
MHRRSSGSSP DADDAEDSLA SRSSEPSHGC ELPEKPLPEI ARTGTSIDLR RDTNGKSTPR
SRNSSTWRTL SSATTTWASH DPPRYPAVMI TPQRLAIEAS PDSPHRSRLA RLRSPWSCSI
LTALTTILAC VFLFSIVRSF SALQTGSDGC GVPVMSPTFL RMVGFDTEHT RFASKYNLFL
YREEGVDPYN HENLGLNGAP VLFLPGNAGS YRQVRSLAAE ASRHYAQVVQ HDQERLRAGT
RSLDFFMIDF NEDMAAFHGQ TLLDQAEYVN EAVAYILSLY HDPRRTRRDA DLPDPSSVIL
IGHSMGGIVA RTALTMANYQ ENSVNTIITM SAPHAKAPVS FDSDIVHTYK QINDYWREAY
SQTWANNNPL WHVTLISIAG GSRDTVVPSD YASISSLVPE THGFTVFTST MPDVWIGVDH
LSITWCDQFR KAIIKSLFDV VDVRRASQTK PRAERMRIFK KWYLTGLESV SERMLTRNEP
STLVTLEDHT NTILAQGQRL VLRELGHRTG PNVHLLPVPP QGVSGKKFTL LTDQRLDRTG
EQGSLEVLFC SVFPLHNGKA SSVFALNMDS SDSSGSTRLA CKNAAVDEIH LPASTRTSRN
AYDRARPFSY LQYDLEDLAE HQFVAVVDKA RVPMKGWAIA EFSDSSDALI KARIGLGGLL
SAGLKVRLPA NRPMLTEVRI PALYSSLLDY KLRVVRHHQA GDPRELFAPL LRQSIADPHE
SKFFVNVDKV NVNLHGLAPY MPPPLRQTSQ NGVSFQLWTD PTCDSTVDIT LTVDIVSSLG
ELVMRYRTVF AAFPLLVVSL TLRKQFQVYD ETGFFITFAE GLDSALRSSM PALLLAMSLL
ASSLATSTKL PTGDDPFHWA TNSTETPIDF TKNDLLLGSQ DAFFWFLVPL FGLICVGVCV
LLNYVALIVL QILSVVYGLW NSKSGYIRRD EKGYLPVFPA PSPRRRMIKM GVLLVLVSTA
IPYQFAYLVA CIVQLATCVR AQWHAKETRS TAHYNFANYA YSVFILMLWV LPINILVLLV
WAHNLVVHWF MPFSSHHNVL SIMPFIILVE TMTTGSMIPR VTTRFKHVTS VLLFCIAVYS
AVYGVSYAYI SHHLVNILAG WLVSIYFFRS GFSLHRFWKI VEGDETPSTP ESGSHMKKKP
