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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
 
 
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