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ATG26_NEOFI
ID   ATG26_NEOFI             Reviewed;        1418 AA.
AC   A1CYS1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Sterol 3-beta-glucosyltransferase {ECO:0000305};
DE            EC=2.4.1.173 {ECO:0000305};
DE   AltName: Full=Autophagy-related protein 26 {ECO:0000250|UniProtKB:Q06321};
GN   Name=atg26 {ECO:0000250|UniProtKB:Q06321}; ORFNames=NFIA_034590;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Probable sterol 3-beta-glucosyltransferase that mediates
CC       autophagic degradation of peroxisomes (pexophagy) (By similarity). Also
CC       required for cytoplasm to vacuole transport (Cvt) and autophagic
CC       degradation of mitochondria (mitophagy) and nuclei (nucleophagy) (By
CC       similarity). {ECO:0000250|UniProtKB:Q2U0C3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sterol + UDP-alpha-D-glucose = a sterol 3-beta-D-glucoside +
CC         H(+) + UDP; Xref=Rhea:RHEA:22724, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15889, ChEBI:CHEBI:37424, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.173; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06321}.
CC       Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q2U0C3};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:Q2U0C3}.
CC   -!- DOMAIN: The GRAM and PH domains are required for the localization of
CC       ATG26 to the preautophagosomal structure (PAS) and are involved in
CC       autophagy (By similarity). {ECO:0000250|UniProtKB:Q2U0C3}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; DS027686; EAW23891.1; -; Genomic_DNA.
DR   RefSeq; XP_001265788.1; XM_001265787.1.
DR   AlphaFoldDB; A1CYS1; -.
DR   SMR; A1CYS1; -.
DR   STRING; 36630.CADNFIAP00003624; -.
DR   EnsemblFungi; EAW23891; EAW23891; NFIA_034590.
DR   GeneID; 4592869; -.
DR   KEGG; nfi:NFIA_034590; -.
DR   VEuPathDB; FungiDB:NFIA_034590; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_000537_6_0_1; -.
DR   OMA; YPDWIRI; -.
DR   OrthoDB; 1024049at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0102203; F:brassicasterol glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102205; F:cholesterol alpha-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102202; F:soladodine glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016906; F:sterol 3-beta-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032120; P:ascospore-type prospore membrane formation; IEA:EnsemblFungi.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   Gene3D; 2.30.29.30; -; 3.
DR   InterPro; IPR004276; GlycoTrans_28_N.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   Pfam; PF02893; GRAM; 2.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00568; GRAM; 2.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Autophagy; Cytoplasm; Glycosyltransferase; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Protein transport; Reference proteome; Repeat;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transferase; Transport.
FT   CHAIN           1..1418
FT                   /note="Sterol 3-beta-glucosyltransferase"
FT                   /id="PRO_0000318044"
FT   DOMAIN          249..288
FT                   /note="GRAM 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          289..387
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          733..799
FT                   /note="GRAM 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1339..1418
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        83..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..598
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..635
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1339..1355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1359..1375
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1376..1394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1418 AA;  158867 MW;  8CC8F82911C7D41D CRC64;
     MRPFLDDAKR RVDRKLSASR QSLSTSRLLP SALPDRLKDN HDAQVDFTAP PGGSGSREGH
     LQYMQQSIFG MIAAVGSRSD FHARFDESSD SDGESEQRPR KESSVRKGTS ASANTSSPLD
     SSQRSSSRTD GKSEKESGTR GRRHPRTISD HKLFRPFESN SKHEPQTDPS TGDEMPNISP
     PTRPRSATPR AAPILSRMVE AQAQFDLKAS STERSQPSLD ESGEKGPRGA SVSPLSTRLM
     DMFGFDKPEK VLVEYACSLL QSILLQGYMY VTEGHICFYA YLPKKSTVAI KSGYLYKRGR
     KNPKYSRYWF SLKGDVLSYY ADPSNLYFPS GHVDLRYGIS ASLGEAKEKG REPRDFQVTT
     DQRTYYFRAD SSMSAKEWVK ALQKVIFRTH NEGESVKISF PIESIIDIEE SPMVDFAETF
     KIRVIEDDDS YAIDEYFFTF FNSGREAFEF LRSLINDQSL KISSQHLSPQ PDRSPRSDPT
     RKSRNRWSLT SGTSRVLGNS RAETQRKASA STSHTSLAHD VIKSSPATRH QDSSESILNS
     FEQGTESSAA WQSMTDAAES ASQILNRSDV FQSPTIHGLD RRPSGGERRG RRNSDETARS
     LSTRANVGTG QQIDELGRRM DGDTSGREAR DSTGESDQYT QDPTKSFSGA PSLNELVKAG
     VYPLQRAAGL AEYLRTRSKQ MSNLLASESM GYIEKVSGMW TGGRKHYGEA EDVLPDDQDV
     DPEDKEDGCN YGDRFRAHFA LPRTEKLQAT YFAYLHRVLP LYGKIYVSQK KLCFRSLIPG
     TRTKMILPLR DIENVEKEKG FRFGYHGLVI IIRGHEELFF EFRTSDARDD CAVTLHQHLE
     AVKFMAESGL LAEQEQNDSE AAMTEHRMLQ EARYDDYGEN DLRPLNESSE LHPIFDDPRA
     SIVNFKPAES LRITCLTIGS RGDVQPYIAL CKGLLAEGHR PKIATHAEFE PWVRKHGIDF
     APVEGDPAEL MRICVENGMF TYSFLKEASQ KFRGWIDDLL SSAWASCQDS DLLIESPSAM
     AGIHIAEALR IPYFRAFTMP WSRTRAYPHA FAVPEHRMGG AYNYITYVMF DNVFWKAIAG
     QVNRWRKNEL GLKATTLDKM QPNKVPFLYN YSPSVVPPPL DYPDWIRITG YWFLNEGSDW
     TPPTALCEFI HRAREDGKKI VYIGFGSIVV SDPSALTKTV IESVRKADVR CILSKGWSDR
     LGDPASAKPE VPLPPEIHQI QAAPHDWLFS HIDAAVHHGG AGTTGASLRA GVPTIIKPFF
     GDQFFFGSRV EDLGVGICMK KLNVSVFSRA LWEATHSERM IIRAQDLGAR IRSEDGVATA
     IQAIYRDLEY AKTLARQRSI ASSTPFSPTP SAKTTAEQDA DDDVEDSEEW TFVGDDTDME
     MSRRLRDRAI SDADMLPDRL LANSVPGDSG PGRKLSGR
 
 
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