ATG26_GIBZE
ID ATG26_GIBZE Reviewed; 1443 AA.
AC I1S8Q3;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Sterol 3-beta-glucosyltransferase ATG26 {ECO:0000250|UniProtKB:Q06321};
DE EC=2.4.1.173 {ECO:0000250|UniProtKB:Q06321};
DE AltName: Full=Autophagy-related protein 26 {ECO:0000303|PubMed:28894236};
GN Name=ATG26 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG07850, FGRAMPH1_01T25811;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX PubMed=28894236; DOI=10.1038/s41598-017-11640-z;
RA Lv W., Wang C., Yang N., Que Y., Talbot N.J., Wang Z.;
RT "Genome-wide functional analysis reveals that autophagy is necessary for
RT growth, sporulation, deoxynivalenol production and virulence in Fusarium
RT graminearum.";
RL Sci. Rep. 7:11062-11062(2017).
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:Q06321,
CC 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 -!- DISRUPTION PHENOTYPE: Does not significantly decrease the growth rate
CC under nutrient-rich conditions (PubMed:28894236).
CC {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
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DR EMBL; HG970335; CEF83977.1; -; Genomic_DNA.
DR RefSeq; XP_011327675.1; XM_011329373.1.
DR AlphaFoldDB; I1S8Q3; -.
DR SMR; I1S8Q3; -.
DR STRING; 5518.FGSG_13231P0; -.
DR GeneID; 23560038; -.
DR KEGG; fgr:FGSG_13231; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G25811; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR InParanoid; I1S8Q3; -.
DR Proteomes; UP000070720; Chromosome 4.
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: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 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; Coiled coil; Cytoplasm; Glycosyltransferase; Membrane;
KW Protein transport; Reference proteome; Repeat; Transferase; Transport.
FT CHAIN 1..1443
FT /note="Sterol 3-beta-glucosyltransferase ATG26"
FT /id="PRO_0000443924"
FT DOMAIN 240..284
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 289..385
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 765..870
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 883..910
FT /evidence="ECO:0000255"
FT COMPBIAS 16..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1443 AA; 161424 MW; 47A3087DA9B74550 CRC64;
MATQADDAAA SQANIEDGDL KEHVHDELDK IQQQRSTATV FPEPLRESDS EDSDDEDNGP
AQAPPMFMNM NQSIYGLIAQ ASNRVDFNDR FDGMSSDEEG ESSQNTRTES IARTSILQPA
GKGKDKVHRR RKLSEHKLLR SLPALPKLRS RHKSQHSTLP APEEVADEAD DEHGDGGLLP
APALTLTRQD TQDRLAPVMS RMLEAKADLS IRPSFDLDRL SSDVSRSSDS DEVSALSRKL
KEIFEFDEYE QVIEEYPCWL LQSVLLQGYM YITSKHICFY AYLPKKTHEA VKSGYLSKSG
KRNPSYARFW FRLKGDVLTY YKTATDVYFP HGQIDLRYGI SASIVDTDKE ALHFVVETRH
RTYKFKADSA PSAKEWVKSL QRVIFRSHND GDSVKISLPI KNVMDIEDTQ MISFADTCKI
RVIDNDETYA IDEYFFSFFS FGKEAINVLK ILIEDSSGAR SAEQVITGDD HDSSQPSSGH
ASKAASKRAP SKLSTGKLPD TVKATLAPMS PLSPRSPSQL SPRASMDAPR SSFDGFRRFG
KKSLDVTSSI GDHSPRRSFS GRRSTSHQHR QGTTTPKQAH DSEDSFLQSS IENPSISTLS
PSSYDEPSAS QILQGSDVFH SPMMRRSAST SRKRDRSGKR TPRSSSAHGD RHHGIPHAAT
TGAIHKMGDE QADSQRPATP TLNSITKIGA YPLQRANAFA EYLSRTSQRM GSMFATESLG
YVEKVHGMWK GEHRHYDEPQ ELRTDDDGED IDSEADDKMQ TTIDRFRAHF ALPESEKLVA
TYFGAIFKVL PLYGKFYISD RSFCFRSLYP GTRTKLILPL KDIENVHKEK GFRYGYYGLT
VVIRGHEELF FEFRKPGLRD DCAVTLHQLM ETNRFLEQSG ILDQEEQDDE EAAAAMAERD
ELQEARQDEF VDHELTLPRT TSGVSNAPTI LFDNPNSSGL AFKPQKSMKI TCLTIGSRGD
IQPYIALCKG LLAEGHKPRI ATHGEFQEWV ESHGIEFARV EGDPGELMRL CIENGTFTWA
FLREANSTFR GWLDDLLDSA YTACEGSELL IESPSAMAGI HIAEKLEIPY FRAFTMPWTR
TRAYPHAFIM PEHKMGGAFN YMTYVMFDNI FWKATAYQVN RWRNKTLGLP STSLEKMQPN
KVPFLYNFSP SVVAPPLDFS DWIRVTGYWF LNEGGGDWKP PQELQDFIAK ARADGKKIVY
VGFGSIIVKD PAKMTQEVID AVLKADVRCI LSKGWSDRIS PKDDPSKPPP DEPVIPAEIH
VITSAPHDWL FSQIDAAAHH GGSGTTGASL RAGIPTIIRP FFGDQFFFST RVEDLGVGVC
VRKWGTNSFG RALWEVTRNE RMIVKARVLG EQIRSESGVD NAIQCIYRDL EYAKSLIKRR
AGKNNAEHGL AEDDDDTEES WTFVGRDEPD PDAVTKKLSD GLAGLGAAGD RPPPLGSQAP
TVA
