ID   ATG26_ASPOR             Reviewed;        1384 AA.
AC   Q2U0C3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 101.
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:0000303|PubMed:27696999};
GN   Name=atg26 {ECO:0000303|PubMed:27696999}; ORFNames=AO090011000498;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DOMAIN.
RX   PubMed=27696999; DOI=10.1080/09168451.2016.1240603;
RA   Kikuma T., Tadokoro T., Maruyama J.I., Kitamoto K.;
RT   "AoAtg26, a putative sterol glucosyltransferase, is required for autophagic
RT   degradation of peroxisomes, mitochondria, and nuclei in the filamentous
RT   fungus Aspergillus oryzae.";
RL   Biosci. Biotechnol. Biochem. 81:384-395(2017).
CC   -!- FUNCTION: Probable sterol 3-beta-glucosyltransferase that mediates
CC       autophagic degradation of peroxisomes (pexophagy) (PubMed:27696999).
CC       Also required for cytoplasm to vacuole transport (Cvt) and autophagic
CC       degradation of mitochondria (mitophagy) and nuclei (nucleophagy)
CC       (PubMed:27696999). {ECO:0000269|PubMed:27696999}.
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:0000269|PubMed:27696999};
CC       Peripheral membrane protein {ECO:0000269|PubMed:27696999}.
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 (PubMed:27696999). {ECO:0000269|PubMed:27696999}.
CC   -!- DISRUPTION PHENOTYPE: Leads to white colonies with decreased
CC       conidiation and aerial hyphae formation (PubMed:27696999). Impairs
CC       autophagy by the accumulation of the intermediate of autophagosome
CC       (PubMed:27696999). {ECO:0000269|PubMed:27696999}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE64992.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007171; BAE64992.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q2U0C3; -.
DR   SMR; Q2U0C3; -.
DR   STRING; 510516.Q2U0C3; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   Proteomes; UP000006564; Chromosome 7.
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   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..1384
FT                   /note="Sterol 3-beta-glucosyltransferase"
FT                   /id="PRO_0000318042"
FT   DOMAIN          237..284
FT                   /note="GRAM 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          285..384
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          714..817
FT                   /note="GRAM 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1322..1350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..574
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..589
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1384 AA;  154514 MW;  A5B4031635513FCB CRC64;
     MPNMKPLLED AKRRVDRRLS ASRQSISSSR IFSSAFPDRL KDDHDAQVDY TAPPRGAGSR
     DGQLPYMHQS IFSMIAAVGS KSDFHARFDE SSDSEGEAEG QTQKQPGKAS LSNKKKFPLS
     PTLKPQSTLE GRGRRHRRSI SDNKLLRSLK PSPKSSKGTE TTVQTEPPTS DEMSPLASPR
     RARSATPRAA PILSRMLEAE ALLDKKQSAD QPSSSTKGET DGTSEQSCAS PLSLRLKEMF
     GFEMPEKVLM EYACSLLQNI LLQGYMYVTE GHICFYAYLP RKSAVTIRSG YLHKRGRKNP
     KYNRYWFSLK GDVLSYYTDP SSLYFPSGHV DLRYGISASL TEQKDKDKEV RDFQVTTDQR
     TYYFRADSSA SAKEWVKALQ KVIFRAHNEG DSVKISFPIE SIIDIEESPI TDLAETFKIR
     VVESDESYAI DEYYFSFFES GRDAYNFVKG LISEGPMKTS QLLPPPSEQT SPATRARGPR
     NRWSLNSDLS QSRGNGIFKT QRKRSASTGQ TNSGPDGIGM SPRQRDLSDS FVNSFEQATD
     ASAVLQSMID TTESASQILN RSDVFQSPTI HTLRQRHPSG DRTGRRLSDG TARSTHPNAA
     DANRNGQEMQ YASSDSDQGT QHPSKVNSSA PTLNELVKAG AYPLQRAAGF AEYLRSRSRQ
     MSNLLASESM GYIEKVSGMW AGGRRHYGET EGVLPDDQDV DPEDKEDGVK HGDRFRAHFA
     LPSTERLQAT YYAYLHRVLP LYGKIYISQK KLCFRSLIPG TRTKLILPLK DIENVEKEKG
     FRFGYQGLVI IIRGHEELFF EFNTADARDD CAVTVHQSLE SMRFLVESGL LAEQEKDEIE
     SAQAEHRMLQ EARLDGAGEH DSHASVNESS ELHPIFDDPR ASIINFKPSE SLRITCLTIG
     SRGDVQPYIA LCKGLLAEGH KPKIATHAEF EPWVRQHGID FAPVDGDPAE LMRICVENGM
     FTYSFLKEAS TKFRGWIDDL LSSAWASCQD SDLLIESPSA MAGIHIAEAL RIPYFRAFTM
     PWSRTRAYPH AFAVPENKMG GAYNYITYVM FDTVFWKAIA GQVNRWRKKQ LGLKATTLDK
     MQPNKVPFLY NYSPSVVAPP LDYPDWIRIT GYWFLSEGGN WTPPTDLLDF IHRARSDGKK
     IVYIGFGSIV VSDPSALTRT VVESVLKADV RCILSKGWSD RLGDPASAKV EIPLPPEIFQ
     IQAAPHDWLF SQIDAAAHHG GAGTTGASLR AGVPTIVKPF FGDQFFFGTR VEDLGVGICM
     KKLNVSVFSR ALWEATHSER MIVKARELGA QIRSENGVDT AIQAIYRDLE YAKTLARQRS
     IVSSTPFSPT PSAKTTAEQE EDDVDDSEEW TFVGDDTEID VSRRLRDRAV SDADMLPEPV
     TSAS