ATG26_ASPNC
ID ATG26_ASPNC Reviewed; 1371 AA.
AC A2QNQ5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 86.
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=An07g06610;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK39507.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAK39507.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AM270135; CAK39507.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001391739.2; XM_001391702.2.
DR AlphaFoldDB; A2QNQ5; -.
DR SMR; A2QNQ5; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PRIDE; A2QNQ5; -.
DR EnsemblFungi; CAK39507; CAK39507; An07g06610.
DR GeneID; 4981929; -.
DR KEGG; ang:ANI_1_830064; -.
DR Proteomes; UP000006706; Chromosome 4L.
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; -; 2.
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..1371
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000318041"
FT DOMAIN 241..301
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 292..391
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 717..783
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1325..1352
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 87..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1371 AA; 153536 MW; 1E8C4CF3CEFA773F CRC64;
MRPFIDDAKR RVDRRLSASR QSISNSRMFA SVLPERLRND NDDDDDSQVD FSAPPGGMGP
REGHMQYMHQ SIFGMIAAVG SRSGFHARYD ESSDSDGEDE SRARKDAENL SATAGALPKR
SGNESPRLSP KPQSPTPERG RRHRRTISDH KLLRPFKLNS KQNKGQEPAV QSEPQTGDEM
SRASTPKRPR SVTPRAAPVL SRMVEARALL DTEDSTKGAP STTEEIRDEG PTQKSASALS
LRLKEMFGFE APEKVLVEYA CSFLQSMLLQ GYMYVTEGHV CFYAYLPRKS TVAIKSGYVY
KRGRKNPKYN RYWFSLKGDV LSYYADPSKL YFPSGHVDLR YGISASLAEP KDKGREVKDF
QVTTDQRTYY FRADSSSSAK EWVKALQKVI FRTHNDKGSV KISFPIENII DIEESPMVDF
AETFKIRVVE SEETYAIDEY YFTSFNYGQD AFNFLKGLVA DTPMKRSQQT LSPQPEQTSR
SRRTRGSQNR WSITSATSQS RGIGKSGNRR RSASTGQFSF GHDALSMSPP MRQQDSSLSF
GNSFEQATEA SGILQSMTDT TESASQILNR SDVFQSPTIR TMRRGPSGAE KTVRRHSDET
ARSVHTTRNG PEIQYAVSES DRDTQTPSGL HPSTPALNEL VRAGVYPLQR AAGFAEYLKT
RSKQMSNLLA SESMGYLEKV SGMWAGGGKH YGESENILPD DQAVDPEDLE AGCKDGDRFR
EHFALPPSEK LQASYFAWLH RMIPLYGKIY ISQKKLCFRS LMPGTRTKMI LPLKDVENVD
KEKGFNFGRH GLVVVIRGHE ELFFEFGTAD TRDDCAVTLH KGLESTKFLM ASGLLAECEE
KDESESATAE HRLLQEARLD ITGMHSSRSA MAASNELHPI FDDPRASIIN FKPTESLRIT
CLTIGSRGDV QPYIALCKGL LAEGHRPKIA THAEFEPWVR KHGIDFALVD GDPAELMRIC
VENGMFTYSF FKEATAKFRG WIDDLLSSAW KACQDTDLLI ESPSAMAGIH IAEALRIPYF
RAFTMPWSRT RAYPHAFAVP EHKMGGAYNY ITYVMFDNVF WKSVAGQVNR WRKKELGLKA
TGLDKMQPNK VPFLYNYSPT VVPPPLDYPD WIRITGYWFL SEGSDWTPPA ELVDFIQRAR
KDEKKVVYIG FGSIVVSDPS ALTRTVIESV QKADVRCILS KGWSDRLGDP ASAKSEVPLP
PEIYQIQSAP HDWLFSHIDA AAHHGGAGTT GASLRAGVPT IVKPFFGDQF FFGTRVEDLG
VGICLKKLNV TMFSRALWEA THDERMIVKA HKLGAQIRSE DGVDTAIQAI YRDLEYAKTL
AQARSNVSST PFSPTPSAKT VAEQEADEDV PEEEWTIVED DTELEMRPTV A
