ID   ATG26_NEUCR             Reviewed;        1553 AA.
AC   Q7S1I0; A7UXD3; A7UXI0; V5IKF3;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=apg-12; Synonyms=atg26 {ECO:0000250|UniProtKB:Q06321};
GN   ORFNames=NCU09301, NCU11419/NCU11407;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002242; ESA41790.1; -; Genomic_DNA.
DR   EMBL; CM002242; ESA41791.1; -; Genomic_DNA.
DR   EMBL; CM002242; ESA41792.1; -; Genomic_DNA.
DR   RefSeq; XP_011395289.1; XM_011396987.1.
DR   RefSeq; XP_011395290.1; XM_011396988.1.
DR   RefSeq; XP_011395291.1; XM_011396989.1.
DR   AlphaFoldDB; Q7S1I0; -.
DR   SMR; Q7S1I0; -.
DR   STRING; 5141.EFNCRP00000009839; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PRIDE; Q7S1I0; -.
DR   EnsemblFungi; ESA41790; ESA41790; NCU09301.
DR   EnsemblFungi; ESA41791; ESA41791; NCU09301.
DR   EnsemblFungi; ESA41792; ESA41792; NCU09301.
DR   GeneID; 23568507; -.
DR   KEGG; ncr:NCU09301; -.
DR   VEuPathDB; FungiDB:NCU09301; -.
DR   HOGENOM; CLU_000537_6_0_1; -.
DR   InParanoid; Q7S1I0; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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; 1.
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..1553
FT                   /note="Sterol 3-beta-glucosyltransferase"
FT                   /id="PRO_0000215613"
FT   DOMAIN          323..370
FT                   /note="GRAM 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          374..470
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          464..495
FT                   /note="GRAM 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          834..900
FT                   /note="GRAM 3"
FT                   /evidence="ECO:0000255"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          805..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1446..1504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1527..1553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..650
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1470..1492
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1553 AA;  171968 MW;  574FB8BAD1645240 CRC64;
     MASSQPTSSG PILDSPPSPN PQSQLNTETS SSQHRANPSE APAQPGPGPA RPSALTKRPS
     HREVAAYRMS RKLQRLRADS NQPHSPTMEL PDRLKDNGKE EDNEEDVLQP QGGMFMNMNQ
     SIFGLIAAAG STVDFHDRFE GQSSEDEDDV PNHMAMTFAG PGIKGTARNR ETAGTVKSLS
     QTVVFNKPPA SATVDAGPSN IHRRRLPGHK LLQSVPSLSR LSSSHKSKKT KQHNATAMAD
     NKIEEEEDPD PSSPLPPLSK DETESLGLAP PIEIVRAEGN GAPLMSRMLE ARAEMEARPS
     FDLDRLSGEH RRDDAGVTGQ LAKKLKDIFE FDTAEEVIEE YPCWLLQHVL LQGYMYITAN
     HIAFYAHLPK KAHEIAKSGY LSKSGKRNPK YNRYWFRLKG DVLSYYQDPK DHYFPAGQID
     LRYGISASVN DKEKEGNYFS VSTHHRTYHF KADSARSAKE WVKSLQRVIF RSHNDGDSVK
     ISIPIRNILD IEEAQMVEFA DTCKIRVIDN DETYAIDEYF FSFFSFGKKA IQVLKVLVED
     SSPEDSGAND APKGTGGDRA IGDNLGSPRT RTFSEGVKAT LSPVSPIQIA SPSSRASGDY
     FKSSFDGTRP FSRRSFDASP GTAGYAGSPP RRLHGDGRRS FSKPRHEPHA STDSYAQSFD
     DPSQASLSAL VASGSEDQSA SQILRGSDVF HSPIFRRSAS ATRATTEGEG VAAPPIVRQH
     TAGLVRLHGP HHAATTGQIG DHMAEAEGGP STPMLQSIAM MGNYPLQRAN AFMGYLDQQS
     RRMSNLLATE SMGYVEKVSG MWKGGKKHYD HPAGRRTERE DVEDDPEERA LSEARFQAHF
     ALPETERLQA AYFGFIVRVL PLYGKIYISN RHFCFRSLLP GTRTKLILPL KDIETVDKEK
     GFRFGYSGLV VVIRGHEEIF FEFAKAENRD DCAITIIQSL DAARYLAESQ EVEEAQAAEA
     ERDALNQARN EEFPDHEIEL PRQASGVSDA PTILFDDPKA SFLNFKPSEP MRITCLTIGS
     RGDVQPYIAL CKRLLEEGHR PKIVTHREFK DWIESHGIEF GPVEGDPSEL MRICIENGTF
     TYAFLREANS KFRGWLDELL TSAWEACQGS DLLIESPSAM AGIHIAEALG IPYFRAFTMP
     WTRTRAYPHA FIMPGQKMGG AYNYITYVMF DNVFWKATAH QVNRWRNKYL GLPNTSLEKL
     QPNKVPFLYN FSPSVVPPPI DYSDWIRVTG YWFLDEGGDK WQPPKELTDF IAKARADEKK
     LVYIGFGSII VSDPAKMTQE IIDAVLKADV RCILSKGWSD RSATVDGVEK PKVADPSFPP
     EILQIQSAPH DWLFQQVDAA AHHGGSGTTG ASLRAGIPTI IRPFFGDQFF FAGRVEDLGV
     GIYLKKWGVQ SFARALWEAT HSSRMQMRAE VLGGQIRAEN GVDTAIQAIY RDLDYARNLI
     TLKRQKHQSR RNSVATPTPG AKPNAPEDDQ GQAAEEDDID ADDEEEESWT FVGGNEDDLT
     GSMSMSRSDM LSQTVADLRG VKVGKAPALG SRVLSSPPTS PGAMRGAGGV KYV