ATG26_ASHGO
ID ATG26_ASHGO Reviewed; 1227 AA.
AC Q751Z4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 115.
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}; OrderedLocusNames=AFR681W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 353.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Probable sterol 3-beta-glucosyltransferase that is not
CC involved in cytoplasm to vacuole transport (Cvt), pexophagy or
CC nonselective autophagy (By similarity). {ECO:0000250|UniProtKB:Q06321}.
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 Membrane {ECO:0000250|UniProtKB:Q06321}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q06321}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
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DR EMBL; AE016819; AAS54053.2; -; Genomic_DNA.
DR RefSeq; NP_986229.2; NM_212365.2.
DR AlphaFoldDB; Q751Z4; -.
DR SMR; Q751Z4; -.
DR STRING; 33169.AAS54053; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR EnsemblFungi; AAS54053; AAS54053; AGOS_AFR681W.
DR GeneID; 4622518; -.
DR KEGG; ago:AGOS_AFR681W; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR InParanoid; Q751Z4; -.
DR OMA; YPDWIRI; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C: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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
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 Pfam; PF00201; UDPGT; 1.
DR SMART; SM00568; GRAM; 2.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycosyltransferase; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Reference proteome; Repeat; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..1227
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000215606"
FT DOMAIN 188..229
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 239..342
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 602..668
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..132
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 136399 MW; 8AD3965B13219B9C CRC64;
MLKGQKEGEA EPVPEGDKSG AGSSPSGVRK GLRVPLGLVS HSFSSLAKHK EAERRLTDEE
ESLSSPQDRE DDAASPNIMA KSIAGLLTTA SMYVGIGDIH RAEQLATGQP ETDAGADETE
DEMDEAGDET GDDADAPATG TDGEEESRPV SAQESRRSTL FELSIEPHPE SHTAQASRTK
NRRSRMTSKL RSKFNLDDDE ELVREYPCWL LRDVLIQGHI YLTSRNLLFF AFLYKSNGSA
RLTGNLSICN NGLSISGISG KPTRYWTVLK DHTLSLYSSS TDLYFPVLTI DLRYVTKVQH
CKNNGKDTRQ FHITTESKTY TFYSDNEHSA RSWSSALKKQ VFATQNSDND SMSVRIPLSN
IIDVEEQAIV EQGLTLRVRV MESSDSFALD DYFFMFFNNA GSQLKELIQI QVANLEMLGA
ANVDYARHPL PPDTEASLPA VASDAAPQDA AIASEAAADA AAADTASHSP STNAEPRARG
RSTERAMAAS AYLFGRLTSP RRDDAKQLSP SKVKLRFRSV ADTLKLTTPR QPGSDAPQEP
EPETTILESR PRLNYWSPRP FTTMRSMWNA QPVHYAAKGM SLFADDDELM IGDEAELLAA
DKRFKAHFSL TDDESLVASY YTYLNRSMPL YGKIYLGKTI MCFRSLLPGS KTKMILPLHD
VENCYKEQGF RFGYFGLVVV IYGHEELFFE FASQKSRDDA EYVILKIIDS LKPVDGVMAD
DMSAGAYSLK AAQGRDATTD AKVKLFEQRI SSVGYDIPIM VEDNPFYKTT ITPKKFYTFG
MLTIGSRGDV QPYIALGKGL LQEGHRVVVI SHAEFGDWVR SHGLQFRAIA GDPAELMALM
VQHGSMNVGL IREAASTFRN WIRDLLETAW EACQGIDVLI ESPSAMAGIH IAEALQIPYF
RAFTMPWTKT RSYPHAFIVP DQKRGGNYNY FTHVLFENIF WKGINSQVNR WRVEKLGLKK
TNLEFMQQGK VPFLYNMSPT VFPPSVDFAE WIKVTGYWFL NESSNYVPPQ ALLEFMAKAR
RLDKKLVYIG FGSIVVKDPV KMTMAVVEAV VKADVYCILN KGWSARLGGQ SQKSIEVQLP
NCVYDAGNVP HDWLFPRVDA AVHHGGSGTT GATMRAGVPT VIKPFFGDQY FYANRIEDIG
AGIALRKLNA CTLSRALKEV TTNTRIIAKA KKIGQDISKE DGVATAIAFI YSEMAYAKSL
IKAKRQEDKK AAKEAKQIQN EDSWLLL
