ATG26_YARLI
ID ATG26_YARLI Reviewed; 1456 AA.
AC Q6C8M8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 109.
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=YALI0D18403g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP FUNCTION.
RX PubMed=14585290; DOI=10.1016/j.cellbi.2003.08.004;
RA Stasyk O.V., Nazarko T.Y., Stasyk O.G., Krasovska O.S., Warnecke D.C.,
RA Nicaud J.-M., Cregg J.M., Sibirny A.A.;
RT "Sterol glucosyltransferases have different functional roles in Pichia
RT pastoris and Yarrowia lipolytica.";
RL Cell Biol. Int. 27:947-952(2003).
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; CR382130; CAG81176.2; -; Genomic_DNA.
DR RefSeq; XP_502984.2; XM_502984.2.
DR AlphaFoldDB; Q6C8M8; -.
DR SMR; Q6C8M8; -.
DR STRING; 4952.CAG81176; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR EnsemblFungi; CAG81176; CAG81176; YALI0_D18403g.
DR GeneID; 2911115; -.
DR KEGG; yli:YALI0D18403g; -.
DR VEuPathDB; FungiDB:YALI0_D18403g; -.
DR HOGENOM; CLU_000537_6_0_1; -.
DR InParanoid; Q6C8M8; -.
DR OMA; YPDWIRI; -.
DR Proteomes; UP000001300; Chromosome D.
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: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 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; 1.
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..1456
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000215615"
FT DOMAIN 200..247
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 251..351
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 827..893
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 60..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1456 AA; 159607 MW; 6C585F5A9266FDA5 CRC64;
MLSASQFLKH RVSCLPMLNK VESDSTDGDP DDACQHPHDC NIFSVLVNGA TDRLEGFFDE
SDEEDGDEVE TPSTTTTAVS PSATMSAPSP TATAPTPHSG THTPKSPLHS ISHCPSFNSV
AQALPHSLSP HSLCHTSSHE ASRRGSAEQP SRTQSELARR IKTENILNSF HDSLEAAYEK
CHGGANPEEH QSNKTEYFQQ KLKGFAALDV DEQLIADYPV WLLKNVLIQG HLYITAKHMC
FLSYLPRRQN ANIRSGTLVK ARKRSLREGT RYWCVLKNDS FSYYPDSTDV YFPAGTIDLS
EALAAELCDD EGDVTEPESF RIVMPKKSVL FKADSHSAAH EWVKALQKEI FRAHNQGDTV
RIVIPLQNIV DLEKTKIFEF ATTIKTSVVE SNETYAIDEY IFTFFKFGDD VLRTLTENGV
EISGGNFSPR QSQLAVGHKH VTESVRDSTL LHASGHHHHF FHSAHHESDG KSNSKSHTSS
RSHTPRNLTP QVTGEQPHER DEKRDSKLPR LPKFLRRFKD KVDDKCDDKP TLVPSFLKSR
ASSRRNSAEG SDRPNLASQR TSSSTLFPSA PPTPGSQPTT PGVHAPGSST PGGSYGTTTP
GTPASADSVS LAGTPGVAAP VGDIEGLNGN PMPAGIAAEL KEKRKSGGAT SSGAATGATT
PGGAAAPGST GNSSPGTPGG LGGPGAVGAG GPGVMGGAES APAGTVPQQS HHAGISVVAP
HDPAAAAAAA DAAAPFTRGP GSGIPEIQDD SDSSDDDHWG HIGTAEVDED PEQDTFKKKN
KRFSTLSKVS DLWSGSTKHY GKHHTERLGD DDDKHLASAE EITESNERFQ KRFALGTEER
LIASYHCHLH RGGIPTYGKM YVSTNYVTFR SFLRTKTLMI VPLKVVENAT KDSGFKFGYS
GLVLTIQGYE EIFFEFASAS HRDDAEVMLL RQLDIIRPHI NDDIKSDDQY MLQSARLCTY
EDALKAEANV EMPPVIIDGN LASVLPGLVT PQSKMLFTLL TIGSRGDVQP YISLGKALIE
EGHRVRIATH SEFKDWIEGY GIEFKEVAGD PSELMKIMVD HGVFSVSFLR DAASKFRGWI
NELLASSWEA CQGSDVLIES PSAMAGIHIA EALQIPYFRA FTMPWSRTRA YPHAFIVPDQ
KMGGSYNYLT YVMFDNVFWK GISGQVNRWR KKTLHLPRTN LDHMEQNKVP FLYNVSPAVL
PPPVDFPDWI KITGYWFLDE GSKDYTPDDK LCRFMEKARN DGKKLVYIGF GSIVVSDPTA
LTKSVVESVL KADVRCILNK GWSDRLGKKD AKEPEIPLPE EVLQITNCPH DWLFPQIDAC
VHHGGSGTTG AGLRAGLPTI IKPFFGDQFF YANRVEDLGA GIHLRKLNVS QFSKALWEAT
HNERIIAKAA AVGRQIRSEN GVISAIQAIY RDLDYARSLV QKKRGYTPTS DKEEETWTLV
DDIERQMQDE VEKHNL
