ATG26_YEAS7
ID ATG26_YEAS7 Reviewed; 1198 AA.
AC A7A179;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=SCY_3757;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000169; EDN59412.1; -; Genomic_DNA.
DR AlphaFoldDB; A7A179; -.
DR SMR; A7A179; -.
DR PRIDE; A7A179; -.
DR EnsemblFungi; EDN59412; EDN59412; SCY_3757.
DR HOGENOM; CLU_000537_6_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
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; Phosphoprotein; Repeat; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..1198
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000318050"
FT DOMAIN 187..236
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 238..336
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 570..636
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06321"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06321"
SQ SEQUENCE 1198 AA; 135968 MW; 03572AAD61DCFD73 CRC64;
MPITQIISAS DSEAGPKPSI SLVPDKPSEP ETSPRHHRLS RSLSKFKRWR GRSNSSLSMG
SSEQQELQDS PNEARSDDDE NGYNNDNADD LAKSKYMMKS IAGLLTTASV YAGMNNAQEM
NVLSQVDSEE SDSSDSFQEN IGQNEVKSKK ENLKTKSHPE VPRLDKRKPT LFDFSITREK
LSKDNVAKLR QRFCLDEQEP FLNDFPAWLL KDVLVQGHIF ITTKHFLFFA YLPKNPRSVK
MSGNLNIRTK LIRSTRYWCV LKNHLFSMYT SSTELYFPVL TIDLREVQKI ETQKHTLNGS
ATKTFKLYTD ESTFKFNADS EFSAKSWVNA LKKEQFAAQN SENNSISLKI PLPNIIEIDD
QPIVNKALTL RLRALESSQT YAIDDFMFVF MDGSGSQVKE SLGEQLAILQ KSGVNTLYYD
IPAKKSKSSF GKETPATAEQ KNNGEDSKYL NVPTSAVPSS ENGKKSRFRF RERSNSWFRR
AKPLEDSQVE DVEEIYKDAA NDIDSSVHST IHIHEQEDSQ EQTVAWKPSH LKNFAEMWAA
KPIHYRNKFI PFQKDDTYLI KETEEVSANE RFRYHFKFNK EKSLISTYYT YLNRNVPVYG
KIYVSNDTVC FRSLLPGSNT YMVLPLVDVE TCYKEKGFRF GYFVLVIVIH GHEELFFEFS
TEVARDDIER ILLKLLDNIY ASSAEGSNIS SASLGDVQHN PDSAKLKLFE DKINAEGFEV
PLMIDENPHY KTSIKPNKSY KFGLLTIGSR GDVQPYIALG KGLIKEGHQV VIITHSEFRD
FVESHGIQFE EIAGNPVELM SLMVENESMN VKMLREASSK FRGWIDALLQ TSWEVCNRRK
FDILIESPSA MVGIHIAEAL QIPYFRAFTM PWTRTRAYPH AFIVPDQKRG GNYNYLTHVL
FENVFWKGIS GQVNKWRVET LGLGKTNLFL LQQNNVPFLY NVSPTIFPPS IDFSEWVRVT
GYWFLDDKST FKPPAELQEF ISEARSKGKK LVYIGFGSIV VSNAKEMTEA LVEAVMEADV
YCILNKGWSE RLGDKAAKKT EVDLPRNILN IGNVPHDWLF PQVDAAVHHG GSGTTGASLR
AGLPTVIKPF FGDQFFYAGR VEDIGVGIAL KKLNAQTLAD ALKVATTNKI MKDRAGLIKK
KISKEDGIKT AISAIYNELE YARSVTLSRV KTPRKKEENV DATKLTPAET TDEGWTMI
