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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
 
 
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