ATG26_YEAST
ID ATG26_YEAST Reviewed; 1198 AA.
AC Q06321; D6VYJ2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Sterol 3-beta-glucosyltransferase {ECO:0000305|PubMed:10224056};
DE EC=2.4.1.173 {ECO:0000305|PubMed:10224056};
DE AltName: Full=Autophagy-related protein 26;
DE AltName: Full=UDP-glycosyltransferase 51 {ECO:0000303|PubMed:10224056};
GN Name=ATG26; Synonyms=UGT51 {ECO:0000303|PubMed:10224056};
GN OrderedLocusNames=YLR189C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP IDENTIFICATION.
RX PubMed=10224056; DOI=10.1074/jbc.274.19.13048;
RA Warnecke D.C., Erdmann R., Fahl A., Hube B., Mueller F., Zank T.,
RA Zaehringer U., Heinz E.;
RT "Cloning and functional expression of UGT genes encoding sterol
RT glucosyltransferases from Saccharomyces cerevisiae, Candida albicans,
RT Pichia pastoris, and Dictyostelium discoideum.";
RL J. Biol. Chem. 274:13048-13059(1999).
RN [4]
RP NOMENCLATURE.
RX PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT "A unified nomenclature for yeast autophagy-related genes.";
RL Dev. Cell 5:539-545(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION.
RX PubMed=17012830; DOI=10.4161/auto.3371;
RA Cao Y., Klionsky D.J.;
RT "Atg26 is not involved in autophagy-related pathways in Saccharomyces
RT cerevisiae.";
RL Autophagy 3:17-20(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-693, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Probable sterol 3-beta-glucosyltransferase that is not
CC involved in cytoplasm to vacuole transport (Cvt), pexophagy or
CC nonselective autophagy (PubMed:17012830).
CC {ECO:0000269|PubMed:17012830}.
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:0000269|PubMed:14562095}. Membrane
CC {ECO:0000269|PubMed:14562095}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
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DR EMBL; U17246; AAB67475.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09508.1; -; Genomic_DNA.
DR PIR; S51434; S51434.
DR RefSeq; NP_013290.1; NM_001182076.1.
DR PDB; 5GL5; X-ray; 1.90 A; A/B=722-1198.
DR PDB; 5XVM; X-ray; 2.77 A; A/B=722-1198.
DR PDBsum; 5GL5; -.
DR PDBsum; 5XVM; -.
DR AlphaFoldDB; Q06321; -.
DR SMR; Q06321; -.
DR BioGRID; 31459; 75.
DR DIP; DIP-6644N; -.
DR IntAct; Q06321; 3.
DR STRING; 4932.YLR189C; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR iPTMnet; Q06321; -.
DR MaxQB; Q06321; -.
DR PaxDb; Q06321; -.
DR PRIDE; Q06321; -.
DR EnsemblFungi; YLR189C_mRNA; YLR189C; YLR189C.
DR GeneID; 850886; -.
DR KEGG; sce:YLR189C; -.
DR SGD; S000004179; ATG26.
DR VEuPathDB; FungiDB:YLR189C; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR InParanoid; Q06321; -.
DR OMA; WCNNITK; -.
DR BioCyc; YEAST:YLR189C-MON; -.
DR BRENDA; 2.4.1.173; 984.
DR Reactome; R-SCE-156588; Glucuronidation.
DR Reactome; R-SCE-189483; Heme degradation.
DR Reactome; R-SCE-9749641; Aspirin ADME.
DR Reactome; R-SCE-9753281; Paracetamol ADME.
DR Reactome; R-SCE-9754706; Atorvastatin ADME.
DR PRO; PR:Q06321; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06321; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
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; IDA:SGD.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IGI:SGD.
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; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycosyltransferase; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transferase.
FT CHAIN 1..1198
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000215616"
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..467
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..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..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:0007744|PubMed:19779198"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT STRAND 741..745
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 750..765
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 769..774
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 779..784
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 788..791
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 797..805
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 810..839
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 842..846
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 848..850
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 853..860
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 864..870
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 876..878
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 881..883
FT /evidence="ECO:0007829|PDB:5XVM"
FT HELIX 891..919
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 928..931
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 933..935
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 938..940
FT /evidence="ECO:0007829|PDB:5GL5"
FT TURN 944..946
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 957..959
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 975..986
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 990..995
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 998..1000
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 1004..1017
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 1020..1025
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 1028..1031
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 1048..1050
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 1056..1059
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 1060..1062
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 1063..1068
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 1072..1080
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 1085..1087
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 1093..1103
FT /evidence="ECO:0007829|PDB:5GL5"
FT STRAND 1106..1109
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 1115..1127
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 1129..1144
FT /evidence="ECO:0007829|PDB:5GL5"
FT HELIX 1147..1169
FT /evidence="ECO:0007829|PDB:5GL5"
SQ SEQUENCE 1198 AA; 136054 MW; 74DED87BBBF75B51 CRC64;
MPITQIISAS DSEAGPKPSI SLVPDKPSEP ETSPRHHRLS RSLSKFKRWR GRSNSSLSMG
SSEQQELQDS PNEARSDDDE NGYNNDNADD LAKSKYMMKS IAGLLTTASV YAGMNNAQEM
NVLSQVDSEE SDSSDSFQEN IGRNEVKSKK 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 GKETPATVEQ 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 MVGIHITEAL 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
