ID   ATG26_KLULA             Reviewed;        1209 AA.
AC   Q6CUV2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=KLLA0C02035g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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).
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; CR382123; CAH01138.1; -; Genomic_DNA.
DR   RefSeq; XP_452287.1; XM_452287.1.
DR   AlphaFoldDB; Q6CUV2; -.
DR   SMR; Q6CUV2; -.
DR   STRING; 28985.XP_452287.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PRIDE; Q6CUV2; -.
DR   EnsemblFungi; CAH01138; CAH01138; KLLA0_C02035g.
DR   GeneID; 2891856; -.
DR   KEGG; kla:KLLA0_C02035g; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_000537_6_0_1; -.
DR   InParanoid; Q6CUV2; -.
DR   OMA; WCNNITK; -.
DR   BRENDA; 2.4.1.173; 2825.
DR   Proteomes; UP000000598; Chromosome C.
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   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..1209
FT                   /note="Sterol 3-beta-glucosyltransferase"
FT                   /id="PRO_0000215611"
FT   DOMAIN          167..217
FT                   /note="GRAM 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          218..315
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          568..634
FT                   /note="GRAM 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1186..1209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1209 AA;  136047 MW;  0D5653C52FE15CF7 CRC64;
     MPKDSSEHQK SPSRFTRSMF VDPRAFVRRS VSPVDQLCHS VADLRFVSSN TETLESRLQA
     LSKKFDNGSE NHGQDTDTVE DVAKTQYMAK SFAGLIATAS MYVGINELGD KEENDEDELE
     LMNDAASVLD TSSQANQTLF EVSIEMNADA ISQISTDSKS RKELIRERLI KKFLPNDDEK
     YIEEYPCWLL RDIMIQGHAY LTNKHLFFFA FIPNFESDFN VTGSLRLISG HVLSKSHRYW
     VVLKGHTLSF HNSSTDLYFP LLTIDLRDIS SVQMTSSENN PTKFELSIKD QSLVLKADSF
     HSARHWVSSI KKQMFASQHS DTNTMTIKIP LQNIVDLEET SILDKSGTLR IKALENLSTY
     AVDEYFFVFF KGNANAMKQK VNSLLKDLEM NGSQILVNFN KVDSPLGINE KLPDLNYDDP
     SNENNLVDDA DINSAETDTL SPGTMQSALT LQQTSSAFSP RHSAYPRKVK KKLKSMAGSL
     KLGSPSKFTK LEDDIIIEHY SPGLINDQTI DYDKDSKSII SRLTPKKFQN VPLMWAADPV
     HFNSDDGIVF PLDDKYTADA DISNQSNVRF RQHFSFDETA NLVASYHGYL NRNVPIYGKI
     YISDKNICFR SLLPGVSTKT VLPLEDVENC YKETRFRFGY FGLVIVIHGH EELFLEFGNK
     NARDDCEFVM IKVMDAVSSH RSTLKRKSTA EVVHRLSEAA SLKLLEEKIS EQGFDIPLIV
     EKNPYFTTVI KPSKSYKFGL LTIGSRGDVQ PYIALAKGLQ AEGHEVIILT HGEFKDWIVS
     HNIGFREISG NPAELISLMV QHGSMNMGLL RDASTNFSTW ISSLLDTAWE GCQGIDILIE
     SPSAMAGIHI AEALRIPYFR AFTMPWTRTR AYPHAFIVPD QKRGGNYNYF THVLFENIFW
     KGISGKVNEW RETKLKLPKT NLVSMQQNRV PFLYNVSPIV FPPSVDFNEW IKVTGYWFLD
     EKRSYKPPAE FMEFLNKARE LKKKVVYIGF GSIVVNDPEK MTDTIIEAVR DAGVYCVLNK
     GWSNRFGDPL AKKIDKELPS YIYNSGDVPH DWLFTKIDAT VHHGGSGTTG ASLRAGLPTI
     IKPFFGDQFF YASRVEDIGA GVALKKLNRS SLAKALKEVT TNTRIIQKAR QIGESISKEH
     GVATAIGAIY SELGYARSLI KTKNPVDDKE MEAASTKLSN DAVVTAKGNE KEEYSSEGSG
     SNDGSWLLI