ATG26_DEBHA
ID ATG26_DEBHA Reviewed; 1574 AA.
AC Q6BN88; B5RU66;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 104.
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=DEHA2E23738g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382137; CAR65878.1; -; Genomic_DNA.
DR RefSeq; XP_002770537.1; XM_002770491.1.
DR AlphaFoldDB; Q6BN88; -.
DR SMR; Q6BN88; -.
DR STRING; 4959.XP_002770537.1; -.
DR PRIDE; Q6BN88; -.
DR EnsemblFungi; CAR65878; CAR65878; DEHA2E23738g.
DR GeneID; 8998839; -.
DR KEGG; dha:DEHA2E23738g; -.
DR VEuPathDB; FungiDB:DEHA2E23738g; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR InParanoid; Q6BN88; -.
DR OMA; WKGISSQ; -.
DR OrthoDB; 1024049at2759; -.
DR BRENDA; 2.4.1.173; 1111.
DR Proteomes; UP000000599; Chromosome E.
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; 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..1574
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000215609"
FT DOMAIN 253..288
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 323..471
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 854..920
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 37..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1505..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1574 AA; 177279 MW; 7435219832B0944C CRC64;
MLPKEDKVNS NHFKGVNDAH KTSLYKRLSS SVIPPLTFLN QNPASPNNEE VPGNNEANKD
EKTFSDDEDI AHPIGSVGSS NNFLSFLYAG MGKLSDLKGN DASNANEAKD SKLNDNLRSS
RNEQANEPEY RREYKLDYDI DESEEDDIES TRDENTLKPK TEDTSVHSKL DPEERLENVV
NMLFDDHDES TTALASDPSK GTVFQQSVLK NFDPFRIQQT ELLKLKDITL STEEDESEEQ
KLKKKFFRLK VADKLKRVFE LNDDDYFYGN YNVWLVRDVL LQGHIYLTKE SILFFTFLPK
RHNTISASKG TTGGFQHHDD SHDVIQSGSL GMKTALYGDT VFSTPLTHRF WVILRNETIT
VYHSPTDLYF PITLIDLKSC VRAEVIEKGR NDNASPRPDL HRNDSQEVSS GDEEVEFSNM
LNSNYQLEDN SENVSGGYWF KVVTKKKTHK FHSDSLYSAR QWVNNIVKVV FQLHNSNANN
EVIMKIPIND VLSFDLNEVF GASEKNSDSN GGEEKPKVLN VKYLENGSKG RYALSASRMK
KELKNKTKKK MKKNSGNEPD ELLSENTYFL LFKDGDEVFS TLNEIVNENH HSSNIFRNRH
NSISKKYTSE KGSNWNRPFT HKDEEIHIPR AISTLTTDHF QNSIIDQIEE ASHRNTHTQN
TDLASPRSEC GLTHSVSTSP QSKIRKFGKT LITPSKIFSN KSRTESEKST PDRSQTTSPV
QGINLSLSGL KDLNMAFEAS QKNYEVSCTR YSHTEENSTN SPSNFQNNTL SKADALSPQI
KSPQPLEAGP LNLTDPSEYE DNKKKNSTLS SIGKSIKAMS SIRSKLAAVN HYEQLDENDT
YFIRDVSARE VDTRHFQERF SFNNKKQLIA SYHCHIIRAV PVFGKVYLGD SEICFRSMLP
GVSTRMILPL IDVDTCSKEK GSNIAYSGLV LVIRGYDELF MEFSVQSARD DCLAMILRQL
EKNRESGNES SDDNKSAQHG KSGCFQKTPS SAETTKSSNE IKLAQWRIEN ARLKLFEDKI
NAAAGLHVPI VLEDSPFYKT EIRPSTSFNF TLLTIGSRGD VQPYIALGKG LLNEGHNVTI
ATHSDFEEWI VGHGIKFKTI AGNPVELMSL MVTHGSMSLS FLKEASSKFR GWIQELLDTS
WKACQGSDIL IESPSAMVGA HIAEALGIPY IRAFTMPWTR TRAYPHAFIV PDKKKGGSYN
YITHLMFETV LWKGISSQVN KWRRESLGLP RTNLYRLAQY DIPFLYNISP TIFPPSVDFP
DWVKVTGYWF LDEGAADDFE PSKELVEFMN KARADDKKVV YIGFGSIVVE DAKSLTKAIV
EAVLNADVRC ILNKGWSDRN SSPAKDNAEP EVELPEEIYN SGSIPHDWLF PKIDAAVHHG
GSGTTGATMR AGIPTIIKPF FGDQFFYSSR IEDIGAGIGL KKLNARSLCT ALKTATSDAK
MITKAKKISE RLKQENGVLN AIEAIYYELE YARSLILAKQ HENTKHDLKS GTQTPVVNET
NEYFDSDTYD ADHDSDKESD HDQTYEQDNH SDYDVANDDN MTEIVEPSLE DGNDTVRIAP
DSGNDNTTVT DANK
