ATG26_CANAL
ID ATG26_CANAL Reviewed; 1512 AA.
AC Q5A950; A0A1D8PS52; Q5A9F2; Q9Y752;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 102.
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};
DE AltName: Full=UDP-glycosyltransferase 51;
GN Name=ATG26 {ECO:0000250|UniProtKB:Q06321}; Synonyms=UGT51, UGT51C, UGT51C1;
GN OrderedLocusNames=CAALFM_CR02160WA; ORFNames=CaO19.10147, CaO19.2616;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1161;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; AF091398; AAD29571.1; -; Genomic_DNA.
DR EMBL; CP017630; AOW30966.1; -; Genomic_DNA.
DR RefSeq; XP_718281.2; XM_713188.2.
DR AlphaFoldDB; Q5A950; -.
DR SMR; Q5A950; -.
DR STRING; 237561.Q5A950; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PRIDE; Q5A950; -.
DR GeneID; 3640147; -.
DR KEGG; cal:CAALFM_CR02160WA; -.
DR CGD; CAL0000189652; UGT51C1.
DR VEuPathDB; FungiDB:CR_02160W_A; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR InParanoid; Q5A950; -.
DR OrthoDB; 1024049at2759; -.
DR BRENDA; 2.4.1.173; 1096.
DR PRO; PR:Q5A950; -.
DR Proteomes; UP000000559; Chromosome R.
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; 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..1512
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000215607"
FT DOMAIN 296..331
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 359..520
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 816..880
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 22..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1467..1495
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 164
FT /note="K -> E (in Ref. 1; AAD29571)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="K -> RTA (in Ref. 1; AAD29571)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="K -> E (in Ref. 1; AAD29571)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="V -> A (in Ref. 1; AAD29571)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="S -> L (in Ref. 1; AAD29571)"
FT /evidence="ECO:0000305"
FT CONFLICT 810
FT /note="D -> E (in Ref. 1; AAD29571)"
FT /evidence="ECO:0000305"
FT CONFLICT 1130
FT /note="A -> G (in Ref. 1; AAD29571)"
FT /evidence="ECO:0000305"
FT CONFLICT 1491
FT /note="E -> EEE (in Ref. 1; AAD29571)"
FT /evidence="ECO:0000305"
FT CONFLICT 1506
FT /note="P -> R (in Ref. 1; AAD29571)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1512 AA; 170442 MW; 0648684CBDF93866 CRC64;
MSFYKKVTRG LATPLQGSIN LFSGSPNVSG DEGTDADNEN PEHRTTYHSL SGRVNHDDDD
EDVAKLEDIV GFFTGLLNTT TVCAGLGSLN NLKKHYLDEF IKKSALNPLR PQNYGPETSS
KLNNNSIEEL LNNGDTSLEK VRKMSLYDFD EHTSDSEEED SADKEEESIA ENLKPGKSGK
ARNHPRDSRT TATLITTQIT RTKTATTATP TPTPTSSVDT DVTDVTEPIG KVTTKIPEEQ
LQGLNPLQKS VVKNLDPHHV REGVLIKVKN SETPLKNDRQ ELLEKIQLRL KIADKLQRVF
DLSDEDTFCG NYSAWLIKDV LLQGHVYLTK DALLYFAFLP KRFSLENSSE VLDEDNSSSI
VYSGNLGLKS AKYGEVVLNT VLQHRYWAVL RAETLSIYSS STNLYFPVLV IDIKKCLYTE
IIDKEKLNRE AISPVNRGTY SPNGGLSGTA TPRASTLENT ASELNSMLSG DSYSPTEDNV
ETTASTVWFK LVTKKKTYKF SCDSSFSARQ WCNNITKLIF QHNNANSNGE VLIKIPISKI
AEYNKRALFS EEEEEDRTLD VTMNDIPLNV TIKYLGDNDN ERKRDKLKRK YKGEEPTIEE
VHFLFPKSGV EFFETFDKLV NPVVSDNDNQ SSKSSITSTN FSEKAISTLS KSPNHLVQTV
LDFNKPVDDD ISAFKKFGTT ITSPTRIFKA TITSPEMTSI DETSLRDSFD SDRLHLPRDM
SERALKNLEV SFVTSLKKLE DASKRYEKPH MEHSQTNLAS ILSDPSEVKK ESKTAISKSI
KALYSVGTHW SATPNHYFEL GKYYVNKVQD RDSSQRNFQS HFSTNSKLLA SYYGHLLRTV
PVYGKIYVSE TDVCFRSLLP GVSTKMVLPM TDIEEVRASR GSRLTYHGLR LIVRGSEELD
LEFGSSKSRD DFQKVVLSVL ERLHSKEGFR PEPYQWGSNF EVELYKTRME YSDSENREIQ
QYDNSIDIKF AEKKIEMARV RMFEDRLMAA SGLDVPIILE DSPFFKTELR PSTSYNITLL
TIGSRGDVQP YIALGKGLVK EGHNVTIATH AEFGDWIKTF GLGFKEIAGD PAELMSFMVT
HNSMSVGFLK NAQQKFRSWI SKLLTTSWEA CQGSDILIES PSAMSGIHIA EALGIPYFRA
FTMPWTRTRA YPHAFFVPEQ KKGGSYNYLT HVLFENIFWK GISGQVNKWR VEELDLPKTN
LYRLQQTRVP FLYNVSPAIL PPSVDFPDWI KVTGYWFLDE GSGDYKPPEE LVQFMKKASR
DKKKIVYIGF GSIVVKDAKS LTKAVVSAVR RADVRCILNK GWSDRLDNKD KNEIEIELPP
EIYNSGTIPH DWLFPRIDAA VHHGGSGTTG ATMRAGIPTI IKPFFGDQFF YATRIEDLGA
GIALKKLTAK TLGDALVKAT HDLKIIDKAK RVSQQIKHEH GVLSAIESIY SELEYSRNLI
LIKDIHNQNY KRHHPVPSGV QTPAYDTDSD DYDDDEDDDE SDKDDEEEEE ENSYDGYDGN
GVNNSPSQNS SN
