ID   ATG26_KOMPG             Reviewed;        1211 AA.
AC   Q9Y751; C4R718;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 115.
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 {ECO:0000250|UniProtKB:Q06321};
DE   AltName: Full=Peroxisome degradation protein 3;
DE   AltName: Full=Pexophagy zeocin-resistant mutant protein 4 {ECO:0000303|PubMed:11856375};
DE   AltName: Full=UDP-glycosyltransferase 51 {ECO:0000303|PubMed:10224056};
GN   Name=ATG26 {ECO:0000250|UniProtKB:Q06321};
GN   Synonyms=PAZ4 {ECO:0000303|PubMed:11856375}, PDG3,
GN   UGT51 {ECO:0000303|PubMed:10224056}, UGT51B1;
GN   OrderedLocusNames=PAS_chr4_0167;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
RN   [3]
RP   FUNCTION.
RX   PubMed=11856375; DOI=10.1046/j.1356-9597.2001.00499.x;
RA   Mukaiyama H., Oku M., Baba M., Samizo T., Hammond A.T., Glick B.S.,
RA   Kato N., Sakai Y.;
RT   "Paz2 and 13 other PAZ gene products regulate vacuolar engulfment of
RT   peroxisomes during micropexophagy.";
RL   Genes Cells 7:75-90(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=14585290; DOI=10.1016/j.cellbi.2003.08.004;
RA   Stasyk O.V., Nazarko T.Y., Stasyk O.G., Krasovska O.S., Warnecke D.C.,
RA   Nicaud J.-M., Cregg J.M., Sibirny A.A.;
RT   "Sterol glucosyltransferases have different functional roles in Pichia
RT   pastoris and Yarrowia lipolytica.";
RL   Cell Biol. Int. 27:947-952(2003).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX   PubMed=12839986; DOI=10.1093/emboj/cdg331;
RA   Oku M., Warnecke D.C., Noda T., Mueller F., Heinz E., Mukaiyama H.,
RA   Kato N., Sakai Y.;
RT   "Peroxisome degradation requires catalytically active sterol
RT   glucosyltransferase with a GRAM domain.";
RL   EMBO J. 22:3231-3241(2003).
RN   [6]
RP   FUNCTION.
RX   PubMed=19605559; DOI=10.1091/mbc.e09-03-0221;
RA   Nazarko T.Y., Farre J.C., Subramani S.;
RT   "Peroxisome size provides insights into the function of autophagy-related
RT   proteins.";
RL   Mol. Biol. Cell 20:3828-3839(2009).
CC   -!- FUNCTION: Probable sterol 3-beta-glucosyltransferase that mediates
CC       autophagic degradation of peroxisomes (pexophagy) (PubMed:11856375,
CC       PubMed:14585290, PubMed:12839986, PubMed:19605559). Also required for
CC       cytoplasm to vacuole transport (Cvt) and autophagic degradation of
CC       mitochondria (mitophagy) and nuclei (nucleophagy) (By similarity).
CC       {ECO:0000250|UniProtKB:Q2U0C3, ECO:0000269|PubMed:11856375,
CC       ECO:0000269|PubMed:12839986, ECO:0000269|PubMed:14585290,
CC       ECO:0000269|PubMed:19605559}.
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;
CC         Evidence={ECO:0000305|PubMed:10224056};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12839986}.
CC       Preautophagosomal structure membrane {ECO:0000269|PubMed:12839986};
CC       Peripheral membrane protein {ECO:0000269|PubMed:12839986}.
CC   -!- DOMAIN: The first GRAM domain is required for association with the
CC       micropexophagic apparatus (PubMed:12839986).
CC       {ECO:0000269|PubMed:12839986}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; AF091397; AAD29570.1; -; Genomic_DNA.
DR   EMBL; FN392322; CAY71393.1; -; Genomic_DNA.
DR   RefSeq; XP_002493572.1; XM_002493527.1.
DR   AlphaFoldDB; Q9Y751; -.
DR   SMR; Q9Y751; -.
DR   STRING; 644223.Q9Y751; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   EnsemblFungi; CAY71393; CAY71393; PAS_chr4_0167.
DR   GeneID; 8201077; -.
DR   KEGG; ppa:PAS_chr4_0167; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_000537_6_0_1; -.
DR   InParanoid; Q9Y751; -.
DR   OMA; WCNNITK; -.
DR   BRENDA; 2.4.1.173; 4827.
DR   Proteomes; UP000000314; Chromosome 4.
DR   GO; GO:0034045; C:phagophore assembly site 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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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   Autophagy; Cytoplasm; Glycosyltransferase; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Protein transport; Reference proteome; Repeat;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transferase; Transport.
FT   CHAIN           1..1211
FT                   /note="Sterol 3-beta-glucosyltransferase"
FT                   /id="PRO_0000215614"
FT   DOMAIN          196..235
FT                   /note="GRAM 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          248..347
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          586..652
FT                   /note="GRAM 2"
FT                   /evidence="ECO:0000255"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          500..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..523
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1211 AA;  136364 MW;  7C3CF0FC7A7C3822 CRC64;
     MSQLRPRDSS AGKSSSPRRT DRNPESIDVN SKGGSEGMTS GLVPGTAPHK EDETEAEDDI
     DCGRLITSKS LATMLTTASM YAGVSQLDDD AIESSALDEP IPYVPYEEDA ESVMSESTVG
     VDTVRDTDSS EQINPEIDGL VALRKKQQHT LSKFELSVVR KRCSQLSLAG SSSGSTRRNS
     FTLDNNETTR AVKLCEKLKT TFDLSDDDEF VNDYPCWLLH EVFLQGHIYI TSRYLLYFAF
     LPKRDSTVTM SGALSIRSST TMRFSVRRWA VLKGNYFRLY ANSTERYFPS LNIDLRFLLK
     VELSNPNLEE NKPTVFKLIT EARTHYFQAD SLDNARSWVT DLRKHIFTAK NSGGHVTIKV
     PLENILDLSI ETLFEASQTL KLKVLESEES YAIDDYYFMF FNNGDQVLDS IRQSMKALGI
     ELTDSDSSES DSDVSGSETN GRSTHRKSKL SRSLSVLTPI PRGIGSIYKP IKSSASGIIG
     AIKKPQKSAT RPFSSVVETV VPNDNDSELK QDHAGDAPKD SEEPSTKPSN WSAKSLVQGF
     LSTTSSISQS MLFASPMHYN NQLFIERGEE DPYFVTNKEE REVAQSRFRK HFSLPDSEEL
     LASYFCHFQK NIPVYGKVYL GTTCICYRSL FPGTNTTMIL PYSDIENVYN LKGFRFGYSG
     LVIVIRAHEE LFFEFGSNES RDDCDLFLLK QLDFTKSHKN AHSEQKRKRN DSIKLAESVQ
     LADARLRYFE TRIESDIGRE VPIILEENQY STSEIRSKRR YKFVLLTIGS RGDVQPYISL
     AKGLLAENHK VKIVTHEEFK PWVESYGIEF ATIAGNPAEL MSLMVTHKSL SVGFLKEAKE
     KFTGWIGELL QSSWDACQDA DVLIESPSAM AGIHIAEKLQ IPYFRAFTMP WTRTRAYPHA
     FVVPEQKRGG SYNYLTHIIF ENVFWKGISG EVNKWREQVL MLPKTNLERL EQNKVPFLYN
     VSPTVFPPSM DFPHWVKVVG YWFLDEGEAD SYDPPKPLLE FMEKAKTDGK KLVYIGFGSI
     VVSDPKQLTE AVIDAVLSAD VRCILNKGWS DRLGKQTGVE VELPEEIYNS GNVPHDWLFG
     KIDASVHHGG SGTTGATLRA GIPTIIKPFF GDQFFYANRV EDIGVGIGLR KLNSKSLSKA
     IKEVTTNTRI IEKAKEIGKQ IQSENGVSAA IRCLYQEMEY AKKLSKSKQK YWDNQSEDIS
     DDSVSGSWFE V