ATG26_PENRW
ID ATG26_PENRW Reviewed; 1374 AA.
AC A7KAN4; B6GYP9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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}; ORFNames=Pc12g16190;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=17204848; DOI=10.4161/auto.3595;
RA Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT "ATG genes involved in non-selective autophagy are conserved from yeast to
RT man, but the selective Cvt and pexophagy pathways also require organism-
RT specific genes.";
RL Autophagy 3:106-116(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
CC -!- FUNCTION: Probable sterol 3-beta-glucosyltransferase that mediates
CC autophagic degradation of peroxisomes (pexophagy) (By similarity). Also
CC required for cytoplasm to vacuole transport (Cvt) and autophagic
CC degradation of mitochondria (mitophagy) and nuclei (nucleophagy) (By
CC similarity). {ECO:0000250|UniProtKB:Q2U0C3}.
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 Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q2U0C3};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q2U0C3}.
CC -!- DOMAIN: The GRAM and PH domains are required for the localization of
CC ATG26 to the preautophagosomal structure (PAS) and are involved in
CC autophagy (By similarity). {ECO:0000250|UniProtKB:Q2U0C3}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
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DR EMBL; EF110900; ABO31321.1; -; Genomic_DNA.
DR EMBL; AM920427; CAP81246.1; -; Genomic_DNA.
DR RefSeq; XP_002558417.1; XM_002558371.1.
DR AlphaFoldDB; A7KAN4; -.
DR SMR; A7KAN4; -.
DR STRING; 1108849.XP_002558417.1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR EnsemblFungi; CAP81246; CAP81246; PCH_Pc12g16190.
DR GeneID; 8306628; -.
DR KEGG; pcs:Pc12g16190; -.
DR VEuPathDB; FungiDB:PCH_Pc12g16190; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR OMA; YPDWIRI; -.
DR OrthoDB; 1024049at2759; -.
DR BioCyc; PCHR:PC12G16190-MON; -.
DR Proteomes; UP000000724; Contig Pc00c12.
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; -; 3.
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; 2.
DR Pfam; PF00169; PH; 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..1374
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000318045"
FT DOMAIN 234..283
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 285..382
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 704..770
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1374 AA; 153587 MW; 1ED04830463732DF CRC64;
MRPLRDDAKR RADRQLSASM KPTSSNRPFS DRVPDRFKDG DDAQFDFTAP PRGMGSRDGN
VHYMQQSLFS MIAAVGSKSD FHARFDESSD SDGEMEEQPR VEQTTGKASS RTPPVPSLDP
RQPSKRSEPS KLVLEERGRR HQRACSDNKL LQRLPKSDAE GGVNESSNQS DSLLKVPPLR
RTRSATPRAA PVLSRMVEAQ SHFDLTSATP YLPPNNPDKS MEDQPQSSAS ALSMRLMKMF
EFAKPEKVLV EYACSLLQSM LLQGYMYVTE GHICFYAYLP KKSNVAIKSG YLSKRGRKNP
KYHRYWFALK GDVLSYYADP SNLYFPSGHV DLRYGISASL TERKDGDAKD FQVTTDQRTY
LFRADSATSA KEWVKALQQV IFRTHNEGDS VKVSFPIANV IDLEESPMAD FAETFKIRVI
DSGETYAIDE YFFSFFDSGQ DAFNYIKGLV NAVSTTTATK EAQDQHDIKH QPESSRTAYK
RQSVSSVRVS DQRREDSPRK RSSSVGNENQ GSADSFAEQG TGSSPIIQSM TDTTESASQI
LHRSDVFQAP TMRTLQGRSL DVGESIRRYS DDTTPSASAR LDLDAAVGSP CGTLGHNETT
EDARYATGQS DLMQSSRPSS VTQLNELVKA GVYPLQRAAG FAEYLKSRSK QMSTLLATES
MGYIEKVSGM WIGGQKHYGE REGPLLEDQN VDPEDNEGSF NYGDRFRAHF ALPPTEKLQA
TYYAYLHRVL PLYGKIYISQ KKLCFRSLIP GTRTKMILPF KDIENVEKEK GFRFGYHGLV
VIIRGHEELF FEFNASDSRD DCAVTLHQNL ESVKFLVESG LLAEDERDEV EAAKAEHRML
EEARLDSPEG HDAPPTLTED SSEIHPFFDD PRASIINFKP PEPLRITCLT IGSRGDVQPY
IALCKGLLAE GHKPKIATHA EFEPWIRKHG IDFAPVDGDP AELMRICVEN GMFTYSFLRE
ASLKFRGWID DLLSSAWIGC QGSDLLIESP SAMAGIHIAE ALRIPYFRGF TMPWTRTRAY
PHAFAVPENR MGGAYNYITY VMFDNIFWKA IAGQVNRWRN NELGLKATTL DKMQQNKVPF
LYNYSPSVVA PPLDYPDWIR ITGYWFLNEG TDWTPPTELS NFIAQARSDG KKLVYIGFGS
IVVSDPSALT RTVIESVLKA DVRCILSKGW SDRLGDPAST KTEIPLPPEI LQIQSAPHDW
LFSQIDAAAH HGGAGTTGAS LRAGVPTIVK PFFGDQFFFG SRVEDLGVGI CMKKLNVSVF
SRALWEATHS ERMIVKARNL GIQIRNEDGV ATAIQALYRD LEYAKTLARQ KSLASSTPFS
PTPTAKASPD GGDDDLDDIE EWTFVGDETG FDIAKRMRER AASDADRIGS NMFQ
