ATG26_LEPMC
ID ATG26_LEPMC Reviewed; 1456 AA.
AC Q8NJS1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 81.
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 {ECO:0000303|Ref.1};
GN Name=ATG26 {ECO:0000250|UniProtKB:Q06321};
GN Synonyms=UGT51 {ECO:0000303|Ref.1};
OS Leptosphaeria maculans (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=5022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION.
RX DOI=10.1016/S0885-5765(03)00074-2;
RA Idnurm A., Warnecke D.C., Heinz E., Howlett B.J.;
RT "Characterization of neutral trehalase and UDP-glucose:sterol
RT glycosyltransferase genes from the plant pathogenic fungus Leptosphaeria
RT maculans.";
RL Physiol. Mol. Plant Pathol. 62:305-313(2003).
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; AF522873; AAM81359.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NJS1; -.
DR SMR; Q8NJS1; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
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 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; Repeat;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transferase; Transport.
FT CHAIN 1..1456
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000215612"
FT DOMAIN 236..283
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 287..384
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 774..840
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..197
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1456 AA; 162245 MW; 9D414C1416FCAB9C CRC64;
MASQDRGSDR TSRRLTKKRK DGKKPMRDVS LDMPERFKDG DDAHEDVTAP KGNHTMSMNQ
SIFSMIARAG QQSNTDLGTM QEVDSGDSDD EGTRNVPYHI LDGAARLSRL STANDFQKTS
GQTRDGKTEK GKHRRALSEN KLLRSLPKLK IASRKDARSD GQGADQMSSS QFLPPRPSPE
GSMPAPASSP PPPAAKGRVR PGDGIQMEKG RNVARKTRQR SPAAAATGEA PVSLAKRIQH
IFEFAQEEEV ISEYPCWLLQ SILLQGYMYI TQKHICFYAY IPKKHHDVSK TGYLSKRGRS
KHNRYWFILR GDVLAYYTNP AELYFPRNRI NLQYAISAEV LEPKRKGDEE TSFVVTTDER
TYQFKADSVA SAREWVKSIQ KVIFRTHNEG NSVKISLPIQ NVLEIEESSI LDFAETAKVR
VIDNDETFAI DEYFFSFFTK GQDALNVLRI MINDNEHHQA AQKPVEPPSR ALGQSDSGFM
ASTNAPSEVP HITENVRATL SPLTAPHVGR SSMSDISVRS SVDANRKNRD VRRSMDAGRT
LRRWSLEGRR LSHEAHRSPS PSGHDKTHKG RVGDRSPKSP RATDSDSATF SLDPGTESSA
AIQSMDDSTA SASQILDRSD LFRAPVVSSP NAFSNGVNMS AHSQDTTRSS APRPAYSKGT
HPTTSPSIDP LSPGAPDGEY DTDAGGATRL SGSSSALQDI ASYPLQKASG LAGFLRTRSK
KMGNLLAAES MGYYEKVSGM LAGGRKHYNT AEGLETDDQV NVYEDDEDAA KATDNFREHF
AFREDEVLQS SFFASLQRVL PNYGKIYISG RYFCFRSLMP TSKTKIILPM KDIENVNKEK
GFRLGYYGLA IVIRGHEELF FEFGKAEYRD ECAITVLRIL ENTKYLEDDQ SSSSGVDSND
EAAKAEHDLL QQAREDNNVD KTKNLSEIVR AAADDRIPLI FDDPLASFVD FKPPEPLTIV
CLTIGSRGDV QPYIALCKEL LKEGHKPRIA THAEFEPWVR KHGIDFAPVD GNPAELMRIC
VEHGMFTYNF MKEANSKFRG WLDDVCSSSW RACQGADVLI ESPSTMAGIH IAEALEIPYF
RAFTMPWTRT RAYPHAFSVL EKKMGGGYNS ITYITFDTIF WTAISGQINK WRRRELGLQN
TSQSKMQASL RPFLYNFSPH VVPPPLDWPD WVRVTGYWFL DEADTYEPPA DLVAFMDKAR
KDGKKLVYVG FGSIVIDDPA ALTKTVVDSV LKADVRCVLS KGWSDRLETK DASKPEIPLP
SEIFQIQSAP HDWLFKQMDA AVHHGGSGTT GASLRAGIPT IIKPFFGDQY FFAQRVEDMG
VGVWLKKVNT SVFSRALWEV TNSQRMIVKA RVLGQKIRKD NGTQVAIQTI YRELDRARSL
VKKHAKLDGE LSEEFEEDWT MVEDGEEIDV PHPFEVQQPV AGISQDASKM GGGSLVLGSM
VLKGAQKRSP ESAYRG
