ATG26_ASPCL
ID ATG26_ASPCL Reviewed; 1406 AA.
AC A1CFB3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-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=ACLA_092600;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(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; DS027052; EAW11562.1; -; Genomic_DNA.
DR RefSeq; XP_001272988.1; XM_001272987.1.
DR AlphaFoldDB; A1CFB3; -.
DR SMR; A1CFB3; -.
DR STRING; 5057.CADACLAP00008281; -.
DR PRIDE; A1CFB3; -.
DR EnsemblFungi; EAW11562; EAW11562; ACLA_092600.
DR GeneID; 4705245; -.
DR KEGG; act:ACLA_092600; -.
DR VEuPathDB; FungiDB:ACLA_092600; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR OMA; YPDWIRI; -.
DR OrthoDB; 1024049at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
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:0032120; P:ascospore-type prospore membrane formation; IEA:EnsemblFungi.
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..1406
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000318039"
FT DOMAIN 236..286
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 286..385
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 730..796
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 83..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1406
FT /note="Disordered"
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 102..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1371
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1406 AA; 157611 MW; E9CFD7129621A573 CRC64;
MRPFLDDAKR RVDRRLSASK QSISTSRLLP SVLPDRFKDN HDAQVDFTAP PGGVGSREGH
MQYMQQSIFS MIAAVGSRSD FHARFDESSD SDGETEGRSQ TESPVKKVLG SSNPVNSQTE
QRSGSQTSRK SEKDQSSRGR HHRRTISDHK FLRPFKTSSK PEPDTEPSTG DERLRVTLPR
RPRSTTPRAA PILSRMVEAQ AQFDSKTPSA GRSQNSSQES SIHSSHESST SPLSTRLMEM
FDFNKPEKVL VEYACSLLQS MLLQGYMYVT EGHICFYAYL PRKSTVAIKS GYLHKRGRKN
PKYNRYWFSL KGDVLSYYAD PSNLYFPSGH VDLRYGISAS LAESKEKGRE PKEFQVSTDQ
RTYHFRADSS VSAKEWVKAL QKVIFRTHNE GDSVKVSFPI ENIIDIEESP MMDFADTFKI
RVVEDDDSYA IDEYFFSFFD SGREALTLLK SLVNENASGH SSRTLSPHAD RSPRSDRTRR
SRNRWSLTSG TSQPGNGSAD THRKRSASTS HLSLGPDAIP TSPVTRHQDP SESILNSFEQ
GTESSAVWQS MEDGAESASQ ILHRSDVFQS PTIHNLDKRA CSDERSGRRQ AGGTARSTLT
HVNANKDGSP GEYSKLGNDG KPDREIRHVI HELDQETQGP SKPGPGAPTL NELVKAGTYP
LQRAAGFAEY LRTRSKQMSN LLASESMGYI EKVSGMWVGG RRHYGEAEDV LPDDQAVDPE
DKEDGCNYGD RFRAHFALPS TEKLQATYFA YLHRVLPLYG KIYISQKKLC FRSLIPGTRT
KMILPLKDVE NVEKEKGFRF GYQGLVIIIR GHEELFFEFR TSDARDDCAV TLHQHLESVK
YLAESGLLAE QEKDESEAAM AEHRMLQEAR LDDYGENDIP PLNESSGLHP IFDDPRASIV
NFKPAESLRI TCLTIGSRGD VQPYIALCKG LLAEGHKPKI ATHAEFEPWV RRHGIDFAPV
DGDPAELMRI CVENGMFTYS FLKEASQKFR GWIDDLLSSA WASCQDSDLL IESPSAMAGI
HIAEALRIPY FRAFTMPWSR TRAYPHAFAV PEHKMGGAYN YITYVMFDNV FWKAIAGQVN
RWRKNELGLK ATTLDKMQPN KVPFLYNYSP SVVPPPLDYP DWIRITGYWF LNEGVDWTPP
VDLSAFIQRA REDDKKIVYI GFGSIVVSDP SALTRTVIES VQKADVRCIL SKGWSDRLGD
PSSAKTEVPL PPEIFQIQAA PHDWLFAQVD AAVHHGGAGT TGASLRAGIP TIIKPFFGDQ
FFFGSRIEDL GVGICMKKLN VSVFSRALWE ATHSERMIIR ARDLGAKIRD EDGVATAIQA
IYRDLEHAKT LAQQRSIASS TPFSPTPSAK NTAEQGDDDV EDSEEWTFVG DDNEMDMSRR
MRDRAISDAE MLPDRLLTNS IHGAGR
