ATG26_SCLS1
ID ATG26_SCLS1 Reviewed; 1435 AA.
AC A7ERM5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=SS1G_07979;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476630; EDN92117.1; -; Genomic_DNA.
DR RefSeq; XP_001591353.1; XM_001591303.1.
DR AlphaFoldDB; A7ERM5; -.
DR SMR; A7ERM5; -.
DR STRING; 665079.A7ERM5; -.
DR GeneID; 5487401; -.
DR KEGG; ssl:SS1G_07979; -.
DR VEuPathDB; FungiDB:sscle_11g081870; -.
DR InParanoid; A7ERM5; -.
DR OMA; YPDWIRI; -.
DR Proteomes; UP000001312; 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: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..1435
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000318048"
FT DOMAIN 211..258
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 262..360
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 760..826
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1435 AA; 160945 MW; B2BF72431A06DF92 CRC64;
MAPDDESKKR ATRKSTKRWK EEHQVATEIP ERFREGDDED EDCTAGHALN KSVFGMIAAA
SSIVDFNARF DAQSSDEEYD LGKPTRQSSE SHINRSSIDQ KMGKFEGHRR LLSESKILRS
FSRFSSRSKS KSSNTIARGS RTPSPLRESR QEPTSPEIRY SPLQPKDTPV MSRMLEARAE
LSLRPSFEMP RKSKDPAEVD DERTSPDSLA ERLMEIFKFE TPEDVLEEYP CWLMKSVLLQ
GYMYITTKHI CFYAYLPKKA NEVVKSGYLS KSGRHNPKYN RYWFRLKDDV LSYYTNPSDL
YFPSGNIDLR YGISASIVEK EKGKDSTHFT VETHQRKYNF NADSAPSAKE WVKALQKIIF
RSHNDGDSVK ISLPIENIID IEDSRIIDFA DTCKIRIIDN DETYAIDEYF FSFFTNGKLA
LSVLKILVGD TAAQKIPEEL LSPLSTADDS RGSSKRTSFQ VSRDRKLHGP SVQPNAPALE
ETVRATLSPL LAPGAGSPRA STDMSLSSSD IFRRSLDINK HGRRSIDLNR LTTEHHRSNS
ANSISTRRSL STNRLDQEKR TSKQGSSDSY VHSLEEPGSS EALPSASDET QASASQILRG
SDVFLSPTIQ HSPSVACNRN KDEIQGPKSR SLTSPIKSAD VSPTRTQRPQ HPKHAATTGS
VSDSNVGQAE ISSGPSLQSI VKAGSYPLQR AAGFAGYLNR HSKRMSTLLA SESMGYVEKV
SGMWKGGKKH YEEPHGIPRD NEMPSIGDDD DNRDGATPAD RFRDHFALPP DEKLHATYFG
YLQRVLPLYG KIYISDRSFC FRSLLPGTRT KFILPLKDIE NVDKEKGFRF GYSGLVITIR
GHEEIFFEFN QAENRDDCAI TLLQNVETMQ YMQDSGLLTM YERESAEMAG AEHRALIQAR
RGIRSEHDID MHKAADGGSQ SISFDDPRAS ILNFKPTEPL RITCLTIGSR GDVQPYIALC
KGLMAEGHQT KIATHLEFKE WIESHGIEFA PVDGDPAELM RICVENGMFT VSFLKEASSK
FRGWIDDLLS SSWRACQNSD ILIESPSAMA GIHIAEALRI PYFRAFTMPW TRTRAYPHAF
AVPEHKLGGS YNYVTYLMFD TVFWRAISGQ VNRWRQKELN LQATGLEKMQ PNKVPFLYNF
SPSVVVPPLD YSDWIRVTGY WFLDEGANYT PPKDLTDFIA NARADGKRLV YVGFGSIVVA
DSAVLTKTVV ASVLKADVRC ILSKGWSDRL EKKGANNVEI PLPPEIFQIK SAPHDWLFSQ
VDAAAHHGGA GTTGASLRAG IPTIIRPFFG DQFFFGQRVE DLGVGVLIKK INVSVFSRAL
WEATHSERII TKARVLGEQI RKENGVDTAI QSIYRDMEYA KSLIKCKEGK SDDDTLEDSE
ESWTFIGDDT DPELIKRFYD WESMAHSGTL SDKNMMAWSG SDVASAALSP TRKAA
