ATG26_NEOFI
ID ATG26_NEOFI Reviewed; 1418 AA.
AC A1CYS1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=NFIA_034590;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027686; EAW23891.1; -; Genomic_DNA.
DR RefSeq; XP_001265788.1; XM_001265787.1.
DR AlphaFoldDB; A1CYS1; -.
DR SMR; A1CYS1; -.
DR STRING; 36630.CADNFIAP00003624; -.
DR EnsemblFungi; EAW23891; EAW23891; NFIA_034590.
DR GeneID; 4592869; -.
DR KEGG; nfi:NFIA_034590; -.
DR VEuPathDB; FungiDB:NFIA_034590; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR OMA; YPDWIRI; -.
DR OrthoDB; 1024049at2759; -.
DR Proteomes; UP000006702; 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..1418
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000318044"
FT DOMAIN 249..288
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 289..387
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 733..799
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1375
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1418 AA; 158867 MW; 8CC8F82911C7D41D CRC64;
MRPFLDDAKR RVDRKLSASR QSLSTSRLLP SALPDRLKDN HDAQVDFTAP PGGSGSREGH
LQYMQQSIFG MIAAVGSRSD FHARFDESSD SDGESEQRPR KESSVRKGTS ASANTSSPLD
SSQRSSSRTD GKSEKESGTR GRRHPRTISD HKLFRPFESN SKHEPQTDPS TGDEMPNISP
PTRPRSATPR AAPILSRMVE AQAQFDLKAS STERSQPSLD ESGEKGPRGA SVSPLSTRLM
DMFGFDKPEK VLVEYACSLL QSILLQGYMY VTEGHICFYA YLPKKSTVAI KSGYLYKRGR
KNPKYSRYWF SLKGDVLSYY ADPSNLYFPS GHVDLRYGIS ASLGEAKEKG REPRDFQVTT
DQRTYYFRAD SSMSAKEWVK ALQKVIFRTH NEGESVKISF PIESIIDIEE SPMVDFAETF
KIRVIEDDDS YAIDEYFFTF FNSGREAFEF LRSLINDQSL KISSQHLSPQ PDRSPRSDPT
RKSRNRWSLT SGTSRVLGNS RAETQRKASA STSHTSLAHD VIKSSPATRH QDSSESILNS
FEQGTESSAA WQSMTDAAES ASQILNRSDV FQSPTIHGLD RRPSGGERRG RRNSDETARS
LSTRANVGTG QQIDELGRRM DGDTSGREAR DSTGESDQYT QDPTKSFSGA PSLNELVKAG
VYPLQRAAGL AEYLRTRSKQ MSNLLASESM GYIEKVSGMW TGGRKHYGEA EDVLPDDQDV
DPEDKEDGCN YGDRFRAHFA LPRTEKLQAT YFAYLHRVLP LYGKIYVSQK KLCFRSLIPG
TRTKMILPLR DIENVEKEKG FRFGYHGLVI IIRGHEELFF EFRTSDARDD CAVTLHQHLE
AVKFMAESGL LAEQEQNDSE AAMTEHRMLQ EARYDDYGEN DLRPLNESSE LHPIFDDPRA
SIVNFKPAES LRITCLTIGS RGDVQPYIAL CKGLLAEGHR PKIATHAEFE PWVRKHGIDF
APVEGDPAEL MRICVENGMF TYSFLKEASQ KFRGWIDDLL SSAWASCQDS DLLIESPSAM
AGIHIAEALR IPYFRAFTMP WSRTRAYPHA FAVPEHRMGG AYNYITYVMF DNVFWKAIAG
QVNRWRKNEL GLKATTLDKM QPNKVPFLYN YSPSVVPPPL DYPDWIRITG YWFLNEGSDW
TPPTALCEFI HRAREDGKKI VYIGFGSIVV SDPSALTKTV IESVRKADVR CILSKGWSDR
LGDPASAKPE VPLPPEIHQI QAAPHDWLFS HIDAAVHHGG AGTTGASLRA GVPTIIKPFF
GDQFFFGSRV EDLGVGICMK KLNVSVFSRA LWEATHSERM IIRAQDLGAR IRSEDGVATA
IQAIYRDLEY AKTLARQRSI ASSTPFSPTP SAKTTAEQDA DDDVEDSEEW TFVGDDTDME
MSRRLRDRAI SDADMLPDRL LANSVPGDSG PGRKLSGR
