ATG26_ASPFU
ID ATG26_ASPFU Reviewed; 1405 AA.
AC Q4WID6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 117.
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=AFUA_2G02220;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL87319.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAHF01000008; EAL87319.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_749357.1; XM_744264.1.
DR AlphaFoldDB; Q4WID6; -.
DR SMR; Q4WID6; -.
DR STRING; 746128.CADAFUBP00001883; -.
DR GeneID; 3507158; -.
DR KEGG; afm:AFUA_2G02220; -.
DR VEuPathDB; FungiDB:Afu2g02220; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR InParanoid; Q4WID6; -.
DR OrthoDB; 1024049at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
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..1405
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000318040"
FT DOMAIN 246..285
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 285..384
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 724..790
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
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..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1366
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1405 AA; 157749 MW; EDF70E3002C995D4 CRC64;
MRPFLDDAKR RVDRKLSARR QSLSASRFLP SALPDRLKDN HDAQVDFTAP PGGSGSREGH
LQYMQQSIFG MIAAVGSRSD FHARFDESSD SDGETGQRPR KESSVRKGTS VSVNTSSLDP
SQRSSSQTDG NSEKDLGTRG RRHRRTISDH KLLRPFMSNS KHEPDPSTGD EMPTVSPPSR
PRSATPRAAP ILSRMVEAQA QFDLKASSTE RSQSSLNETG AKGPRDASVS PLSTRLMDMF
GFDKPEKVLV EYACSLLQSM LLQGYMYVTE GHICFYAYLP KKSTVAIKSG YLHKRGRKNP
KYSRYWFSLK GDVLSYYADP SNLYFPSGHV DLRYGISASL GDPKEKGREP RDFQVTTDQR
TYYFRADSAM SAKEWVKALQ KVIFRTHNEG ESVKISFPIE SIIDIEESPM VDFAETFKIR
VIEDDDSYAI DEYFFTFFNS GREAFEFLKI LINDQSLKIS SQHLSPQPDR SPRSDRTRKS
RNRWSLTSGT SRAETQRKRS ASTSHMSLAH DIVKSSPATR HQDSSDSILN SFEQATESSA
AWQSITDAAE SASQILNRSD VFQSPTIYGL DRRPSGRERR GRRNSDETAR SPSTRVNVGT
GQQIDELDRR TDGNTSGREA RDTTSESDQY TQDPTKSFSG APSLNELVKA GVYPLQRAAG
LAEYLRTRSK QMSNLLASES MGYIEKVSGM WTGGRKHYGE AEDVLPDDQD VDPEDKEDGC
NYGDRFRAHF ALPPTEKLQA TYFAYLHRVL PLYGKIYVSQ KKLCFRSLIP GTRTKMILPL
RDIENVEKEK GFRFGYHGLV IIIRGHEELF FEFRTSDARD DCAVTLHQHL EAVKFMAESG
LLAEQEQNES EAAMTEHRML QEARYYDYGE NDLRPLNESS ELHPIFDDPR ASIVNFKPAE
SLRITCLTIG SRGDVQPYIA LCKGLLAEGH RPKIATHAEF EPWVRKHGID FAPVEGDPAE
LMRICVENGM FTYSFLKEAS QKFRGWIDDL LSSAWASCQD SDLLIESPSA MAGIHIAEAL
RIPYFRAFTM PWSRTRAYPH AFAVPEHRMG GAYNYITYVM FDNVFWKAIA GQVNRWRKNE
LGLKATTLDK MQPNKVPFLY NYSPSVVPPP LDYPDWIRIT GYWFLNEGSD WTPPTALSEF
IHRAREDGKK IVYIGFGSIV VSDPSALTKT VIESVLKADV RCILSKGWSD RLGDPASAKP
EVPLPSEIHQ IQAAPHDWLF SHIDAAVHHG GAGTTGASLR AGVPTIIKPF FGDQFFFGSR
VEDLGVGICM KKLNVSVFSR ALWEATHSER MIIRAQDLGA RIRSEDGVAT AIQAIYRDLE
YAKTLARQRS IASSTPFSPT PSAKTAAEQD ADDDVEDSEE WTFVGDDTDV EMSRRLRDRA
ISDADMLPDR LLANSVPGDS GPGRN
