ATG26_EMENI
ID ATG26_EMENI Reviewed; 1396 AA.
AC Q5B4C9; C8V7T8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=AN4601;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACD01000079; EAA60403.1; -; Genomic_DNA.
DR EMBL; BN001303; CBF77171.1; -; Genomic_DNA.
DR RefSeq; XP_662205.1; XM_657113.1.
DR AlphaFoldDB; Q5B4C9; -.
DR SMR; Q5B4C9; -.
DR STRING; 162425.CADANIAP00005835; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR EnsemblFungi; CBF77171; CBF77171; ANIA_04601.
DR EnsemblFungi; EAA60403; EAA60403; AN4601.2.
DR GeneID; 2872399; -.
DR KEGG; ani:AN4601.2; -.
DR VEuPathDB; FungiDB:AN4601; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR InParanoid; Q5B4C9; -.
DR OMA; YPDWIRI; -.
DR OrthoDB; 1024049at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; 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; -; 2.
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; 1.
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..1396
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000215610"
FT DOMAIN 238..273
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 289..388
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 717..783
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1324..1346
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 48..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1396 AA; 157238 MW; C6C05DFB6B278F47 CRC64;
MRPFIDDAKR RAERRLSASR QSISARRMFA SSFPDRLKVD ADDAQMDYTA PPSSNDSRDG
MQYMQQSVMS LIAAVGSRTD LRARFDDSSD SEEETRTRPR FLSEKPFDQQ ITASPRADVT
LHVPSAPETR SSSRERGRRH RRSISEHKLF RPFKAGSASQ DKKQDASPDP GPSTSDRLSP
IPVLPRPRSA TPRAAPILSR MVEARALLET ENPEENPQTL EEKEQGVSKK SQVSPLSRQL
MEMFRFPTPE KVVVEYACSL LQSMLLQGYM YVTEGHICFY AYLPRQSTRV IKSGYIYKRG
RKNPKYNRYW FSLKEDVLSY YADPSNLYFP SGQIDLRYGI SASLTEPKDK SRESRDFQVT
TDHRTYYFRA DSSVNAKEWV RALQKVIFRT HNEGESIKVA FPIENILDVE ESPMVEFAQT
FKIRVVESEE TYAIDEHYFT FFDPDSGRRA FDLLKGLISG TPTRSPPGLS PLPDHTAQPR
RSRGSQNRWS LTSGSKSQVV STRRQRSAST SILGSGTGNE NSPQRQEDSS SSFFNSIDQV
TESSAVLQSI TDTTESASQI LNRSDVFQSP TIHTWQQRTS GTARSNRRHS DEITRSTTEH
GLDGISLARD GPEMQYTNSD SEQESKDASR LYSAVALNEI VKAGTYPLQR AAGLAGYLKS
RSKEMSNLLA TESMGYIEKV SGMWAGGRRH YGETDGLLPD DRALYPETAE ESLRDRERFR
AHFALPPTEK LEAAYFAYLH RALPLYGKIY ISQNRLCFRS LLPGTRTKMI LPLHDIENVE
KEKGFQFGYH GLVVVIRGHE ELFFEFNAAD ARDDCAVTLH QRLESAKFLV ESISLSQQET
DESEAAKVEH RMLQEARRNA SAEQDLRPGL SESSELHSIF DDPRASIVNF KPAEPLKITC
LTIGSRGDVQ PYIALCKGLL AEGHKPKIAT HAEFEPWVRK HGIDFAPVDG DPAELMRLCV
ENGMFTYSFL KEATAKFRGW IDDLLSSAWR ACQDSDLLIE SPSAMAGIHI AEALRIPYFR
GFTMPWSRTR AYPHAFAVPE SRLGGAYNYI TYVMFENVFW RAIAGQVNRW RMKELGLRAT
NLDKMQPNKV PFLYNFSPSV VPPPLDFPDW VRITGYWFLS ESSDWTPPRA LAEFIQCARQ
DGKKIVYIGF GSIVVSDPSA LTRTVVESVQ KADVRCILSK GWSARLGDPT STKVEIPLPP
EIHQIQSAPH DWLFSQIDAA AHHGGAGTTG ASLRAGVPTI IKPFFGDQFF FGNRVEDLGV
GICMKKLNVS VFSRALWTAT HDERMIVRAK QLGERIRSED GVATAIQAIY RDLEYATTLT
RQRSSISSTP FSPTPSTKTS DDQNANDDIA DIEDWTFIGD ESDLEFPRRA RERAVSGADN
IPERTILGSR SIYADS
