ATG26_ASPTN
ID ATG26_ASPTN Reviewed; 1396 AA.
AC Q0CKU4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=ATEG_05690;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476601; EAU33451.1; -; Genomic_DNA.
DR RefSeq; XP_001214868.1; XM_001214868.1.
DR AlphaFoldDB; Q0CKU4; -.
DR SMR; Q0CKU4; -.
DR STRING; 341663.Q0CKU4; -.
DR PRIDE; Q0CKU4; -.
DR EnsemblFungi; EAU33451; EAU33451; ATEG_05690.
DR GeneID; 4321815; -.
DR VEuPathDB; FungiDB:ATEG_05690; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR OMA; YPDWIRI; -.
DR OrthoDB; 1024049at2759; -.
DR Proteomes; UP000007963; 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..1396
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000318043"
FT DOMAIN 237..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 719..785
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..880
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..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1396 AA; 156512 MW; 0F29E96658D0B63D CRC64;
MRPLLDEAKR RVDRRLSASR QSLSTSRIFP SALPERLKDD HDAQVDYTAP PGGGGTKEGH
FQYMQQSIFG MIAAVGSQSD FHARFDDSSD SERDTDRPPQ KRTEKESQAT DAPPSSKNEK
KALRSPQRPK SPSQERGRRH RKTLSGSRIL RPLMPGSSQR QGGAQTEPST GNQMSRVPSP
ERPRSTTPRA APVLSRMVEA QALFDSKGSM NQSPRSPPAE TQEEQSQEQT SASPLSLRLM
EMFGFESPEK VLVEYACSLV QSMLLQGYMY VTEGHICFYA YLPRKSTVAI KSGYLYKRGR
KNPKYNRYWF SLKGDVLSYY ADPSNLYFPS GHIDLRYGIS ASLSEPKEKD REARDFQVTT
DQRTYYFRAD SSTSAKEWVK SLQKVIFRTH NDGDSVKISF PIESIIDIEE SPMVDFAETF
KIRAIESGET YAIDEYYFSF FNDGQDAFNF VKGLVSESQA KNPSRESPQP GRTTPQSRAR
GSRARWSLTS GLSQVLGSSD ARRRRSASAS QFSPGRDAAG LSPTSRQRDL SESFVNSFDQ
ATESSTVLQS MTDTAESASQ ILNRSDVFQY PAMQPFRRQS LSEDQFGRRH SDETARSTND
IARLGPGITP RDVQRFYPPS DSDHDAQDAA RVQQSASSLN ELVRAGAYPL QRAAGLAEYL
RNRSKQMGTL LASESMGYIE KVSGMWAGGR RHYGEAEGIL PDDQDVDPED KEDGCNHGDR
FRAHFALPPT EKLQATYFAY LHRVLPLYGK IYVSQKKLCF RSLLPGTRTK MILPLKDVEN
VEKEKGFRFG YHGLVVIIRG HEELFFEFNA ADVRDDCAVT IHQHLESVRF LSESGMLAEQ
EQDESEAAKA EHRMLQEARK DASGGLIPQT PSDESPEIHP IFDDPRASII NFKPTESLRI
TCLTIGSRGD VQPYIALCKG LLAEGHRPKI ATHAEFEPWI RKHGIDFAPV EGDPAELMRI
CVENGMFTYS FLKEASMKFR GWIDDLLSSA WRSCQDSDLL IESPSAMAGI HIAEALRIPY
FRAFTMPWTR TRAYPHAFAV PEHKMGGAYN YITYVMFDNV FWKAIAGQVN RWRQSELGLK
ATNLDKMQPN KVPFLYNYSP SVVVPPLDYP DWIRITGYWF LSEASDWTPP ADLMAFIQRA
RDDGKKLVYI GFGSIVVSDP SALTRTVVES VQKADVRCIL SKGWSDRLGD PASVKSEIPL
PPEIFQIQAA PHDWLFSQID AAAHHGGAGT TGASLRAGVP TIVKPFFGDQ FFFGTRVEDL
GVGICLKRLN VSLFSRALWE ATHSERMIVK ARNLGQQIRS EDGVATAIQA IYRDLEYAKT
LARQRSIVSS TPFSPTPSAK TVAEQEVDDD VTDSEEWTFI GDETDIDISR RVRGRAVSDV
DMLPEPLAVR SPELAQ
