ATG26_GLOLA
ID ATG26_GLOLA Reviewed; 1475 AA.
AC C4B4E5;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 51.
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:0000303|PubMed:19363139};
GN Name=ATG26 {ECO:0000303|PubMed:19363139};
OS Glomerella lagenarium (Anthracnose fungus) (Colletotrichum lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=5462;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19363139; DOI=10.1105/tpc.108.060996;
RA Asakura M., Ninomiya S., Sugimoto M., Oku M., Yamashita S., Okuno T.,
RA Sakai Y., Takano Y.;
RT "Atg26-mediated pexophagy is required for host invasion by the plant
RT pathogenic fungus Colletotrichum orbiculare.";
RL Plant Cell 21:1291-1304(2009).
CC -!- FUNCTION: Probable sterol 3-beta-glucosyltransferase that mediates
CC autophagic degradation of peroxisomes (pexophagy) (PubMed:19363139).
CC Also required for cytoplasm to vacuole transport (Cvt) and autophagic
CC degradation of mitochondria (mitophagy) and nuclei (nucleophagy) (By
CC similarity). However, is not essential for nonselective autophagy (By
CC similarity). Involved pathogenesis via peroxisome degradation inside
CC appressoria that are developing into the host invasion stage
CC (PubMed:19363139). {ECO:0000250|UniProtKB:Q06321,
CC ECO:0000250|UniProtKB:Q2U0C3, ECO:0000269|PubMed:19363139}.
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 infection-related pexophagy
CC (PubMed:19363139). {ECO:0000269|PubMed:19363139}.
CC -!- DISRUPTION PHENOTYPE: Leads to delayed autophagic degradation of
CC peroxisomes in the appressoria (PubMed:19363139).
CC {ECO:0000269|PubMed:19363139}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
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DR EMBL; AB365481; BAH60889.1; -; Genomic_DNA.
DR AlphaFoldDB; C4B4E5; -.
DR SMR; C4B4E5; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
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 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; Membrane; Protein transport;
KW Transferase; Transport.
FT CHAIN 1..1475
FT /note="Sterol 3-beta-glucosyltransferase"
FT /id="PRO_0000443925"
FT DOMAIN 270..315
FT /note="GRAM 1"
FT /evidence="ECO:0000255"
FT DOMAIN 318..413
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 798..901
FT /note="GRAM 2"
FT /evidence="ECO:0000255"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1475 AA; 165689 MW; D9F013674039EF26 CRC64;
MPPPPLSLPL HGPAGAASVT FAGDEDVKKR VGKKLQKKRH EPTTPAVELP ERLKEGDDAG
EEDLVPTQGP PMFMNMNQSI FGLIAAAGSR VDFHDRFESS DDESADEGPQ RDSADRSHSS
STHGLFLHRK QRRRDESDVA KTTVLNKDPY GSGKPEKHKR KISGHKLLRS LPALPRLPRH
KSKKESSKLE PPSEEASDGS GFAQSQPVDE AEDDEDDKDH RLAPVMSRML EAKAEMSARP
SFDVERFSSD QLTYSESADS NDTALARRLQ DIFEFDQPEA VIEEYPCWLL QSVLLQGYMY
ITAKHICFYS YLPKKALEVV KSGYLSKSGK RNPKYNRYWF RLKGDVLSYF KDPSNVYFPS
GQIDLRYGIS ASVTDKKDGL NFTVVTHHRT YHFRADSAPS AKEWVKSLQR VIFRSHNEGD
SVKISLPIEN VIDIEDTQML NFADTCKIRV IDNDETYAID EYFFSFFSFG KEAISVLKIL
IEDASSTAKD AARLKAVQEE EDRQQQQQQQ HPMQPPMQAS ARSSMSGSRR AIAPPKLTTN
KLPEAVKATL SPMSAHSPSA LSPRASMDAA RASFDAFRSF RRRSLDLSTI IRDSSPRRSF
SGNRRSMSRN RLDDQRRGPH QQGSTDSYVQ SSMEEPSFSG MVASSIEDPS ASQILRGSDV
FQNPTMRRSG SASRTEVEKQ QRRDPRSPPT LATYSGQHAA TAGSLNDGDK QPVTPTLQSI
TKMGAFPLQR VGAFAEYLNN TSSKLGSMLA TESMGYVEKV SGMWRGGRKH YDAPPEIKTD
DEDLYEDAEG KIQTSMDRFR AHFALPETEK LQATYFGHIL RVLPLYGKIY ISDKSFCFRS
LLPGTRTKLI LPLKDIENVD KEKGFRFGYS GLVVVIRGHE EIFFEFGQAE VRDDCAVTLL
QSLETTRYLE KIGDLDTEER EDEENAMAER DALKEARQTE EFHDHDVHLP KETSGVSDAP
TILFDDPKAS FLNFKPPQPL KITCLTIGSR GDVQPYIALC KGLLAEGHKP RIATHGEFKD
WIEGHGIEFA KVEGDPGELM RLCIENGTFT WAFLREANSM FRGWLDELLV SAWEACKGSD
LLIESPSAMA GIHIAEKLSI PYFRAFTMPW TRTRAYPHAF IMPEYKMGGA YNYMTYVMFD
NVFWKATAHQ VNRWRNNTLK LPNTSLEKMQ PNKVPFLYNF SEYVVAPPLD FSDWIRVTGY
WFLDEGSDWV PPQELTDFIA KARADEKKLV YVGFGSIIVN DTAKMTQEVI DAVLKADVRC
ILSKGWSDRM GKQGEEAVDQ PVMPPEIHVI KSAPHDWLFS QIDAAAHHGG SGTTGASLRA
GIPTIIRPFF GDQFFFGSRV EDIGVGICLK KWGAISFARA LWEATHNDRM IVKARVLGEQ
IRSENGVDSA IQCIYRDMEY AKSLIKRKAG KNIQVEPDED EESAEESWTF IGNDEPDPDM
TTKKLSEMPT LPGSSDTKPL GTRIMRVSPS QQSVA
