ATG27_GIBZE
ID ATG27_GIBZE Reviewed; 348 AA.
AC I1RD82;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Autophagy-related protein 27 {ECO:0000303|PubMed:28894236};
DE Flags: Precursor;
GN Name=ATG27 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG01574, FGRAMPH1_01T03835;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28894236; DOI=10.1038/s41598-017-11640-z;
RA Lv W., Wang C., Yang N., Que Y., Talbot N.J., Wang Z.;
RT "Genome-wide functional analysis reveals that autophagy is necessary for
RT growth, sporulation, deoxynivalenol production and virulence in Fusarium
RT graminearum.";
RL Sci. Rep. 7:11062-11062(2017).
CC -!- FUNCTION: Effector of VPS34 phosphatidylinositol 3-phosphate kinase
CC signaling (By similarity). Regulates the cytoplasm to vacuole transport
CC (Cvt) vesicle formation (By similarity). Plays a role in ATG protein
CC retrieval from the pre-autophagosomal structure (PAS) and is especially
CC required for autophagy-dependent cycling of ATG9 (By similarity).
CC Autophagy is required for proper vegetative growth, asexual/sexual
CC reproduction, and full virulence (PubMed:28894236). Autophagy is
CC particularly involved in the biosynthesis of deoxynivalenol (DON), an
CC important virulence determinant (PubMed:28894236).
CC {ECO:0000250|UniProtKB:P46989, ECO:0000269|PubMed:28894236}.
CC -!- SUBUNIT: Forms a complex with ATG9 and ATG23 (By similarity).
CC {ECO:0000250|UniProtKB:P46989}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P46989}; Single-pass type I membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P46989};
CC Single-pass type I membrane protein {ECO:0000255}. Mitochondrion
CC membrane {ECO:0000250|UniProtKB:P46989}; Single-pass membrane protein.
CC Preautophagosomal structure membrane; Single-pass type I membrane
CC protein {ECO:0000255}. Note=Cycles among the pre-autophagosomal
CC structure (PAS), mitochondria and Golgi (By similarity).
CC {ECO:0000250|UniProtKB:P46989}.
CC -!- DISRUPTION PHENOTYPE: Does not significantly decrease the growth rate
CC under nutrient-rich conditions (PubMed:28894236).
CC {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the ATG27 family. {ECO:0000305}.
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DR EMBL; HG970332; CEF73723.1; -; Genomic_DNA.
DR RefSeq; XP_011317387.1; XM_011319085.1.
DR AlphaFoldDB; I1RD82; -.
DR STRING; 5518.FGSG_01574P0; -.
DR GeneID; 23549007; -.
DR KEGG; fgr:FGSG_01574; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G03835; -.
DR eggNOG; ENOG502S1VT; Eukaryota.
DR HOGENOM; CLU_047751_0_0_1; -.
DR InParanoid; I1RD82; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.70.130.10; -; 1.
DR InterPro; IPR018939; Autophagy-rel_prot_27.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR Pfam; PF09451; ATG27; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR PROSITE; PS51914; MRH; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Membrane; Mitochondrion; Protein transport;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..348
FT /note="Autophagy-related protein 27"
FT /id="PRO_5010124089"
FT TOPO_DOM 21..274
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P46989"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46989"
FT DOMAIN 24..255
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT REGION 180..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 26..69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 82..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 175..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ SEQUENCE 348 AA; 38518 MW; 0CE04CE26AC7218D CRC64;
MYRPDLLAFL LPLLAAPVFS AETLDCGKIR ADGHTFDLSK LGGPHSVVTT RYKPNPAGHY
NTTYTLDVCK PLKKSGGSKS ECPNGTRVCA ITHLLKSDGD KKEEDEVTDI VAIAGNLENA
GGSRFEWTPT RLSTAESDSD KKKEGLRLVL TGGKDPLSGP SKEKTDQKAI IEFLCDPNKE
GTEGEWVSEE KYEKRADEKK DDDKKEDGGD KDEGESTLEH QLKHENASLI WDGFEVEKDV
GILRLTWHTK YACEKRDESG GGGSDDGGDN SSSHWGFFTW FVLIAFLLIA GYLIFSSWIN
FTRYGARGWD LLPHSDTIRD IPYLLKDFIR RILNTVQGTG SRGGYSAV
