ATG23_GIBZE
ID ATG23_GIBZE Reviewed; 1139 AA.
AC I1RGD4; A0A098DHN2;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Autophagy-related protein 23 {ECO:0000303|PubMed:28894236};
GN Name=ATG23 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG02793, FGRAMPH1_01T11327;
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: Required for cytoplasm to vacuole transport (Cvt) vesicle
CC formation and efficient autophagy (By similarity). Plays a role in ATG
CC protein retrieval from the pre-autophagosomal structure (PAS) and is
CC especially required for autophagy-dependent cycling of ATG9 (By
CC similarity). Autophagy is required for proper vegetative growth,
CC asexual/sexual reproduction, and full virulence (PubMed:28894236).
CC Autophagy is particularly involved in the biosynthesis of
CC deoxynivalenol (DON), an important virulence determinant
CC (PubMed:28894236). {ECO:0000250|UniProtKB:Q06671,
CC ECO:0000269|PubMed:28894236}.
CC -!- SUBUNIT: Forms a complex with ATG9 and ATG27 (By similarity).
CC {ECO:0000250|UniProtKB:Q06671}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06671}.
CC Preautophagosomal structure membrane {ECO:0000250|UniProtKB:Q06671};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q06671}. Note=Found
CC in pre-autophagosomal structure and other punctate structures (By
CC similarity). Correct localization of ATG23 to the membranes is strictly
CC dependent of ATG9 (By similarity). Cycling through the pre-
CC autophagosomal structure and correct location to other punctate
CC structures is ATG1- and ATG13-dependent (By similarity).
CC {ECO:0000250|UniProtKB:Q06671}.
CC -!- DISRUPTION PHENOTYPE: Significantly decreases the radial growth of
CC colonies under nutrient-rich conditions (PubMed:28894236).
CC {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the ATG23 family. {ECO:0000305}.
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DR EMBL; HG970333; CEF77466.1; -; Genomic_DNA.
DR RefSeq; XP_011323020.1; XM_011324718.1.
DR AlphaFoldDB; I1RGD4; -.
DR SMR; I1RGD4; -.
DR STRING; 5518.FGSG_02793P0; -.
DR GeneID; 23550151; -.
DR KEGG; fgr:FGSG_02793; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G11327; -.
DR eggNOG; ENOG502S0A5; Eukaryota.
DR HOGENOM; CLU_002906_0_0_1; -.
DR InParanoid; I1RGD4; -.
DR Proteomes; UP000070720; Chromosome 2.
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 InterPro; IPR000237; GRIP_dom.
DR Pfam; PF01465; GRIP; 1.
DR SMART; SM00755; Grip; 1.
DR PROSITE; PS50913; GRIP; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Cytoplasm; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1139
FT /note="Autophagy-related protein 23"
FT /id="PRO_0000443922"
FT DOMAIN 1082..1132
FT /note="GRIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00250"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 142..170
FT /evidence="ECO:0000255"
FT COILED 215..259
FT /evidence="ECO:0000255"
FT COILED 323..495
FT /evidence="ECO:0000255"
FT COILED 566..1067
FT /evidence="ECO:0000255"
FT COMPBIAS 14..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 127843 MW; 2241F44AEC40EF4F CRC64;
MFQRFKSAID RTIAEEQARQ QTATQSRSPS RTGSTSSRKG DGTPGQRVKS RKQASDAGDA
PNPDPAVFEA AFVIDDSDEP SRAATPLPPN AADEKKSDNT NGQGNMPEDK TPEGQGANDE
GSADKAQDGA TDAPATKPQA PKLQEMSPEI RQKLRKLEKL EATYPELLRS YRVAHRRATA
IEPFEKALRE NTPLTSISDP EALVEYLNQV NLRSDMVMQE LKKVSTDKDE LQKKYNEAEE
KAKKLEEELV AVRSASTDQP KTSDSETSKD AQDGKNGATS PEDPEKSKSP VSSVMGMFSP
KHKPQKSLGE VAETKESNEE FFSYDDEIPQ LQADVASKSE EIEKLKSEVE DLQKELTTAR
ETSTGLVESL ENATRELSKT RDVASVKDSL QAQLDDRNKE ITSLNQRLEE VQKQLKQLEE
DKNAHTAKVD ELEVSLASSD KRTSELDAEL AKASNAKNIS KKLIDDLNNQ IETLKNEKSD
SQTKITDLTK KLESKPAPAM LTPAATPMPT VLQPAATSAT AASGGGKKKN NKKKKGKGGV
GGAVAPSQAP TAGDPVETPE PVITTDTAGN AELKAEIVKL KEEVAEKDTQ IDRLSKRRKT
EEDLREEIES LQENILMIGQ DHVEAKDKIK ELEAEKLELK TQITDLEKKI SSSTSDAEAS
SKMQSEMESI KTEYSDLKEK TSTLQADLGA AQQLAQNRFK DLTELREVLQ KAQPELKSLR
QESATLKATK EELANKTKEL RDMEKREKDL KRDVERAQKI SSDRETEIKS LQEKLTVETN
AKLRLEDAQR VSGRDLRRSE AEKVEISGRA DKAEQELQSV QEELSKLRPK VKELEEQMHK
LKREKAASQE EADFKTQQYS NAQGLLSSMR DQTAEMSVQL KESKSQAESL EEELAEVQRL
LQERTREGET MRRLLADVDE RADNKVRDMR ARMEAAVEER DRIEDESATL ARRKTRETED
LKQKLKDLER EVKTLTHERD ELEQREKEWR KRREELESVE EKAEAETDEL RTTASQLRTA
LDASEKQVRD VEKQRAELRR MLEESRQRYE KLSKDLKAAQ TKLVASSSRS SFDSVRSGSN
GSPAGAPDTV YLKTILLQFL EQKDTKLRAQ LVPVLGKLLR FDKTDEQKWQ KAVQHIEVK
