ATG22_GIBZE
ID ATG22_GIBZE Reviewed; 657 AA.
AC V6QX21;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Autophagy-related protein 22 {ECO:0000303|PubMed:28894236};
GN Name=ATG22 {ECO:0000303|PubMed:28894236};
GN ORFNames=FG012251, FGRAMPH1_01T03029;
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: Vacuolar effluxer which mediate the efflux of leucine and
CC other amino acids resulting from autophagic degradation (By
CC similarity). The release of autophagic amino acids allows the
CC maintenance of protein synthesis and viability during nitrogen
CC starvation (By similarity). Autophagy is required for proper vegetative
CC growth, asexual/sexual reproduction, and full virulence
CC (PubMed:28894236). Autophagy is particularly involved in the
CC biosynthesis of deoxynivalenol (DON), an important virulence
CC determinant (PubMed:28894236). {ECO:0000250|UniProtKB:P25568,
CC ECO:0000269|PubMed:28894236}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P25568};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P25568}.
CC Note=Vacuole and punctate structures (By similarity).
CC {ECO:0000250|UniProtKB:P25568}.
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 ATG22 family. {ECO:0000305}.
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DR EMBL; HG970332; CEF73316.1; -; Genomic_DNA.
DR RefSeq; XP_011316999.1; XM_011318697.1.
DR AlphaFoldDB; V6QX21; -.
DR STRING; 5518.FGSG_01225P0; -.
DR GeneID; 23548674; -.
DR KEGG; fgr:FGSG_01225; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G03029; -.
DR eggNOG; ENOG502QR9I; Eukaryota.
DR HOGENOM; CLU_017518_1_1_1; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032974; P:amino acid transmembrane export from vacuole; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR CDD; cd17483; MFS_Atg22_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR044738; Atg22.
DR InterPro; IPR024671; Atg22-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF11700; ATG22; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Autophagy; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..657
FT /note="Autophagy-related protein 22"
FT /id="PRO_0000443921"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..155
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..212
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..349
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..409
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..481
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..554
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 576..583
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..657
FT /note="Vacuolar"
FT /evidence="ECO:0000305"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 657 AA; 72241 MW; 800F835FB87CCD09 CRC64;
MAPNLQPQPQ SQLQRPRLKD HRPWSGLSNI SKRSFRSCAT SAFEADDERS SSDGDMSPRN
SEADLRRPVV PRHFGHDARP TSRRELLGWY AYAFAAETYV ICGIASFIPI LLETLARENG
VLVSDRKTPC GSSDSKNDGD GQCIVWVFGM EINTASFAMY TFSVSVLVQA LLVVSISCAA
DHGNYRKKLL LTFAWIGSFA VMSYIFITKD NYILGALLTV ISNTSFGASF VLLNSFLPLL
VRYHPDVIEA NVATTPDLGS SEFESRPLDQ SVGQLESSPV TATSPLLHPE DGGRLKPTAS
HAEITSKELE LSTRISAIGI GTGYIAALFL QCICIGVLIS LHNTTWGQRV VLFMVGVWWT
VFTIPAAMWL RPRPGPPLAD NGRKGIMAGL AYILYAWKSL FKTIQQARRL LDIVLFLAGW
FLLSDAIATT SSTAILFAKT QLHMKPWALG MINVISTTAG VFGAFGWSWV SRLFNLKAHQ
TILVCIALFE LIPLYGLLGY LPFVKNWGVF GLQQPWEMYP LAAVYGVVLG GLSGYCRSLY
GELIPPGSEA AFYALYAITD KGSSVFGPTI VGAIIDRTGT IRPAFWFLAV LVGFPAPLIW
FIDVERGRRE GAKLAKSITD SIVQEEDESD DGAERRGMLS DYEREHGQSI DDERAGR
