ATG2_GIBZE
ID ATG2_GIBZE Reviewed; 2182 AA.
AC I1S0P7; A0A098DCH7; A0A1C3YJ58;
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 2 {ECO:0000303|PubMed:28894236};
GN Name=ATG2 {ECO:0000303|PubMed:28894236}; ORFNames=FGRAMPH1_01T07725;
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: Lipid transfer protein required for autophagosome completion
CC and peroxisome degradation and peroxisome degradation (By similarity).
CC Tethers the edge of the isolation membrane (IM) to the endoplasmic
CC reticulum (ER) and mediates direct lipid transfer from ER to IM for IM
CC expansion (By similarity). ATG2 binds to the ER exit site (ERES), which
CC is the membrane source for autophagosome formation, using basic
CC residues in its N-terminal region (NR) and to the expanding edge of the
CC IM through its C-terminal region (By similarity). The latter binding is
CC assisted by an ATG18-PtdIns3P interaction (By similarity). ATG2 then
CC extracts phospholipids from the membrane source using its NR and
CC transfers them to ATG9 to the IM through its predicted beta-sheet-rich
CC structure for membrane expansion (By similarity). Autophagy is required
CC for proper vegetative growth, asexual/sexual reproduction, and full
CC virulence (PubMed:28894236). Autophagy is particularly involved in the
CC biosynthesis of deoxynivalenol (DON), an important virulence
CC determinant (PubMed:28894236). {ECO:0000250|UniProtKB:P53855,
CC ECO:0000269|PubMed:28894236}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:O94649};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:O94649};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:O94649};
CC -!- SUBUNIT: Interacts with ATG18 (By similarity).
CC {ECO:0000250|UniProtKB:P53855}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:P53855}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53855}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P53855}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53855}.
CC -!- DISRUPTION PHENOTYPE: Does not significantly decrease the growth rate
CC under nutrient-rich conditions (PubMed:28894236). Causes only mild
CC infection in point-inoculated spikelets of flowering wheat heads and
CC impairs the spreading to nearby spikelets (PubMed:28894236). Reduces
CC strongly the production of deoxynivalenol (DON), an important virulence
CC determinant (PubMed:28894236). {ECO:0000269|PubMed:28894236}.
CC -!- SIMILARITY: Belongs to the ATG2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=SCB64594.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HG970332; SCB64594.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_011319240.1; XM_011320938.1.
DR AlphaFoldDB; I1S0P7; -.
DR STRING; 5518.FGSG_10283P0; -.
DR GeneID; 23557195; -.
DR KEGG; fgr:FGSG_10283; -.
DR eggNOG; KOG2993; Eukaryota.
DR HOGENOM; CLU_000626_1_0_1; -.
DR InParanoid; I1S0P7; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030242; P:autophagy of peroxisome; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR026849; ATG2.
DR InterPro; IPR026885; ATG2_CAD_motif.
DR InterPro; IPR026886; ATG2_fungi/plants.
DR InterPro; IPR015412; Autophagy-rel_C.
DR PANTHER; PTHR13190; PTHR13190; 2.
DR PANTHER; PTHR13190:SF1; PTHR13190:SF1; 2.
DR Pfam; PF13329; ATG2_CAD; 1.
DR Pfam; PF09333; ATG_C; 1.
PE 3: Inferred from homology;
KW Autophagy; Endoplasmic reticulum; Lipid transport; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..2182
FT /note="Autophagy-related protein 2"
FT /id="PRO_0000443866"
FT REGION 291..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2182 AA; 239159 MW; 37C356C914271B2F CRC64;
MATFFQSFRS SSMPKRLLRY ALSRLELLDA DALEMDNLDL AIGRNTVFEF RDVGIKLKKL
NKLLQLPDTF KLKKAKVLLL RVTIPMDFYT SPIIVEVDGV DIALQVIGNE SKPSRSPGTR
TPDESVAVPN TVDLAQSFLE TQPKSERRKL EDALAAESQD LGASVSMSDD GSEDDLAYGT
GQALSLPAFL ADFLQGIVDR MQVRIKGVNF QLDVEVLVEP SSTTNEMVSF QVALEGIDVE
GVTTRSYDDA GFPTIVHKEG KRHVSLSNVR AYLISEANVF SALAKSPSIA SPSLASSPAM
TRNPPSRQAT ELSLASLRDE PVSSSQASIR SNEPESASHH SLPENDHILS SQHSIDQRLE
SSLRQSLQRK DPLADSHESL QDDYFMDQEP VEQDYPLGDS EDALGIPYEF SNPQDDDAED
SPATPRASMY HDFNNAANDE TLFHSILLPG EHGSQSTVLE NERSMWSTPE REARSAPNLE
TPVAQFNMEA SSSSIQNEQL RRTFSSESFG VASTEELAQS HMYTHEDAEN EPAPEVEQTT
EPEKPDSPVL DTSVHELARP QTPEPELSIA EAPVPETSSP KALSLRAPSP VTEDAPSPVR
EHRKPEGFIP GAWDDDYDDP EEEPVASTTL RRSAYRSKIL SDPADASDSE SSEPAFSRAC
LTDIDPENPR ASTKQQEDVA TPKGPTRLVK EILNLKTISI YIPSQHQHIQ VQPASSESVA
ELSQSLGQSA YPQAPGAFSV HGATHAQQRS SQGTSSVENS LEVDLSPINL RFDASLGFLL
AMVVGKLLEA VKDKKPSPAE GSKQDTASKD APSKETPNVK VTFEEIKLDF VNRLGGISDT
PERYLDPSAF IFDQEVLLNA TLQNLAISIT QTEISTTPVT KGRLTTQPAV LTRIDLQKFR
FGYANGDIIS FDSGKPMSTS VRDTFLSDGT DIGIKILQSG GNTKTEVQTL PLVFQLDLRR
LDETFSWFGG LSSFLNMSAS IASSPAPTPK PAAVVQKPRG VRFDTPVDPD DKSAASENKI
NLRIGGSWVE LIGKDCSMIA ETSAIKLISR DEVIGMACSM MRVSGPHLKN SAAEPPINTE
IGGVRVEFLT TPKDTDLEKL LELIMPSKHQ FDGENDEIMV DTLLRQRRKG SVLRVTVDTV
SVRVQNMPLL SVLPNLGEEV AKLSTVAKYL PEDDRPGLLT LGKIRKVGLS LDFGGKLGHL
GTDIQDLHVG HISIPSLVAI ALHDISVQRN RSEELVSTSP YGARDISLRS PVLMARMIGD
EIEPVIKLKM QDLCIEYRVP TIMDLLELGE DATPQDFEAS LAASVANLGD QAHHVLTGAP
GSPGGKAKSG KPMTLDIGFR DCLLGLNPLG QPSKMVIALT DAHLVALLPQ DVETNAVFTI
NKSSILLIND VAEVKMNELP ATQRSRASSS TSRQVSDMCA RGYVDICYIS SAKVTVDVKE
LEDGEKQLVV ELKDDLLVLE TCADSMQTLV SLANALKPPT PPSKENKYLT DVVPMQDLLA
SISAEAFGRP EGEYDFDQDF AGAQEMAGSG SEADYNTDSP LQVQSRYYDE PVAEELFDAT
SSSIISRGSQ RSGPMMQDTN EGVLLTGFEP TSQQSIDSDD LVIHDDYYDQ GASKDSKAKV
WNSMKNSYDL APSDLVKRSI LRVKVRDVHV IWNLFDGYDW VHTRDVITKA VQDVEAKAYE
RQARAGQVHV YEEELEDEEA IGDFLFNSIY IGIPANRDPQ ELSRAINEGF NDGATETESV
ATTAFTSATN RTARARPRSK RLKLKRSKHH KITFELQGVD ADLFVFPPNS GETLNSIDVR
IKTLDVFDHV PTSTWKKFAT YDQDMGEREM GTSMVHLEML NVKPQPSLEA SEIVLRATIL
PLRLHVDQDA LDFITRFFEF KDDQVPVHTS KSDVPFLQRA EINNISVKLD FKPKRVDYAG
LRSGHTTEFM NFIVLEEARM VLRHVIIYGI SGFEKLGKTL NDIWTPDVKA NQLPGILAGL
APVRSLVNVG SGFRDLVEVP IREYKKDGRV IRSISKGATA FARTTGTELV KLGAKLAVGT
QYALQGAEGM LSGPQQVYEG WDDDDVDPDE QRQISLYADQ PTGVISGIRG GYRSLARDVN
LVRDAIIAVP GEVMESSTAS GAARAVLKRA PTIIFRPAVG VTRAIGQTLM GATNSIDPNN
RRRIEEVCYL FAILRRILLT AA
