ID   ATG2_MAGO7              Reviewed;        2094 AA.
AC   Q51ZN8; A4QWH2; G4N4M2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=ATG2; ORFNames=MGG_05998;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Lipid transfer protein required for autophagosome completion
CC       and peroxisome degradation. Tethers the edge of the isolation membrane
CC       (IM) to the endoplasmic reticulum (ER) and mediates direct lipid
CC       transfer from ER to IM for IM expansion. ATG2 binds to the ER exit site
CC       (ERES), which is the membrane source for autophagosome formation, using
CC       basic residues in its N-terminal region (NR) and to the expanding edge
CC       of the IM through its C-terminal region. The latter binding is assisted
CC       by an ATG18-PtdIns3P interaction. ATG2 then extracts phospholipids from
CC       the membrane source using its NR and transfers them to ATG9 to the IM
CC       through its predicted beta-sheet-rich structure for membrane expansion.
CC       {ECO:0000250|UniProtKB:P53855}.
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   -!- 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   -!- SIMILARITY: Belongs to the ATG2 family. {ECO:0000305}.
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DR   EMBL; CM001233; EHA52037.1; -; Genomic_DNA.
DR   RefSeq; XP_003711844.1; XM_003711796.1.
DR   AlphaFoldDB; Q51ZN8; -.
DR   STRING; 318829.MGG_16734T0; -.
DR   PRIDE; Q51ZN8; -.
DR   EnsemblFungi; MGG_16734T0; MGG_16734T0; MGG_16734.
DR   GeneID; 12984228; -.
DR   KEGG; mgr:MGG_16734; -.
DR   VEuPathDB; FungiDB:MGG_16734; -.
DR   eggNOG; KOG2993; Eukaryota.
DR   HOGENOM; CLU_000626_1_0_1; -.
DR   InParanoid; Q51ZN8; -.
DR   OMA; HRWDSTQ; -.
DR   OrthoDB; 54301at2759; -.
DR   PHI-base; PHI:2070; -.
DR   Proteomes; UP000009058; Chromosome 3.
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..2094
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000215833"
FT   REGION          287..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2075..2094
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..579
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2094 AA;  228485 MW;  5DC13AEA09C9C793 CRC64;
     MATLFQSFRG SAMPKRLLRY ALARLDLLDS DALDLDNLDL AIGRNTVLEF RDVGIKLPKL
     AKLLGLPPTF TLLKAKVILL RVTIPMDIYS SSLKIEVDRV DVQLKVDSKD DIDGRSRTTI
     RGPTDVVPNT VDLAQSFLEQ QSPKEKEELE AALSAETQDV GGSLVLGEDE DEQDEGSYGT
     GQALSLPAFL ANFLQGIVDR TQIQIRGVTF QLDVSVPLEP NLNAPDVVTV KLALGQIDVE
     GVTTSLGSDE QDRPKFVHKE GKRLVSLQDI TAFLISEANV FSTFERTTSV PPSLSPQSSA
     ASALRSPVSR ESTSMPFQEQ EVEGRSTQLP SFEDNLGDSE AALNIPYDLS DEDDQEPGNK
     TAASSMSTPR ASILHDHLAH QDESSSFLQG FTPYTAATPG IHLDADQMDE MSPQPAHDLS
     THNQISLSNS VLSNSSSGSS GQEPTEDLTE SHLYTHEDAE SMYMSAFSQH EPTPQSVVPN
     ELYIDPSESS VGVSSPQGTR DEPSSSLGAT YGLEDSQASS TIGFQGLKTS PGLDASTISE
     QSDSSPAPII PPSSDGNTEA GPESSIQGER HDRKSQSPNE CLTPREPTRL AKKVLALDTL
     SLYLPSSQKS VHVVPLDGQS SPGEPQPLSP SLASSVFPHV PGAFGASTSL PPSPPPISPT
     SIELDNQEPN DGILEAILSP ISIQFDASIG FILAMVVSRL LGAISPSKEE PAQQTAKDNP
     SATNQATDHQ AVKVTLQAVS ILFLERLGGV SEAPDSIFGV RTSKFDEDIL LQAQLRNVQC
     LLSSDETVID AEGFTFGYAG DDNHIISFDR SKEMMASVKD AVPSPGSEVS IKLKKGGPSS
     KIDIATLPLQ ICLDLRRLDE TFSWFGGLSS FLNMGSSIAS INGIGNSQPA KPPARPASRG
     VKFDTPINPD DRSATSDNKI NMRINTVRLD LIGKDCNVIL ETSAFKLVSR DEGIGIALRK
     IQVHGPYSNE SGPHPPISVT ITGSRIEYSM TPKEADLERL LELISPSKLR DTPDDDEIMV
     DTLLRQRRKG SVLRLKFDNV AADISNIPHL GCLPSLGEDL ARLGTVAKYL PEDDRPGLMS
     LILVRNAHVS VDVGGRFGVI SASMAHFDVA HVSVPSLLAV AARSLEVNRN QIEELVGSSL
     LASHGDEETP VLVIRLIGGT VEPTITVKLR GLNVEYRVPT IIDLLNLGED ATPQDFEAGL
     AASVAQFGEQ AHVAISGTSA ITADSRTIGQ DRQKLPVVEL YFLDCVVGLN PLGMTSKMGI
     VLSDSCLKVW LEEKGDAKAT WHIKQASILL IDDVALLDPE GKQNVKRHVH RPSDPVSAKI
     WDMDSVLCAQ GFVSISQIRA AIIRVKAIQD EDGQRLIDVE VQDNFLVLET CADSTQTLIG
     LGNALKPPTP PSKENKFKTE IVPIEDMLAS ISQDAFGKAE GDYNFDDDFG EPEESDWTED
     DLDEDLDIMG ALGSQDDGQN TRQLLFDATS SSIMSDRTTT QYANDEVIFS GFSENPSHAN
     SPDMSVENAF FASVPASETP QPEWKSAKMR EVVPKEATIK KYPLKIKIRD MHLIWNLFDG
     YDWQRTRETI GKTVEEIQAK AYERRARMDR RMGYHEEDGL EEEAVSDFLF NSIYIGIPSH
     QDPRELSQNI NQELYGINPS DTESVATTAF TTTTSRMGGP SRPKGKRLKL TRSKHHKITF
     ELSGVNAVVR LLEPGSEETQ SLIRVHIRDL DVYDHVPTST WKRFAMYDED HGPREMGVPM
     VDLKVRIVRP VLDVTAEEIV MFVNVLPLRL HVDQDALDFI TRFFGFKDDT IKTTSSPSDV
     PFIQRAEIYD IPVKLDFKPK RVDYAGIRSG RTTEFMNFII LDNASMVMRH AIIYGALGFE
     RFGEMLNDVW MPEIKRHQLP GVLAGLAPVR SLVDVGSGFR HLYEIPIREY KRNGRVVRSI
     GKGAAAFART TGTELIKLGA KVAIGTQNML QGAEGLLVET PEHNRYGVAG PSTVQRPGEW
     EEIDDSEEDI RHQISLYANQ PTGVIQGLRH GYRSLSRDIS IARQAIIAVP GEVRESSSAT
     GAAKAVLEKA PIFIFRPAIG ATKAIGQTLL GATNSLDPQN LRRMDNKYKP DPKS