ID   ATG2_ASPOR              Reviewed;        2084 AA.
AC   Q2ULE1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=atg2; ORFNames=AO090003000445;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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; AP007155; BAE57624.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2ULE1; -.
DR   STRING; 510516.Q2ULE1; -.
DR   PRIDE; Q2ULE1; -.
DR   EnsemblFungi; BAE57624; BAE57624; AO090003000445.
DR   HOGENOM; CLU_000626_1_0_1; -.
DR   Proteomes; UP000006564; Chromosome 2.
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; 1.
DR   PANTHER; PTHR13190:SF1; PTHR13190:SF1; 1.
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..2084
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000317804"
FT   REGION          57..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          653..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          728..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          907..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2065..2084
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..693
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..745
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..928
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2084 AA;  228423 MW;  39C9A0ED27FED0AE CRC64;
     MAYFLPSFFQ KRLLRYALSR LELVDTEALD LDSLGIRWGQ RSTVELRDIG LRLETRRAET
     HDATTDQKTS GRVDPGSGDE PILPNPTDLA ESFLQAEPKE EKEELQAAIS SQSQVLQHTS
     TSSSDDEEEL GLGNETVSLP SFVAAFLKGV VDRLQVQVDD ISIRVDVETK QEGSSKRHPE
     EKPDLITGLL SVRQVSMGAV STHSESGEAS SSERRRLVSL SDINLALISE PVVFSNYSRF
     AAPASPSTPV QPKSSRPPSR AQSPSPETSS ESSLALAMTR STIFEPPQDL TRQELEEQHT
     PRLEGSVYTY DGRFSDADTE DGKRSYGSLE DSRQFEDDEK LLDNPAYLDS VIDYQFQDDD
     PERLDDMQTR VDGLFRRSRD TPRSQSPEHT AELTDQNSHP EGALIPLNDR HELEVARLPS
     HQHFLEAPEA ITEPGSSGLT PEKDFRPGYK QQLPLVCAPS SEPDSSGSAS ESFKESELSE
     SRLFSNEEAQ SMYMSAISQG STSHSFMPNI PGAWDSPEST YVRDTGFHET PTAMEQDAYS
     EQDETITTPK LTAQEGIYLS HASSIDNLQK TTTGTTGRES IQTSPGFNRL TDVAKRFVSV
     DKVLIWIPSV NHEKVPGDSQ SASHQEMSSD GLKDSTAYLQ DSVIDDDLLA SRIHGFPGPR
     SGANDPSSPH EGVDHKASGY QEKTKHDAGF SSERDEATVE IHSAEVQFDI AIGWLVIKIG
     KRIVNAFGHG DGEPPKKHNS ESKAPEQVQP KESFGLILNK FSIKFVEHVP GHANPFGESR
     QYSPTFFGLM HEDIVLQTTA SGLKAHFSST NDQTKLRLDI TKFTLGVASE DLISFNQDLK
     MRESMRDVLS PMHGDISLSM SKSLESARIH VTTLPLHLNL NIQRLEEVVG WIGGLSTILE
     LGSSISSASG AKTPKKDPPK RPRGVHFEAP PSPEKLPQDT SLPWKVNARI GGVALNIVGE
     SHYLKLRTTA VKVVSRFEGV GVQIDKAKLS GPLPLDDSKD APAKINLSNI RIEYLFAPKE
     VDLDRLLSLI TPSKDKYDED DDIMLDTLFR QRRQGSVLRT TIAGADIMIS RITDFDSLPQ
     LGDELSRLSN VAKYLPEDDR PGLLTLNLIR DFEARVNVGG KVGDITARLK NAEVAYISIP
     SLVAAQVGSA TVLRNGTEEL LGEALPLSAE QRSGQIPHPM LMARFIADEM EPTIKVKMHN
     LRAEYTVPAA IAFLGLNESS TTSDFAANMA QSIGNLAELQ PSKESQSAIK PGSPKSPVRP
     TILALALRDC VIGLNPRGSE AKGLVVLTNA NFSGAMDDGA SSEATLDLRK ASIMIIDDVR
     NMGSTDDSHR RNSTAPPTNQ VQSFIDMGFV TVSSISSATA SVKLLRSGED GTQSLDVELR
     DDLLILETCA DSTQTLISIV NGLQPPTPPS VTKKYRTEVL PLQDMLASFS GDAFALNSSS
     SLEGVSETAG DSAENIQDKE GHIEDEVEYV SDFYPAKPTS GGGSLHEAMT ASGSNELLDS
     FHSQYYVSSS ISDLEFRDDH FATQSAVGGT AHRWDSTENT YGLSDDTKLQ KSPLRIRVRD
     AHVIWNLFDG YDWQRTRDTI SKAVKDVERK ATDRRARANR ASPSFDEDEE SVIGDCLFNS
     IYIGIPANKD PRELRSDINR NIDDLVSETG SYATTTTVTG ATVRQSQSPS FRKKLRLSRS
     KYHKMTFELK GICADLVVFP PDSGETQSSL DVRVNDLEIF DHVPTSTWKK FATYMHEVGE
     KESGTSMVHL EILTVRPVPE LAASEIVLKA TLLPLRLHVD QDALDFLCRF FEFRDDSAPA
     SSAPQDIPFL QRVEINAVPV KLDFKPKRVD YTGLRSGRTT EFMNFFVLDG ADMVMRHVII
     YGVSGFDKLG QTLNDIWMPD IKRNQLPGVL AGLAPIRSLV NVGGGVKDLV VVPMREYRKD
     GRIVRSIQKG ALAFAKTTSN ELVKLGAKLA IGTQTVLQGA EDLLTSPNTQ LAGAEEELGD
     EEEAKKISLY ADQPVGVVQG LRGAFRGLER DLLLTRDAIV AVPGEVVESG SAKAAAKAVW
     KRAPTVILRP AIGVSKAVGQ TLLGAGNTLD PSNRRKMEDK YKRH