ID   ATG2_EMENI              Reviewed;        2090 AA.
AC   Q5B1T9; C8VGC6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=atg2; ORFNames=AN5491;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA62651.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000094; EAA62651.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001305; CBF81808.1; -; Genomic_DNA.
DR   RefSeq; XP_663095.1; XM_658003.1.
DR   AlphaFoldDB; Q5B1T9; -.
DR   STRING; 162425.CADANIAP00003596; -.
DR   PRIDE; Q5B1T9; -.
DR   EnsemblFungi; CBF81808; CBF81808; ANIA_05491.
DR   EnsemblFungi; EAA62651; EAA62651; AN5491.2.
DR   GeneID; 2871780; -.
DR   KEGG; ani:AN5491.2; -.
DR   VEuPathDB; FungiDB:AN5491; -.
DR   eggNOG; KOG2993; Eukaryota.
DR   HOGENOM; CLU_000626_1_0_1; -.
DR   InParanoid; Q5B1T9; -.
DR   OMA; HRWDSTQ; -.
DR   OrthoDB; 54301at2759; -.
DR   Proteomes; UP000000560; Chromosome V.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0030242; P:autophagy of peroxisome; IEA:InterPro.
DR   GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
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..2090
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000215831"
FT   REGION          284..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1967..1986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2071..2090
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2090 AA;  228397 MW;  2A8CE9A14128C9DE CRC64;
     MTYFLPSFFQ KRLLKYALSR LEFIDTEALD PDSLGIRWGQ RSTVELRDIG LRLEKLATLL
     HLPASSKLLA ARIRLLRLTV PADIYSSGII CEASGIDVHL HFPSEKEASA ARTSLFESHE
     FGHESIIPNP ADLAESFLQA EPKEEKEELQ AALSSRSEIL HRTSSSISDD EEELGLGDET
     VSLPSFVAAF LKGVADRLQV HVDEVSIRLD VEMKQDGPSK RQPEEKPDLI SGLLIIRQIS
     VGAVVTASSS DELHPGKRPI SLSAIELALV SEPIVFSNYS QFTAPTSPSS PLRSKSSQSS
     SPASSVPPAP SSASSSTHAM MASTIFEPSQ PTVDIPEDEH GVAKLEGSIY TYDGRFSDAD
     TDENRSHGYL EESQDLSEKL LDDPAYLDSV IDSHLQDDDS EGLGDIQPGD IKPGDSNQSY
     TDRSTPSQPS LGFQAPALVD PHSRSGDHSV AVASMPNIRN IERPLDQYGP QSSMPVLSRP
     LTQDITGNNS QESQPAPPSP SETSSSGSVS AYFNNDLSES RLFSPEEAQS MYMSAMSHRS
     DSRSFIPDIP GAWDSPEATL RREAIQHHGS LGHTDETTEA LEDQDRTPVS TPKPTDRETK
     YHSGHTLGQQ QESYSESTDK HSIQPSPDVN ETTKVSKSFL HIDKVTIWIP STKPTKDHQD
     ISEPLDARSA GGSFKDSTTH LEASQVRERS VSFSKPPSSL RTRRDSTELA LAGTDTKSYT
     KYGLGSLNST NISVEISCIE VQFDISIGWL MIKIGQRVLQ GFGDIGQPKT SKKSTERDVQ
     SPQDIDFTLG TLCIKFVELV PGKSFPLEEQ QDPSTTFFDL LHDSVLLQST VSGVQAHYSN
     ANNVTDFSAA VSKFTIKFAT EDLISFSEDM KMRESTKDGL LPTGNDIVLS LSKSQDSATF
     KTDTLPLCVS LNIQRLEDLL GRFGGLSTIM ELGSSISSMS GSKGPKNDVP RRTRGVRFAG
     SPQSPVRSPT PSVPWKVNAR IGGIVLDVSG ENHYLTLRTT AAKIISRYEM MAVQIDKAKL
     SGPLSIHSGK DAPAKVSLNN IRVEFLYTPK EPDLDRLLSL ITPSKDKYDD DDDIMIDTLF
     RQRKQGSVLR VTVSGAKVVV SRPELGPLQQ LGEELGRLSS VAKYLPEDDR PGILTLVLIR
     DVEARVHIGG QIGTIAANLE NAEAAHISIP SLVAGQLGSI RVTRNGDEEL IGEALPPKPG
     FAPLPVLMVR FIADEMEPTI RVKLHNLRVE YTVSAAMAFL GVSDEMTPGD VAANMASSLA
     NIAELHPPLQ DLEEGSTTPV KPMKLKVSMR DCVLGLNPRG TAAKGLIVLA NSTFNGAIHD
     ISSSEIALDL RKAFVMIIDD VRNTDARGNL PRRRAASPQS DQIQAFTDMG YVSVSSISSA
     TAVVRIMRLT ENGAKSLDVE VRDDLLILET CADSTQTLIS ILSGLQPPSP PSQLKKYRTE
     VVPIRDMLDS LSGDAFAADN LPIGAADQAE IQDHIPERDI DYVTDFHSMT ASEEELASGP
     SSQVRDSFHS QCHVSSSMSE LDFREDHFMQ QSSVGGTAHR WDSTHNTYDL SDDSKLQNSP
     LRVRVRDAHV IWNLFDGYDW QRTRDTISKA VKDVEKKATD RRTSGRATAA FEDDEEAIIG
     DCLFNSVYIG IPANRDPAEL RNDINRNIDD LISETGSYAT TSTVTTARRN MSPGFRGKKL
     RLSRSKDHKM TFELKGICAD LVVFPPGSQE TMSSLDVRVK ELEIFDHIPT STWRKFATYM
     NEAGEKELGT SMVHLEILTV RPVSYLAASE LILKATVLPL RLHVDQDALD FMSRFFEFRD
     DSTAPSGPSQ EPPYLQRSEI NAIPVKLDFK PKRVDYAGLR SGRTTEFMNF FILDEADMVL
     KHVIVYGAKG FDKLGQALND VWMPDIKNNQ LPGVLAGLAP IRSLVNVGSG VKDLVAVPVR
     EYRKDGRIVR SIQKGAFAFA KTTSNELVKL GAKLAIGTQT VLQGAEELLS PPTGQATTGE
     EDEIDEDEAP KKISLYADQP VGVVQGLRGG FRGLERDLLL TRDAIIAVPG EVQESGSAKA
     AAKAVLKRAP TVILRPAIGV SKAVGQTLLG AGNSMDPSNR RKIEDKYKRH