ID   ATG2_ASPNC              Reviewed;        2221 AA.
AC   A2QSC9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=atg2; ORFNames=An08g10270;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM270182; CAK96773.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2QSC9; -.
DR   PaxDb; A2QSC9; -.
DR   EnsemblFungi; CAK96773; CAK96773; An08g10270.
DR   VEuPathDB; FungiDB:An08g10270; -.
DR   HOGENOM; CLU_000626_1_0_1; -.
DR   Proteomes; UP000006706; Chromosome 8R.
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..2221
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000317803"
FT   REGION          108..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          963..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1297..1318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1495..1514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..316
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..606
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..690
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..758
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2221 AA;  242485 MW;  079B3DC93EF948D2 CRC64;
     MAYFLPSFFQ KRLLRYALSR LGLVDTEALD LDSLGIRWGQ RSTVELRDIG LRLDKLATLL
     HLPASSELVS ARIRFLKITV PADIYSSGII CQASGIDVHL RLLSDETRHA GQGDRPMGSG
     PGHDSASDPI IPNPTDLAQS FLQAEPKEER EELKAAISSQ SQVLHRTSTS GSDDEEELGY
     GNEGVSLPSF VAAFLKGVAD RLQVQVDDIS IRVDMETKQD APLKRQPEDK PDLVTGLLTV
     GQVKVDAVSS SSNENEASSR NQRRLISLSD INVALVSEPA VFSNYSRFTA PTSPESTSPE
     SPLQPKPSPP PSHVSSPPSE HASEEDTALD LTRSIMFEPS RGMSESKIIE QYAPEMEGSV
     CTYDGRFSDA DTEEETRSHG NMGESQNLLV DDEILDNPAY LDSVIDSHLH DDELDGIGHF
     PPEVGQRALG NEDTPRLRTP ELHAAGSASH YSDTQNAMIL APRSQVPAVT SLAQDKLQIP
     EAVDIATRPA LPAIELEVTQ DPQPCADNQT SPVTSVPPSE ASSSSSTSGS FNQDELSESR
     LFSNEEAQSM YMSAVSHDSM SRSFMPNIPG AWDSPESTVV RDSHAHMHHE NGRDVQHMDP
     DHEDDDEAVA TPKLTAQAGM HISQECLIDD SPEAHRDPTD KELSRSSSGL NKFTDVARRF
     FSIDKVVISI PSMDEDGDSA DNTPSASYTE EDTRGLEETT ACLRDSATED YFAPPGRKAS
     TRTRSDTIRP ASYGYEGAEK GSSQPSQSDG QAQSRRSPND MEIEVFSAEL QFDIAIGWLV
     LKVGHKILHA FSNDSEVSQQ TGQPQEEVQK RQAIKLALRK FSIKFVEHVP GHSYPAETDS
     SPFFGLLHND ILLQTCLSGL EAHLSIDKDI TKLHLNIKKF SLGFASEHLI SFSEDFKMRD
     SVRDVLSAEQ GDIDLSITKS PDSTTVNLMT LPLQLNLNIQ RLEEAIGWFG GLSTILELGN
     SISSASSGKG PKKEAPKRPR GVHFEEFPPP AASERTGSAP LKVNVRIGGL AADVVGETHY
     VKLRTTAAKI ISRSSGVAVQ IDKAKLTGPL PLDETRDAPA KLSLTDIRIE YRFSPKEEDL
     DRLLGLITPS KDKYDEDDDI MLDTLFRQRR QGSVLCLTIS GARVAVSRTT DLDSISQLAD
     ELSRLSNVTK YLPEDDRPGV LTLALVRELE VQVHIGGKVG EMSAILRNTE LAFISLPSLI
     AAQLGSITVA RNRDEELVGE ASAIGHKSSL SQSPLPVLMA RYIADEMDPT VKVKLHNFRA
     EYTLPSIIAF LGLSDDMTTG DVAANMASSL ANLAELQPPH HDVQLPEKGG RSDTPSKPIK
     LTVDLRDCVL GLNPRGTGAK GLVVLTTAKF SGAIHDPVSS DATLELRKAS LMIIDDVANV
     GYADNVQRRS SAPPHSNQVQ SFIDHGFVTV CTISSATATV KIMRLSDDGA KSLDVELRDD
     LLILETCADS TQTLISIVNG LQPPTPPSAA AKYRTEVLPI QDMLSSFTGD AFFTDMPEPP
     ETTDSPDQNQ GAGHLEDERD YVSDFKHVSA VPEHGSLTEG MMASGSNELL DSFHSQYYVS
     SSISELDFRE DHFAQKSAVG GTAHRWDSTQ NTYGLSDDSK LQKSPLRIRV RDAHVIWNLF
     DGYDWQRTRD TISKAVKDVE RKAIERRARA GSRASPSFDE EEESVIGDCL FNSIYIGVPA
     NKDPRDIRND INRNIDDLAS ETGSYATTTT VTGATVRQSQ SPSVRGKKLR LSRSKYHKMT
     FELKGICADL VVFPPDSGET QSSLDVRIKD LEVFDHVPTS TWKKFATYMH EAGEKESGTS
     MVHLEILTVR PVPQLAATEI VLKATILPLR LHVDQDALDF ICRFFEFRDD SAPTPTAPSD
     VPFLQRVEIN AVPVRLDFKP KRVDYAGLRS GRTTEFMNFF ILDAADMTMR HVIIYGVSGF
     DKLGQTLNDI WMPDIKRNQL PGVLAGLAPI RSLVNVGGGV KDLVAVPVRE YRKDGRLVRS
     IQKGALSFAK TTSNELVKLG AKLAIGTQTV LQGAEDLLTT PNASGAGVED EYADDEEAKK
     ISLYADQPVG VVQGLRGAFR GLERDLLLTR DAIVAVPGEV IESGSAKAAA KAVWKRAPTV
     VLRPAIGVSK AVGQTLLGAG NTLDPSNRRK MEDVSYTFPQ RADSILTLLA EIQAPLTTFV
     AITLAVLSAS SSSWDGYGAI DWDIYRSRSH IHLRAGRYRS TQDDNKMDAC SHLKDFIRGG
     S