ID   ATG2_NEOFI              Reviewed;        2137 AA.
AC   A1DP40;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=atg2; ORFNames=NFIA_059120;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027698; EAW16561.1; -; Genomic_DNA.
DR   RefSeq; XP_001258458.1; XM_001258457.1.
DR   AlphaFoldDB; A1DP40; -.
DR   STRING; 36630.CADNFIAP00004917; -.
DR   EnsemblFungi; EAW16561; EAW16561; NFIA_059120.
DR   GeneID; 4584974; -.
DR   KEGG; nfi:NFIA_059120; -.
DR   VEuPathDB; FungiDB:NFIA_059120; -.
DR   eggNOG; KOG2993; Eukaryota.
DR   HOGENOM; CLU_000626_1_0_1; -.
DR   OMA; HRWDSTQ; -.
DR   OrthoDB; 54301at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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..2137
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000317809"
FT   REGION          108..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2137 AA;  232859 MW;  199DF8C61A7637EC CRC64;
     MAYFLPSFFQ KRLLRYALSR LELVDTEALD LDSLGIRWGQ RSTVELRDIG LRLEKLATLL
     QLPASSELLS AKVQFLKITV PADIYSSGII CEASGINVHL QLPSEESFGA AKDENPNSRR
     PSQAGTHDSS SDHILPTPAD LAESFLDAEP KEEKEELQAA ITSRSQVLHR TSASISDDEE
     ELGLGNEGVS LPSFVAAFLK GVAERLQVKV DNVSIRVDME TKQEGVVKRE PENKPDNVTG
     LLTVREVSVG AVSSATSSSE EEKLSRNRNR PIVISDINMA LISEPIVFSN YSRFAPPTSP
     TTPVQPKSSE PSSRIPSPLP GQASDADSVL AMTRSTILEP SQEHSIQDIE EPGVGRMEGS
     AYTYDGRFSD ADTDDENRSD GYLEGSQQFL DDDKLLDNPA YLDSVIDSQL HDDDLEPPED
     LVPQDDQFPP SSETLRSQTP EVHMHRETSP SNIDTEHTAP FSHYGDGSFM DRSPHGSQPY
     LETDHVATPD VSHSASSPSG SLPSRENSDR QTAPPSESGS VGSSDVANGG ELSESKLFSN
     EEAQSMYMSA ISHGSSRSFV PNIPGAWDLP ESTVVRDVHA GTQLTDAADA KQDVQDETLI
     STPKLTAQAA SALTEKRSFG EQSECPSEAR EPDLTPLSPT LSKLSDVAKR FLRIDRISIS
     IPVGEDRRHT DETVRSADVN SASDSLKDSA MRSGHSSTES ELLSSTMYAS ARLRSDSISS
     EPSFEGTLPR SPPRQANKAD HGPISKSQPG DIAVEISAVD VRFDNAIGWL VVKTGQRVLH
     AFRDGGNVSS GKPAPESVQT RHSLALTLHN FCIKYVDHIP GQTYALNDYD PHSSSPFGLP
     HEDIILRATA SGLTARYLAD KNVTKFGLDV SKFVFGFASD DLISFSESLK MRESTRDVLS
     PVNGDISLSL TKSSDSASLT ITTLPLRLYL NVQRLEEVFG RVGGLSTILE LGNSISSVSS
     GKNMKRDSQR RARGVHFESS PPPENNLQAN PQLSWKVNAR VGGIVFDVAG ETHYLRLKTT
     AVKVVSRFEG IGVQIDKAKL SGPLPLDDSR DAPAKINLSN IRVEFLYSPK EPDLDRLLAI
     ITPSKDKYDE DDDIMLDTLF RQRRQGSVLR TTVAGAKIVV SRTSDLESLS QLEEELGKLS
     TVAKYLPEDD RPGILTLTLI RELESQVYLG GPVGNITTHL RNAEAAYISM PSLIAAQLGT
     IKVVRNGSEE LVGEALPASG SQGQNQSQLP ILMARYIADE MDPTIKIKSH NLRVEYTIPS
     IIAFLGLSED QTTGDVAANM ANSLANIAES QHLHRNASEI SIGSKGRQAS AKPSRLAFAL
     RDCVLGLNPR GTTAKGLVVL TNAKFSAAIS DSGCSEAMLD IKKASIMLID DVKNMGLAEN
     LHRGRSTIPQ SDQIQSFIDM GFVPVSSISS AMATVKLMQL DDDGTKSLDV ELKDDLLILE
     TCADSTQTLI SIINGLQPPT PPSVAVKYRT EVLPIEDMLA SFSGDAFAMD PPPEQAEIPE
     APTIVEPEDG GPGIEDELEY VSDFYPVKSG PDNLPPNESA VPSESNDLLD SFHSQYYVSS
     SVSDLEFKED HFANHSAVGG TAHRWDSTQN TYGLTDDSKI RKSPLRIRVR DAHIIWNLFD
     GYDWQRTRDT ISKAVKDVEK RATERRARAG SRASPGFEEE EESVIGDCLF NSIYIGIPAN
     KDPRELRNDI NHNIDDLASE TGSYATTTTV TGATARQGQS PSYRGRRLKL SRSKYHKMTF
     ELKGICADFV VFPPGSEETQ SSLDVRVNDL EIFDHVPTST WKKFATYMHE AGERESGASM
     VHLEMLTVRP VPELAASELV LKATLLPLRL HVDQDALDFI CRFFEFRDDS ALTPSSPADI
     PFLQRVEVNA VPVKLDFKPK RVDYAGLRSG RTTEFMNFFV LDGADMVMRH VIIYGVSGFD
     KLGQTLNDIW MPDIKRNQLP GVLAGLAPIR SLVNVGGGVK DLVVVPMREY RKDGRLVRSI
     QKGALAFAKT TSNELVKLGA KLAIGTQTVL QGAEEMLTTP TAPTLGSEED MIDEEEANKI
     SPYADQPVGV VQGLRGAFRG LERDLLLARD AIVAVPGEIV ESGSAKAAAR AVFKRAPTVI
     LRPAIGVSKA VGQTLLGAGN TLDPSNRRKI EDKYKRH