ID   ATG2_ASPTN              Reviewed;        2082 AA.
AC   Q0CSI0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=atg2; ORFNames=ATEG_03354;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476597; EAU36628.1; -; Genomic_DNA.
DR   RefSeq; XP_001212532.1; XM_001212532.1.
DR   AlphaFoldDB; Q0CSI0; -.
DR   SMR; Q0CSI0; -.
DR   STRING; 341663.Q0CSI0; -.
DR   PRIDE; Q0CSI0; -.
DR   EnsemblFungi; EAU36628; EAU36628; ATEG_03354.
DR   GeneID; 4317808; -.
DR   VEuPathDB; FungiDB:ATEG_03354; -.
DR   eggNOG; KOG2993; Eukaryota.
DR   HOGENOM; CLU_000626_1_0_1; -.
DR   OMA; HRWDSTQ; -.
DR   OrthoDB; 54301at2759; -.
DR   Proteomes; UP000007963; 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..2082
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000317805"
FT   REGION          108..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..636
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          912..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1435..1454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2062..2082
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..309
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..600
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2082 AA;  228258 MW;  9A5180337C5F5F5E CRC64;
     MAYFLPSFFQ KRLLRYALSR LELVDTEALD LDSLGIRWGQ RSTVELRDIG LRLEKLSTLL
     RLPPSSELLS ARIRLLRLTV PADIYSSGII FQTSGIDVHL RLPLNDVSAD QDTHRSPTDD
     TGDDHVLPNP TDLAESFLQA EPKEEKEELQ AAISSQSQVL QHTSTSSSDD EEEFGLGEEA
     VSLPSFVAGF LKGVVERLQV EVEDVSIRVD VETKQDGPSK RQPEEKPDLV TGLISVRQIN
     VGAVSKSHDS EEGILRWGKR QISVSDVNLA LISDPIVFSN YSRFTAPPLS PSTPVQSRPS
     QPPSEVMSPS PELNPSDSNP GLGMTQSTIF APPQSDDEPV PEAPHELEMA GSVYTYDGRF
     SDADTEETRS YGHLGDSQNF SDDDKLLDNP DYLDSVIDSH LHDEDLERSV NLPRDDAPSA
     REEDTPRLHD SSTFNFEPTM AHHTLQEVSS PTIHGQVLED RTGSFGSASL GRDASSEHSL
     PEDSLSENQH AEEPQHEVRA HMSGSQPAPP SEEGSSSSTS NSFRDGDLSE SKIYSHEEAQ
     SMYMSAISHG STSRSFVPNI PGAWDSPGST ATRYFDVHNR SQCSGDTNRT RDEKDETTAA
     TPRLHAQAGS HIPQEYPLDG SRTAHSEATD KGSFESTQGL NKLNDIAKRF LTIDKMSIWV
     PSRDGTDEPS GAVSEMSFSH GGVDPNVSGH SERRSYPKRS QDETAIELHS AEIHFDISTG
     WLLAKVGQRV VDAFAHNDSE TPKKSRSQQD SHSDQAISLS FGKFSIKFVE HIPGHAYPPE
     DSRIHSPTYF GLMHEDVLLQ TTVAGLQAHY SETGNATKLR LELAKFTLGF ASEDLISFSE
     DLKMRESVRD VLSPVHGDVS LSLTKSADSA RVNIATLPLQ VNINVQRLED VLGWIGGLST
     ILELGNSIPS VSGVKAQKEP PKRSRGVHFE PSPPPVKESR QPSIPWKVDS RIGGMALDVV
     GETHYLKLRT TAVKVVSRQK GIAVQIDKAK LSGPLSLEGT RDAPAKVNFT NIRVEFLFSP
     DDDDLDRLLS LITPSKDKYD EDDDIMLDTL LRQRRQGSIL RATVDGARVA ISRIQDLEHL
     SQLGDELGKL SNVTKYLPED DRPGILSLAL VRDFEARMHV GGQVGDITVR LKEAETAYIS
     IPSLVAARLG SMTVVRNEIE ELVGEALPLH MAQAQHPMLM ARFIADEMEP TIKVKVYNLR
     AEYTVPSMVA FLGLSDDMTA GKVAENMTSS LVNLADLPPP HISPVSGGHE SPRGPVKPIK
     LAVVLRDSVI GLNPRGTAAK GLLVLTNAKF SGAIHDPASS EATLDLRKAS VMVIDDVQNI
     GITDNPRQGR WTTPQSDQVH SFIEMGFVPI SSISSATATI RIMQLSEDGT KSLDVEFRDD
     LLILETCADS TQTLISIVNG LQPPTPPSVA VKYRTEVLPI QDMLASFSGD AFATDAASPE
     HAAEGSSDLA QPANTKGNQI EDELEYVSDF YPVKPGSENA SLHENLAGSG SNELLDSFHS
     QYYMSSSVSE LDFRDDHFAK QSAVGGTAHR WDSTQNTYGL SDDSKLQKSP LRIRVRDAHV
     IWNLFDGYDW QRTRDTISKA VKDVEKRATE KRARVGNRAS PGFDDDEESV IGDCLFNSIY
     IGIPANKDPR ELRQDINRGI DDLASETGSY ATTTTVTGAT ARQNHSPPFK KKLRLSRSKY
     HKMTFELKGI CADLVVFPPD SGETQSSLDV RIKDLEIFDH VPTSTWKKFA TYMHEAGEKE
     SGTSMVHLEV LTVRPVPELA ASEIVLKATI LPLRLHVDQD ALDFLSRFFE FRDDSAPASP
     SPQDIPFLQR VEVNSIPVKL DFKPKRVDYA GLQSGRTTEF MNFFVLDGAD MVMRHVIIYG
     IAGFDKLGQT LNDIWMPDIK RNQLPSVLAG LAPIRSLVNV GGGVKDLVVV PMREYRKDGR
     IVRSIQKGAW SFAKTTSNEL VKLGAKLAIG TQTVLQGAEE MLTSPNAPVP VSEEDSTDEE
     EAKKISLYAD QPIGVVQGLR GAFRGLERDL LLARDAIVAV PGEIVESGSA TAAAKAVWKR
     APTVVLRPAI GVSKAVGQTL LGAGNTLDPS NRRKMEDKYK RH