ID   ATG2_ASPCL              Reviewed;        2131 AA.
AC   A1CUF9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=atg2; ORFNames=ACLA_086450;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027060; EAW06946.1; -; Genomic_DNA.
DR   RefSeq; XP_001268372.1; XM_001268371.1.
DR   AlphaFoldDB; A1CUF9; -.
DR   STRING; 5057.CADACLAP00007538; -.
DR   EnsemblFungi; EAW06946; EAW06946; ACLA_086450.
DR   GeneID; 4700500; -.
DR   KEGG; act:ACLA_086450; -.
DR   VEuPathDB; FungiDB:ACLA_086450; -.
DR   eggNOG; KOG2993; Eukaryota.
DR   HOGENOM; CLU_000626_1_0_1; -.
DR   OMA; HRWDSTQ; -.
DR   OrthoDB; 54301at2759; -.
DR   Proteomes; UP000006701; 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..2131
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000317802"
FT   REGION          106..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          954..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1286..1308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1520..1540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1573..1592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2112..2131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1576..1592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2131 AA;  231480 MW;  782FA9090B8BEF36 CRC64;
     MAYFLPSFFQ KRLLRYALSR LELVDTEALD LDSLGIRWGQ RSSVELRDIG LKLEKLATIL
     QLPPSSELLS AKVRFLKITV PADIYSSGII CEASGIDVHL RLPPEESSRA TKEGEQPHRK
     SLEAVQHDPS GDHILPTPAD LAQSFLEAEP KEEKDELQAA ITSRSQVLHC TATSLNDDEE
     ELGLGDEGVS LPSFVAAFLK GVGERLQVKV DNVSIRVDME TKQDGPVKRE PEDKPDVVTG
     LLTVREITVG AVSSAASGKP DEILPCRRNR PISIFDIDVA LISEPIVFSN YSRFAPPSSP
     TTPMQPRASE PASRVPSPSP LDTPDTESVL AMTRSTIFEP PEKHPVDETE EPAVGGMEES
     AYTSDGRFSD ADTDEENRSG SYLEDSQPFL GDDKLFDNPA YLDSVLDAQF QDGDVEPPED
     LLSFHEQPAS SSGTPRSQTP ELHTSSRFEG SGSETDRAAR LSQHGQGSFN NGSFRDTHHS
     RDATPSVSQL VSHDRSAEAS HLRAESERQS SSHVFGPPSD AGSLSSSDSA NCGELAESKL
     FSREEAQSMY MSAISQGSDR SFMPNIPGAW DSPESTFVRR VNTHTRLADA ASPSRVQEDE
     TSVSTPKLTA REQSDASTPQ PFNEQDKSFS QPIESAAPQS SPTLGRFSDV AKRFLNIDRV
     SILIPVDFDE NSTESPSSSD NKGSGTPAGV PSPESDMLSS TMYASARLRS DSLISPTSFE
     GPQLRSPPRQ TNKADQNFVS GHRADEIVVE VSSIDIQFDN AIGWLVAKVG PRLLRAFSGD
     GKDIPVASNA PEPVQARHSL RLALNSFCIK YLDHIPGQTF APGDAASHLP SSFSLSHEDI
     ILRLAASGLN ARFLAEKNTT KFGVEISKFA FGLASDDLIS FNESLKMRES TRDLLSPLHG
     DISLSLTKSP DSASLNISTL PLQLDLNVQR LEEVLGRVGG LSTILEVGNS ISSVSSGKSV
     KKEPPRRARG VHFENSPPPG DAVQNESQPW KVNARLGGIV LDVAGDTHYI RLKTTAVKVV
     SRFEGIGVQI DKAKLSGPIP LDESKDAPAK VNLTNIRVEF LHTPKEPDLD RLLAIITPSK
     DKYDEDDDIM LDTLFRQRRQ GSVLRTTVAG AYINISRTRD LDSLSQLGEE LGRLSSVTKY
     LPEDDRPGIL TLTLIRELEA QVDIGGTIGT LAAHVRNAEA AYISMPSLIA AQLGAITLVR
     NGSEELVGEA LPLGIGQGQS QGHLPVLMAR YIADEMDPTI KIKSHNLRVE YTVPAIVALL
     GLSEEMTPGD VAANMANSLA SIAQSQHLQR VPSNSSAGSE TRQAPSKSSR LAIALRDCVI
     GLNPRGAAAK GLIVLTNAKF SAAISDQGSS EAMLDLKKAS IMIIDDVKNV GLTENLRRGR
     STIPQSNQVQ SFIDLGFVPV SSISSAMATV KLTAPDEDGT KAIDVELKDD LLILETCADS
     TQTLVTILNG LQPPTPPSVA VKYRTEVLPL EDMLASFSGD AFTMDSPHDQ AGVSEVSVSA
     APDDAEPRIE DELEYVSDFY PVKPGTGRQG SNGESMSSES KDLLDSFHSQ YYVSSSVSDL
     DFREDHFAQP SAVGGTAHRW DSTQNTYGLS DDSKIQKSPL RIRVRDAHVI WNLFDGYDWQ
     RTRDTISKAV KDVEKKATER RARAGSRAPD FDEEEESVIG DCLFNSIYIG IPANKDPRDL
     RNDINRNIDD LVSETGSYAT TTTVTGATIR QGQSPSIRGK KLRLSRSKYH KMTFELKGIC
     ADLVVFPPGS DETQSSLDVR VRDLEIFDHV PTSTWKKFAT YMQEAGERES GASMVHLEIL
     TVRPVPELAA SEIVLKATLL PLRLHVDQDA LDFLCRFFEF RDDSAPAPSS PAEVPFLQRA
     EINAVPVKLD FKPKRVDYAG LRSGRTTEFM NFFVLDGADM VMRHVIIYGV SGFDKLGQTL
     NDIWMPDIKR NQLPGVLAGL APIRSLVNVG GGVKDLVVIP MREYRMDGRI VRSIQKGALA
     FAKTTSNELV KLGAKLAIGT QTVLQGAEEL LTTPNAPIPG SEEDMADEEE AKKISLYADQ
     PVGVVQGLRG AFRGLERDLL LARDAIVAVP GEIVESGSAK AAAKAVWRRA PTVILRPAIG
     VSKAVGQTLL GAGNTLDPSN RRKMEDKYKR H