ID   ATG2_PENRW              Reviewed;        2098 AA.
AC   A7KAL3; B6HPA7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=atg2; ORFNames=Pc22g02410;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=17204848; DOI=10.4161/auto.3595;
RA   Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT   "ATG genes involved in non-selective autophagy are conserved from yeast to
RT   man, but the selective Cvt and pexophagy pathways also require organism-
RT   specific genes.";
RL   Autophagy 3:106-116(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- FUNCTION: Lipid transfer protein required for autophagosome completion
CC       and peroxisome degradation and peroxisome degradation
CC       (PubMed:17204848). Tethers the edge of the isolation membrane (IM) to
CC       the endoplasmic reticulum (ER) and mediates direct lipid transfer from
CC       ER to IM for IM expansion. Atg2 binds to the ER exit site (ERES), which
CC       is the membrane source for autophagosome formation, using basic
CC       residues in its N-terminal region (NR) and to the expanding edge of the
CC       IM through its C-terminal region. The latter binding is assisted by an
CC       atg18-PtdIns3P interaction. Atg2 then extracts phospholipids from the
CC       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, ECO:0000269|PubMed:17204848}.
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; EF107735; ABO31073.1; -; Genomic_DNA.
DR   EMBL; AM920437; CAP97529.1; -; Genomic_DNA.
DR   RefSeq; XP_002564285.1; XM_002564239.1.
DR   AlphaFoldDB; A7KAL3; -.
DR   STRING; 1108849.XP_002564285.1; -.
DR   EnsemblFungi; CAP97529; CAP97529; PCH_Pc22g02410.
DR   GeneID; 8312490; -.
DR   KEGG; pcs:Pc22g02410; -.
DR   VEuPathDB; FungiDB:PCH_Pc22g02410; -.
DR   eggNOG; KOG2993; Eukaryota.
DR   HOGENOM; CLU_000626_1_0_1; -.
DR   OMA; HRWDSTQ; -.
DR   OrthoDB; 54301at2759; -.
DR   BioCyc; PCHR:PC22G02410-MON; -.
DR   Proteomes; UP000000724; Contig Pc00c22.
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..2098
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000317810"
FT   REGION          110..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1602..1622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..489
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..612
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2098 AA;  229364 MW;  DBC004FFBB832DF9 CRC64;
     MASYFMPSFF QKRLLKYALS RLGLVDTEAL DPDNLGIRWG QRSTIELRDI GLKLEKLSTL
     LNLPPSCELL SARVQLLRIT LPADFHNSGI LCEANGIDVH IRLLSEESKK GQHVKRESEK
     HDYSAVPTPS GLAESFLESE PKEEREELQA AIASQSQVLP QDPLAWSTDD DNELGLGSET
     LSLPSFVAGF LKGVVDRLQL KITDAVVRVD MELKQDGTSK RQPEHKPDLV AGLLSVGEID
     VHGVSEKTVG PEESLPFREG KRLISMADIN FGLLSDPSVF SNYSRFAPPA SPTTTMRSKG
     SQPSSRAPSP SPLDRSDEEP LAMTQSTIFE PPQAFGHFST TTDRLEASAF SDGRFSDADS
     ESGSHRGGYM EDSQIFGDDP FQDNPGYLDS VIDTQFDDFD DEQSPVIHPE EGRGAGSEWR
     SHLSHGTRSL HQSQQGESSD GPLVPSGSYH VSQTHDTHHS QIGSEIDEIT QTTQHYDDYE
     NEHDEISELS VSSHPPSTSS PRPEPERTSL GEETSNADLD ESKLFSHDEA QSLYMSATSQ
     GMSGSFMPQM PGGWGSFDSA PGAHGDRSKV IAPIDPAHSA HDQGEADSRC TAPSEDNVTE
     QHDLDDQAQS QTLHKDRTST PSSSGLHRIN EMRKSVLTVD KILLWLPPAA SEEEEEEQVS
     AEPSPVLQKG NVGSDLNEST ASFAESAPGE SLLASRAYKS TRFGRDFSEA RAQPSAGTGL
     PEIAVEVFSV SVHFDIATGW LLTKIGQRLS HTLGTAERDP AEKQLRKDQP ARTPPVHLVV
     HALSIKFIER VSGHVYSSDN SGSPLSPPYS MEDVILRLNL SGLNARLSAQ STTTKLNFDV
     SKFALGFASE DIIFFDERLK MRESTRDVLA PSQGDISISL VKSADLAKVD ISTLPLHINL
     NIQRLEEALG WMGGLSTILE LGGSMSSVST VKGSPPLSKQ RPRGVHFETP APGVHAPKGT
     SALWKVNARV GAILLDVTGE THSLQLTTTA VKIVSRFEGI GIQIDKAKMI GPLSINDTSS
     DSPAKVTLNN IRLEFLFAPK EVDLDRLLTL ITPSQDKFDV EDDIMLDTLL RQRRQGSVLR
     MTVGRLETSI SDTGGLEPLS SLAVELSRLS NVTKYLPEDD RPGILTLILV RDFQGDVHVG
     GEVGDIESRL TSVEVAHITM PSLTAAHIGT MTVRRNNNEE LVGHALWPPN KYQDPDSSYP
     PVLMARFIPD EMDPTYKIKL HNLLVEYTVP SVTAFLGLGG DKMSGDLASS MVNSIANLAE
     HSMSSPSMTG RSMSNESSSS TKPIKLSVVF RDCVFGLNPR NSPAKGLAVL TNAKFGGTIH
     GDESAEASLD VRKASLMIID DVYHESAYNL HQRGSVVPQD TQAQAYIDKG YVPVSSISSA
     TAGVKLTSAE DGTKSLDVEL RDELLILETC ADSTQTLISI MNGLQPPPPP NVNVKYRTEV
     MPIQDMFASF TGDAFAADPP LPHDNDMATI SEGSSREGQL TDELEYVSDF YPVKGGLGGA
     GIEAIDTDSN DLLDSFHSQY QVSSSMTELD FQGDHFAKKS AVGGTAHRWD STRNTYGFAN
     DTKLERSPLR VRMRDVHFIW NLFDGYDWQR TRDTISKAVK DVETKATERR SRGSRVSPSA
     EDEEESVIGD FLFNSIYIGI PANKDPRELH REINHDIDDF TSETGSYATT TTVTGAGSRQ
     GRPTSKREKK LRLHRSKHHK MTFELKGVSA DLIIFPPGSE ETQSSLDVRV KDLEIYDHVP
     TSTWKKFATY MREAGEKESG TSMVHLEILT VKPVPELAAS EIVLKATILP LRLHVDQDAL
     DFMSRFFEFR DETAQPSDTP GDVPFLQRVE INAVQVKLDF KPKRVDYAGL RSGRTTEFMN
     FFVLDGADMV LRHVIIYGVS GFDRMGQTLN DIWMPDVKQN QLPSVLAGLA PIRSLVNVGG
     GVRDLVVVPM REYRKDGRIV RSIQKGALAF AKTTSNELVK LGAKLAIGTQ TVLQGAEDLL
     TTPNAPAFEE DSLDEDEAKK ISLYADQPVG VVQGLRGAFS GLERDLLLAR DAVVAVPGEV
     VESGSAKAAA KAVWKRAPTV ILRPAIGVSK AVGQTLLGAG NTLDPSNRRK MEDKYKRY