ID   ATG2_YARLI              Reviewed;        1525 AA.
AC   Q6C6M0;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=ATG2; OrderedLocusNames=YALI0E08338g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382131; CAG79281.2; -; Genomic_DNA.
DR   RefSeq; XP_503692.2; XM_503692.2.
DR   AlphaFoldDB; Q6C6M0; -.
DR   STRING; 4952.CAG79281; -.
DR   EnsemblFungi; CAG79281; CAG79281; YALI0_E08338g.
DR   GeneID; 2912485; -.
DR   KEGG; yli:YALI0E08338g; -.
DR   VEuPathDB; FungiDB:YALI0_E08338g; -.
DR   HOGENOM; CLU_000626_3_0_1; -.
DR   InParanoid; Q6C6M0; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0030242; P:autophagy of peroxisome; IEA:InterPro.
DR   GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
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; 2.
DR   PANTHER; PTHR13190:SF1; PTHR13190:SF1; 2.
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..1525
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000215835"
FT   REGION          216..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..735
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1525 AA;  166370 MW;  53EC69BDAB275D5F CRC64;
     MNWIPNVQKR AFHYVLNRLA LFSDLELDNM DISLGTAQKA ALTNVKLDPD RVSLPAGMYM
     RSGKIDEVSV EMRLLGGAGI AVKIDGVHIT ASMKQMDVET ATEHVEEFLE RTTADLAASI
     LSEDLSASLQ IDPAEEPPLL GMGGSGISEA LVKKVTQTVL SQLTVDVTNV HVTLFVAADD
     KMDLVVDEVR LRPQGGQEMA LEVRGVKMKV MDKKARGTSA PVTAGSTAHA TTGFTSESDS
     DSDTDPFSNA KKSLLQSTIF SHEEASSIYM SAIAESANLG FESDPLFGVF YVDTIDVLVF
     LGEEMRVSCE VGIVRASLDL LPTVILSLVK VGNGGSGGKK SRDSETKEGT AMDLNMSIKS
     ISASICQLGD DWEFKNIDTN LLFSLSDISG SSGAFHKLQI GVCEVKRGST RVFGFESDEK
     NTDDEEPTPR DSDILLKASS ASFTLVLPKK AVGVFTIPDL IDVVSLITYL LSLIESKQQK
     AATMTERSER AGASKTTVQT NTFDFDVAGH KLYILPIRLS NGQMSLSRVS FGDVHVKGIS
     FENSIVSVDK VDFDIGLPIV EELHQLLLPI IDAMNSAKNR PVPASVQTAP PKLLRIVEEP
     VNASSLVINV ARVKGKVDLG GKVGVIEVVL GGISVTGPTD RIEISTVEIG RDLSDLGLSK
     KWLLHPLKRE SNVVVELSSG QIQLITVKNC ALEFYTELLE LFGGKGDDTK AAELQESSSP
     DSSSRESSSG SESPPKRIPL QIHNCAVGLN PTNSSSSAQF IVKHVTCEIK PSPTFSMTSF
     IGSASLLLID DASLVTPNPT DLMSSYLEQY TSVASLTATS ISISTSPGNP TCININGDTV
     TLSTCADSTQ TLIHLINSLK PAVELSGAKF QLETLDPFLN TFQDVDDCFF KAKNKDACES
     SCSSDNDDID MVSDDVPNNM SFVESYYGGD KPSQSRKSGR QKMAESYTHA DFLLDSDLDS
     LVKRERVRFE EICFEEDYFD KEEEDMPVMS RPRASSHDLA SSNELLTPPT VVINIDLIHN
     IVCNFHDGYD WQYTRNEING AVDGLKKRMK ERPVVEEPPV MTTDLLFNSI YIQAKDEDDL
     DDVVGEQTEP AKPKEANKSR RGLLSRSSNP LVQVWLQGIA CLLTVYAGLE DPDLPPGQVL
     NSLDVKIKDV EIIDHVPTST WNKFLTYMRS RGEREAGAVM AHITMQNVKP VSTLSSQEVI
     CHVTILPLRL HVDQDTLDFL TRFFNFKDVR TTAPPDETFI QKFDIRDVPV KLDYKPKKVD
     YSGLKSGKST ELMNFFILDE SDMVLRRIKL RGITGFANLG QKLNDIWMPD VRRTQLPGVL
     AGVAPVRPLV NLGGGIRNLI VVPVREYKKD GRVVRSLNQG AYAFAKTTTN ELVRFGAKLA
     VGTQNLLEGV VSTERAGESR DLDDSDLEST TKYYTYMGYS DSNNKLISLY ANQPLGVYAG
     LQDAYSSFGK HMNVAKTAIH NLSEDISEAD TAGAAAYAVV KAAPVALIRP IIGTTEAVSK
     TLFGVANEMD PSGRELARDK YKEAN