ID   ATG2_CANGA              Reviewed;        1587 AA.
AC   Q6FP05;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=ATG2; OrderedLocusNames=CAGL0J07634g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380956; CAG60990.1; -; Genomic_DNA.
DR   RefSeq; XP_448039.1; XM_448039.1.
DR   AlphaFoldDB; Q6FP05; -.
DR   STRING; 5478.XP_448039.1; -.
DR   EnsemblFungi; CAG60990; CAG60990; CAGL0J07634g.
DR   GeneID; 2889899; -.
DR   KEGG; cgr:CAGL0J07634g; -.
DR   CGD; CAL0133478; SPO72.
DR   VEuPathDB; FungiDB:CAGL0J07634g; -.
DR   eggNOG; KOG2993; Eukaryota.
DR   HOGENOM; CLU_000626_3_0_1; -.
DR   InParanoid; Q6FP05; -.
DR   OMA; YDWKYTR; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; IEA:EnsemblFungi.
DR   GO; GO:0061908; C:phagophore; IEA:EnsemblFungi.
DR   GO; GO:0032991; C:protein-containing complex; IEA:EnsemblFungi.
DR   GO; GO:0120013; F:lipid transfer activity; IEA:EnsemblFungi.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:EnsemblFungi.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0030242; P:autophagy of peroxisome; IEA:EnsemblFungi.
DR   GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR   GO; GO:0044805; P:late nucleophagy; IEA:EnsemblFungi.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR   GO; GO:0061709; P:reticulophagy; IEA:EnsemblFungi.
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..1587
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000215828"
FT   REGION          128..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1587 AA;  179236 MW;  6EED9DB8034333FB CRC64;
     MAFWLPQNIQ RRLILYVLQQ ITLFSNVDIT KLDVSLGSHS KFTFQDVDLN ISEMNISGCE
     VNSGMLGKLM LGLTVSGDVH ISGDNIDFMI TMINEDDFND MNSFSLAKSF YDLTSSIMQF
     KPDAHLKNEI SGSGSDSPRI PDDYTNPSSA GGNPTTNTYD IIVDDTASST TESDDSSPID
     SIPTSRFNIM QQKVIATALA KLKITLQSVR IRINLGKRKD CNCLDVVVKR IDMSTSEGHV
     RNFDANGISI AYINNEPSVV PPNNMDMAES LYFSQADASS IYMSALSDAN TDIKSLDASV
     FNSERYELLS INGMSFSFVG ISSIDDFAIS RIKINLGTLQ VNIPFLLKVR EDIILTMIFK
     LISPRHTDKV DVKNSPAYKR FQNELHSNDT NLFSNLAIEE ILIGLSSNQK IILRAVDLES
     NEINGINLSV GDIDLVGLDM DWISETRPCF NASFGKSNTI IELANTIIRV SEHDLILFLK
     IYYEIMDFID FVLSKWKILG VKQVSQLRND EKFSLNVGSL VIEIPLDNSI LEINIPNIEH
     DSLNQDLKLY EVNMTHIVES IKISSLKLKE VSIDLSSARK KMKCYNEHFS QYFVFTHYKV
     QITGIDSQIN LKSLWIIGAV IEQFYIASPV QEYPEATNKN SVRFHDNNKR LLSTSLMINK
     RAILAKYIIE LDDIKVCISG FDADQIRHCK FSLQRLLFLN QIDKGLLFNI FQPHVEIKFF
     SGSLNDIIRS TNIGVSGQPH LILCIFADKK IKVSIKDIMI FYQAKWLDSV QRNASLDQEK
     GQNVEYSELP EFSISIRDSA INFLPFRINP SLVILFESII VTKSGNDALI NMHSKVGRFY
     LTDNYDHLKT TQVMNKTICD SLIKSGYSQI GKFEGLSMTL NKKHKIVNCN GCLEKVILSV
     CSDSFHTLVQ LCMDLKVPVT FPDDKKYQPV PSVAVDLFET IEENEFNLSN LDNKDIDKSI
     GSDSDSLHIV NSFLDEVEDF QFHEDYNSGT VWSHTTSDTH SSSDILPISL KEEYLDSRRT
     EVQKHSQSND RNIISEIDFD IKNADIRLYD GYDWRYTRKN VSSAISELEE GLLSGIQRQE
     QTESELSRTT VFDSICIATK QKDLGNLKQI ISEQVQGKHD HLNSDKVYLY PSKHYKSLIK
     ANELIFKIKI YDSNSPRNEE FNNHAAKLFQ ITASISTYEV LDNLPTSTWN KFVTLLKKEA
     WPKSEPMLYF DFMLFKPINS LEATEATINI RSAPLRIHAD QYMVDFLLRF FQFNDKRFEL
     IDEYPEILFL QKFKSNTIKL RIDYKPNKTS SGMYSGKISD LINLFVLDES KVTLKGVVLH
     GINGFNELSE QLVKIWGNDV TSKQIFNILQ GFAPVKSFIA LGAGAQTFIT VLLAEYKRDR
     SISRSVKKSG NIFIKTTTGD FIKLGAKLAV GTQALLENTE GILSGNATQN RTLADVSQTN
     KVLDLDSLLQ QDQVLIGRNP KIRNKSPSAI IIDAADLEES GRPKVVSLYS EQPLDLHKGL
     EEAYHALEKH IQIAYNTIWQ TNQELRGEES RSAKAAAVTI AKAAPVAVIR PMIGATEAIA
     KTLQGIYNQL DKSNIEEIND KYKKEDN