ID   ATG2_KLUMD              Reviewed;        1499 AA.
AC   W0TCD0;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Autophagy-related protein 2 {ECO:0000303|PubMed:26442587};
GN   Name=ATG2 {ECO:0000303|PubMed:26442587}; ORFNames=KLMA_50633;
OS   Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
OS   (Yeast) (Candida kefyr).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=1003335;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DMKU3-1042 / BCC 29191 / NBRC 104275;
RX   PubMed=25834639; DOI=10.1186/s13068-015-0227-x;
RA   Lertwattanasakul N., Kosaka T., Hosoyama A., Suzuki Y., Rodrussamee N.,
RA   Matsutani M., Murata M., Fujimoto N., Suprayogi X., Tsuchikane K.,
RA   Limtong S., Fujita N., Yamada M.;
RT   "Genetic basis of the highly efficient yeast Kluyveromyces marxianus:
RT   complete genome sequence and transcriptome analyses.";
RL   Biotechnol. Biofuels 8:47-47(2015).
RN   [2]
RP   IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26442587; DOI=10.1074/jbc.m115.684233;
RA   Yamamoto H., Shima T., Yamaguchi M., Mochizuki Y., Hoshida H., Kakuta S.,
RA   Kondo-Kakuta C., Noda N.N., Inagaki F., Itoh T., Akada R., Ohsumi Y.;
RT   "The thermotolerant yeast Kluyveromyces marxianus is a useful organism for
RT   structural and biochemical studies of autophagy.";
RL   J. Biol. Chem. 290:29506-29518(2015).
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   -!- DISRUPTION PHENOTYPE: Still forms preautophagosomal structures (PAS) in
CC       proximity to the vacuolar membrane (PubMed:26442587).
CC       {ECO:0000269|PubMed:26442587}.
CC   -!- MISCELLANEOUS: Kluyveromyces marxianus proteins are shorter in length
CC       and have a more ordered secondary structure than their S.cerevisiae
CC       counterparts, which might contribute to the superior thermotolerance
CC       and solubility (PubMed:26442587). K.marxianus could be therefore useful
CC       as a new model organism for further elucidation of the molecular
CC       details of autophagy (PubMed:26442587). {ECO:0000269|PubMed:26442587}.
CC   -!- SIMILARITY: Belongs to the ATG2 family. {ECO:0000305}.
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DR   EMBL; AP012217; BAO41287.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0TCD0; -.
DR   EnsemblFungi; BAO41287; BAO41287; KLMA_50633.
DR   OrthoDB; 203302at2759; -.
DR   Proteomes; UP000065495; Chromosome 5.
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; Transport.
FT   CHAIN           1..1499
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000443867"
FT   REGION          211..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1499 AA;  168691 MW;  7A0BC4319D81168A CRC64;
     MTSWLPQNLQ KRLLLYTIKQ VSLFSNVDVS NLDVSIGSQS HFGFTDIDLN VCEINLPNIE
     VLSGRISKLN LQLAVAGNVE ISGEGMVFVL KPADGFFDDD SSEQWASSLT KSVMDMTKSI
     LDTELSEYQS KIYKDTNEDI KPPTALDSMM DKVLRVALSK LTINLKNVEL QLIISPELML
     KISISEVKMI SADEKRIADV IGVSAVFSKP EQSVPSYGSS SSDKEDDNTS DSEDPLSTSI
     TYSKLEATSI YLSAMESLVL DSLDGETYQF LNIDKIEVQF QGITSINDLK VHDLKIKINA
     LDIHLENVSS ILSHIMSLLN HVQLSNSEDK IRTQELKSYK RFQHEQNIEE DKTLTFVLLN
     SLKFHLRDNL FIMLTEISLN SSVSPYTSVS ISDIQLVLDS KEYINRSDSS EPFLSLNKNS
     STSEQKLHLN RDIKVEVDYS LMKQLILFAN DYMCLYNQII ERPSTYADPS ADPKFLLSSQ
     NVCFLLNLGD LIMEFHFSPF FSNIPHTTFK IPKLSIFSVQ NNEKSHIGEL TDFEFHSRKS
     GCFNISGANS KFCASNVNTK TKATLENLEV SILESDMNKI IQCLSGVLGS LPELLLSSGE
     TTSSKNMEKR SVRMMQSSAF LHNRTALSMF CVQINCMKIK ISNISGKAFG DLMITARKSL
     IYQDKYSDLS ISFTEFTAQR QYRSEKTDII FDINHDSNIA NFVINRTKVG KIKAYLTGVG
     IFIHTKWSEL FSGQKTENSI NEQKKNAKTL VSIPIDIKLY DCALSLKPCR LSTGLAINIP
     RAQINITKNE ITLSTKILDL LLIDDMNLIH ETDLGHTTST SNWYEKQGYS SLVKIDTLSV
     RFCPGGVAST RVNVHKIDSS ICSDSFNALI QTIIDLKPVV TYPENVKYQL EPELVSVFED
     LTDQYFTTAR ISENDLEIYP DTYSNSGESL VFEENYFSPK LESPSKNEVN MAVFEILSNV
     KISVDEIKLK LYDGYDWKHT RKEINSAVEQ LEENFKDGLS CPDAKVFDSI YIPAPRDEDE
     NIKSNINMKI HNEETKEGKM KLRPTKKYKI LIQGNGIKVN IQSGNDELRT TSTLPLSDNT
     YDILNETSVQ INNLEIVDNL PTSTWNKFLT RTKLKTTNTL QQSPMFSLRF TMIRPTPHLY
     ATELIFSVHV KPISLHVDQD ALEFLTLFFQ FKDPRFELID DYPDIPYIQR FEINSVKILL
     DYKPKKVDYV GLRSGKTKEF MNFFILDQAK INLKHVILYG IDGFSRLETI LTDIWTPDIT
     KTQLPGILGA LTPFKPFAGL SYGARALVSV PTEQYQQSGR LGTSLQKGGM VFLRTTGGEF
     VKLAVRLTSG TQTILESTEK LLGGQGSNGR NIKIKLVEGD EIVDAFIDES ILRSTTLFDN
     TANDNNHLDV ILPQGDTQKV ISLYADQPKD FYSGLHDAYS SFGRNLNITF DSMKQAKNDI
     KTANGAQEAV STVAKAAPLA LIRPLIGVTE ALSKTLQGLN NQYDQEEIAH IEEKYKSSN