ID   ATG2_YEAS7              Reviewed;        1592 AA.
AC   A6ZRK1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=ATG2; ORFNames=SCY_4562;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000067; EDN62583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZRK1; -.
DR   SMR; A6ZRK1; -.
DR   PRIDE; A6ZRK1; -.
DR   EnsemblFungi; EDN62583; EDN62583; SCY_4562.
DR   HOGENOM; CLU_000626_3_0_1; -.
DR   Proteomes; UP000007060; 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; 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   Phosphoprotein; Protein transport; Transport.
FT   CHAIN           1..1592
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000317816"
FT   REGION          264..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         236
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53855"
SQ   SEQUENCE   1592 AA;  178398 MW;  146265063015825B CRC64;
     MAFWLPQNIQ KRLLLYVLQQ ISLFSNIDLS NLDVSIGSKS HFSFHDVNLS LDDLNIPNVQ
     INEGIVDELV LKLTVSGGVE IDGSGLRFIM TPLYSSGSQE LHSDFLVKSI QDLTNSMLQF
     SDPLTTYNRY KEDDISSSDS SSDLNSNIEA SKPAANGSYT LQNMRNKALN VALAKLKIAL
     KDVTIRFIVN DRDPSDNIVE VHLESIQLIT TDANLRHINI ENITISSIQK QAVPDSPVHP
     FNNDDLSQSV YLSKMEATSL YMSAMEEQSN EDPSEPQVTQ EEQENDKCKE SLMEINNLNI
     AFKGLSSVND LRMSNIVIDI QDVHLAIHKI VEIKNSTLKN IIDIIVTHLD ANESFSCQDS
     QSPSPDKQEP SALSSVDIKC IYLNLGQDIT VILKSFKLEQ KENNSLAFSL GSFYSNSSPL
     TISHKTKPLL TGEQTPQSIA LNMGDELDII ISHDGIAHFF KIFQFVSKCM SFYQNKSKGM
     MPQIASDTKR TVQLTSKAVK LSLKFPYFLL CFQVSPFIYD SNRELYIELV DVFKKLPSRC
     TKILTMSSIT ISNLQSPLQL GSYDDTLKEA LIYSSVHAII KEVIFNEEYS GIVQLVEDIS
     AFGKLFTDSK NSECTGKSKS KRGSFLQRSV RVLNSSRFVY KQSLSANFSL KIDSMKLKVS
     EIIGPQFGSV EALLSNNFFA ITDDSQIVYF TKNLKVERKT PSLLEPQEIM SVVLNKAVNE
     PVLYVHRRAN GKLKVIFNNI RIHYYARWLE ILKKNIGPDN ASSKDEPVAQ KLSKKQPTSG
     FPWELKCLDC SLILHPFRLK SVMVIVLDNL TTGGSSFIPQ AKLLSKANTL FLIDDYQNFK
     IQKDKNWPSL INFYAGQGFS AIGKIDTLNF LINKSDGALL LDCKIEQVGL SLCADSFQTF
     CQLCIDLKYP QTFPDEEKFR TQLKNPIDVF KDIDCDLFNS AFIRENNHQN DYDSVHLVDS
     FLDKTHEFNN GARSKLSSQG SYEMDSSSGT ATGGILLPHE SYLDSAQPKE EDTPPIASKE
     QERDVDIRGS IDIEKVVIKL FDGYDWKYTR KFIANTVEKL DKELSKAEAS SSKSNVPQSE
     ANIFDSIYIS ANKNNVTDLR RNLDGEIQGV QNSFSDVSKV NLRPSKHYKA LIQLNKVHVN
     LKNYRVDEPD ESNSDNSTDV LNRCVVSVYE FEIIDNVPTS TWNKFVTLLK HEPWPHSSPM
     FLLDLEFIRP IDFLQAVELV MQLNVAPLRL HVDQDTLEFL IRFLGFKDKR FELIDEYPDI
     VFIQKFSTNS IKLRLDYKPK KVDYAGLRSG QTSELMNFFT LDGSKIILKS VVLYGLNGFD
     ELNNKLKAIW TPDITKKQLP GVLEGLAPVR SFMAIGSGVK TLVTVLMSEY RQEGHLGRSL
     KKGGNVFLKT TTGDFVKLGV KLTSGTQAIL ENTEELFGGV GSNGRVYDAS KFGSADGADS
     DTAAVLDLDT LFEEDQLVGS KYSRIRDHEP TAVVIDMSSP GDHNEPTIVS LYADQPLDLP
     TGLKEAYSSL EKHMHIAYDA VWRAKGQMKD DKRGGPSAAA VYVARAAPVA IIRPLIGATE
     AVSKTLQGIA NQVDKTHNEQ INDKYKSNRT DS