ID   ATG2_ASHGO              Reviewed;        1525 AA.
AC   Q75E74;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=ATG2; OrderedLocusNames=ABL208W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 792.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS50563.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE016815; AAS50563.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_982739.2; NM_208092.2.
DR   AlphaFoldDB; Q75E74; -.
DR   STRING; 33169.AAS50563; -.
DR   GeneID; 4618818; -.
DR   KEGG; ago:AGOS_ABL208W; -.
DR   eggNOG; KOG2993; Eukaryota.
DR   InParanoid; Q75E74; -.
DR   Proteomes; UP000000591; Chromosome II.
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_0000215825"
SQ   SEQUENCE   1525 AA;  170849 MW;  BE65DF0A97B9012E CRC64;
     MSSWLPQNVQ KRLLIYLLQQ ISIFSQIDTT NLDVSLGCRS QFAFHDVELN VDHMRVPHIT
     VESGHISELE LGLVVSGGLD ITGDGLCFVV RPELSEVAGS HDLAQSLARS IMDLTNSMMQ
     PLPEVLEGDE VLANSCSEAG DAQQPASSSA LDKMRNKVLE RALSNLTVRI INVRIQVLFP
     GQQSITVLVG SVELSTVDKT RRVDLQDICI SHSELVPSPE QPDEFMSTSA SNSIYMSAID
     SLPFGSRSKM EENARNVRAL LQMDKLHVTF QGISSVEDIS IRDLMLHMGR VDVFLDAIIA
     VDIGVFEVLV QFVAEFQQDT EVSETSNTLQ NYKRFRQEQN LEEDLQITGF TIEELRITLS
     QSVKVSVIDI QLRNRYIENS TVTVGRVTIC DYDLDLLHID AGSKPCLELT VDSRKLQRII
     SVDGDIHMDI SSTFVSSLIP LIFRLQELGR GLHFVGTNNC KMSQEFKTQV ETKTIILSLP
     VGDDTLQMII QPISYELSLH TVFTDFISIS KVQSSETRDI AIIREIKIGY QTANFQVKSY
     NLKLSETLLT SKLRGSVSSV ELYCSDSDIK WLFDGLSPYQ DMITPYMHSK PEVRKPIMNK
     SVRILSASSV IHRQNVFSDM VLLIERITCS LSADSISSFG NVKTELNSSL LSLNTDNSII
     FHSSCVKGST VFSDVKYCLF EPIKTKDVTK PALFVQRFEN GKLKVNVQNT CIYYHAKWLD
     ILDESKGTKS TPQQESAVPV PLQQRIEVKF HDCALSMHPY RLKSALLICV NRCILDISVP
     PANFKCIIRS PTFMLADDCS NMKTSITESW ESLVRYYSKA GFAVIGKSGL LSCTIKQSGG
     QICLDIDVDR IDLSICADSF QCLIQTLIDI KPPVSFPDEK KYRTEPCSIP VFENVDDEFF
     VPKGTSNLPA LNDMHIVDDF INNSNNSFSE VQVIEETEEG SPLKLEDNGL LFDEGHFNKE
     DIPVATDSKF FPFGPVAIVL HLFVRKASIK LHDGYDWVYT RRSISKVVDD LEDEVHKQDQ
     PGRVETSLFD SIYLYATPDS NIKKAVSSNI QSEDIIAENY SSKMKLRPSK HHKILIELTN
     MKLTFSGYSY DEPTEDIADW STDLLNSIDV EVKTFEIVDN VATSTWNKFL TELKEAHGGS
     PSMLALSISL VRPIDFLYAT ELIISAQVSP LRLHVDQDTL DFLIRFSEFK DARFDLIDDY
     PDIVYIQRFE VNSIDVKLDY KPKKVDYVGL KSGHTSELMN FFTLDGAKMT LKRVVLYGVD
     GLGELHNCLS SIWTPDITRS QLSGVLKGVT PLKSIITLGS GVKALVTVPL KEYRQDQRLT
     RSLQKGARDF LKTTSGELIR LGVRMASGTQ AILENTEEFF GGQGARARCM SARLPEDELS
     PVPSACDEFD LFRSSIPRKQ SPIVPIPSEE DDIEPLKAIS LYADQPQNAQ KGVKEAYGSL
     GKNLTIAYGA VRRAQRDARH SISAQDAATA FARATPIAFI RPMIGATEAV SKTLQGISNQ
     MDRDQLVHMR DKYKQSSHYQ RKRER