ID   ATG2_PICPA              Reviewed;        1862 AA.
AC   Q9HFR4;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   23-FEB-2022, entry version 87.
DE   RecName: Full=Autophagy-related protein 2;
DE   AltName: Full=Glucose-induced selective autophagy protein 11;
DE   AltName: Full=Pexophagy zeocin-resistant mutant protein 7;
GN   Name=ATG2; Synonyms=GSA11, PAZ7;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11533052; DOI=10.1074/jbc.m104087200;
RA   Stromhaug P.E., Bevan A., Dunn W.A. Jr.;
RT   "GSA11 encodes a unique 208-kDa protein required for pexophagy and
RT   autophagy in Pichia pastoris.";
RL   J. Biol. Chem. 276:42422-42435(2001).
RN   [2]
RP   FUNCTION.
RX   PubMed=11856375; DOI=10.1046/j.1356-9597.2001.00499.x;
RA   Mukaiyama H., Oku M., Baba M., Samizo T., Hammond A.T., Glick B.S.,
RA   Kato N., Sakai Y.;
RT   "Paz2 and 13 other PAZ gene products regulate vacuolar engulfment of
RT   peroxisomes during micropexophagy.";
RL   Genes Cells 7:75-90(2002).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=14536056; DOI=10.1016/s1534-5807(03)00296-x;
RA   Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y.,
RA   Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.;
RT   "A unified nomenclature for yeast autophagy-related genes.";
RL   Dev. Cell 5:539-545(2003).
CC   -!- FUNCTION: Lipid transfer protein required for autophagosome completion
CC       and peroxisome degradation (PubMed:11533052, PubMed:11856375). Tethers
CC       the edge of the isolation membrane (IM) to the endoplasmic reticulum
CC       (ER) and mediates direct lipid transfer from ER to IM for IM expansion.
CC       ATG2 binds to the ER exit site (ERES), which is the membrane source for
CC       autophagosome formation, using basic residues in its N-terminal region
CC       (NR) and to the expanding edge of the IM through its C-terminal region.
CC       The latter binding is assisted by an ATG18-PtdIns3P interaction. ATG2
CC       then extracts phospholipids from the membrane source using its NR and
CC       transfers them to ATG9 to the IM through its predicted beta-sheet-rich
CC       structure for membrane expansion (By similarity).
CC       {ECO:0000250|UniProtKB:P53855, ECO:0000269|PubMed:11533052,
CC       ECO:0000269|PubMed:11856375}.
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: Prevacuolar compartment
CC       {ECO:0000269|PubMed:11533052}. 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   -!- DOMAIN: The C-terminus (1237-1862) is required for the location to the
CC       perivacuolar compartment. The absence of either ATG1, ATG18, ATG9 or
CC       VPS15 also prevents the correct location.
CC   -!- SIMILARITY: Belongs to the ATG2 family. {ECO:0000305}.
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DR   EMBL; AF309871; AAG30292.1; -; Genomic_DNA.
DR   PRIDE; Q9HFR4; -.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR026849; ATG2.
DR   InterPro; IPR026885; ATG2_CAD_motif.
DR   InterPro; IPR026886; ATG2_fungi/plants.
DR   InterPro; IPR015412; Autophagy-rel_C.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   PANTHER; PTHR13190; PTHR13190; 2.
DR   PANTHER; PTHR13190:SF1; PTHR13190:SF1; 2.
DR   Pfam; PF13329; ATG2_CAD; 1.
DR   Pfam; PF09333; ATG_C; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   Autophagy; DNA-binding; Endoplasmic reticulum; Lipid transport; Membrane;
KW   Metal-binding; Protein transport; Transcription; Transcription regulation;
KW   Transport; Zinc.
FT   CHAIN           1..1862
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000114939"
FT   DNA_BIND        632..659
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          129..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1251..1279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1316..1343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1253..1279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1862 AA;  208598 MW;  1CC87BEC1FA21EF8 CRC64;
     MAAWMPQNIQ KRLLRYVLQQ LSLFAEIDLP NLDVSLGTNS KVHLKELQLD PDKVDIPNFY
     LRNGVVDDMD LTLTLSNGVN IEATGVNLTL APSMTNGVDF DPGKLSFSLY QSTADLATSV
     FFVDQDNNEL PKTDKELDDE HDSSKNVAND DDSSPLADKE NPKQPSKMGN MMAKAVEMAL
     SRLQVQLKDI NLTIITDEST FQICIEEASF DTTDGVRKIE FKGAELSVLK PSVYPGDQPQ
     GESQDDSEDD DSVDESSSFD SHPTDFMSSS FIGSREELEN SMLNSQSSVY MSATSKLLTK
     PKHSTRHPSE TKPSVTLGHV NEGTLTFEGL QSFENVSIII DQIHVAVSPI PESLTALLET
     LSKRLKILRV HSAKSKPSTT TTYTFSSKDG LQEEPEFSDQ ISTSSSTGFK ELKINEIVIS
     LNSALGKNGA FAIDNSLCLS IESLELAMVS EGNLSGTLKT LKMNKSETSE VFSFQPGSNY
     DVRFEMILDD DNDLYNITIL CPKPGVFNLN EEVLNHLLSF CSKIPSTLHS LQSYQYQKAK
     LASLSNPQSN SNNDQENEIY LQTASFEFIL QLTSSDKVKL TSFPLSFNSN TGVIEVERIV
     VERKFKENQV QGDPPSQDRF KMQPHKSTNS GCLTCRKRQV KCDERKPFCL NCEKSEQKCT
     GFTHLSKDLP SSSSSLSSDD SYKSILLING LKTYLFKKPK KVKTFDKSGI QCSYLSPNAS
     EIELIELEMT MSDFTSLIDS LELFFEQLKV VNHPKMDIAK EKTVFRTSFN SRNPVRNPRA
     LGSQTGAMFS HSSLVSFLRI NSVSFLLKEA LNGFGDVSGR IKSINCNFHV KGFQDFFVGS
     LDVARIHKLS SQLILEKVDA PGNKKPMLIA RLKSSSLTIQ LADCLAHYYG EWFSFLHQCN
     MKEREIVKRQ EDIGPKDRAR DSNNFVISLH LNNIIIELNP VSLKSKAVLF IKKGCGTVTF
     GSQRLSISSS LTEITPLLID DTKNLKNEIK LDSKNSHPLG NSFLLLLMDM GYISMGMLSS
     VSVSFETESS ASLIAPVNVN VMCDTLRLDI CADSLQCLLN LIKDLRQPII VPFEQKYRTQ
     PETPLDALKD VDFDAFLPQK TKDSNNVAAT KTRTFSETAL NGAFRPKVYS DGSLEIIDNY
     YEHESVNQGL DNRTYGDLEV FEENSEDDIS LENSLNMKHD HFYHTSFMDN TRNTEHVPFK
     LNLSVEAVYI RLFDGYDWKE TRVSILNAVR RVEAKAAAEL SRIEKIRNTK LRRDSSASNS
     GNEGSLQTDD DSATSGSVSE PVIEETLYQS IHLSLPVGME PTLLAERVNN DVNFKRASSD
     SLDKTQSPSS VSSKSQVSSP QTRRLKLKRS TFHKVALELR NLSITFKLLS SFDPTTIKNK
     SSIRNPNSAE IVNRISVEVD DFLITDNIPT SIWKTFVTYL KEAGSRELNS KMVHLDIATI
     RPTRLLATTE MRIETNVLPL RLYVDQDTLD FLTRFGEFKD LRFVPQVVDD DDLFVSKLHV
     FPVRLKLDYK PKTVDYAGIR SGKTSEFMNF FILDEASIGL RKGWTWIGGL NNQVNSHTKR
     EYGTPDITRN QLKGVLSGLA SINSVVKISS GFKDLIAIPM EEYRRDGRLI TGVRKGAFSF
     AKTTGNELLK LGVKLVAGTQ TILENTEQVL GGEGNLARMP VQVKERKQRR DSDEGNFYVI
     TDRQTYERNL KKTSMNESII GKTSLREANR FDEEYDDDDD DEDDLVNKIK PHLRNTMLDS
     QLFLDDNEIE DEXRGARRPD ESQKTISLYA NQPTTMKEGL QLAYQSFGRN IDSAKRAISK
     ASSKVSEDNR TSNIAYEVMK ATPVVVLRPI IGTTEAVSKA LLGGLNQFDP DNRSKSEDKY
     KQ