ID   ATG2_VANPO              Reviewed;        1566 AA.
AC   A7TM79;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=ATG2; ORFNames=Kpol_529p26;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480420; EDO16646.1; -; Genomic_DNA.
DR   RefSeq; XP_001644504.1; XM_001644454.1.
DR   AlphaFoldDB; A7TM79; -.
DR   STRING; 436907.A7TM79; -.
DR   PRIDE; A7TM79; -.
DR   EnsemblFungi; EDO16646; EDO16646; Kpol_529p26.
DR   GeneID; 5544805; -.
DR   KEGG; vpo:Kpol_529p26; -.
DR   eggNOG; KOG2993; Eukaryota.
DR   HOGENOM; CLU_000626_3_0_1; -.
DR   InParanoid; A7TM79; -.
DR   OMA; YDWKYTR; -.
DR   OrthoDB; 203302at2759; -.
DR   PhylomeDB; A7TM79; -.
DR   Proteomes; UP000000267; 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   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1566
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000317815"
FT   REGION          137..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1566 AA;  178304 MW;  26E0314870BD5816 CRC64;
     MPFWLASNLQ KKLLLYILQK ISLFSNVDLS NVDVSLGSNS KFAFHDVRLN CDDIDLPNIE
     VKESTIQQLD LQLTVSGVLN ISGESVIIVV KPKVDNESNS SKEFSLAKSL HDLTASMIQF
     PQSFDLDEIK NMKTNQNEYD NDIIGSSSSS GNENDIDIYN SSSDEKNEKE SESTGTMKSM
     KNKILSSVLS KFKMELKDVI LKVILQDSAY IEISIDKVSL ANKPDDIRTL IIDQVRIDHV
     KSIVEEQEIS FNRRMPNNLE QSKSLYESNS LYMSALDEIQ HNPEIDLKED RLELLVVKHS
     NITLTGLSTI ENFNLKDLDI TVDHILCSYK NLLCIDEMFF DDVMGTLNSF ISNSNNSPRS
     STAYKRFQIE NDLYENDRKL KLSINTIIFL VDDHISVSLS NFNLDQSEKN EFKINLELMK
     LNDLTTDRSM VFSPFLEAFI SNSVLTLNFL SDLDFYFEKD FIIGLISVCQ KTSKLMNTYN
     RKKNANKRPR EPGRNNIKFS ITTKNVSFKF KLDQSYILIR CDPIIYDWKT DKLAISKIEF
     LNDLNLQKLE RFITVDSLIL KFSNTPIQCL AYDEHFTKCA LITKVLLNIK NICFRYQYHK
     LLQLYGSILE IIDEATRFEK SKKLSKRGSH LRNTVRIMNS SSIIFKKKLN ANTIISIDNI
     DAQFDHFLNE EFGKMVLGLK NNLIALKENS EVYMLSKTLS IDRLLKERRY PILSCLLNSN
     SQEPTLIFEK KVRNKLKIYI KNVCLHYYAR LLPILTKMDT DLKKENSDAD HNSLFIDIKI
     SNTAVVLHPF RIKPALIVIF DSLSISSDFL KCTHKIFFKH GCLLLIDDIG NMKVSSKQPW
     SSLSNYYLQR GFSAIGKITN TNVNIKTDCN GVEATTNVES LGLSLCADSF NTLISLLIDL
     KIPITFPDED KYNIEVPEDV DVFADVDMSF FDPIHIKETE ELIIGGESVH VVNEFLDDFH
     DEVEISEKVA SPKKFFNDYI SSHRITQPLE LEESYIDRVD LDTTLEFTEM EFTAFNLDIK
     KISIKLFDGY DWKYTRKSIS NTIDMVGREI EDYEADDDQN QPLHATIFDS IYISTTKSDV
     SNLKSRVNNE IQGESNPTGF IPKVNLKPSK YFKTLIELNN VNINFTGYPN QELVESRSKD
     TSTILSNIKV VVDTFEVIDN MPTSTWKKFI TLYRHDKWPT GLPMFASEFS LVQPINSLQA
     TEMIMALNIS PLRLHIDQDT LDFLLRFFEF RDVRFELIDD FPEVLFIQKF TMNSVKILLD
     YKPKKINYSG LRSGHSSEFV NFFILDGAKL TLKNLKLYGI NGFEDLSDSL KNVWTPDIIS
     SQLGGIIGGV SPLKSAITIG TSVKKLVSVP ITDYKQDGKL SRSIPKAVNI FLKTASGDFV
     RLGAKMASGT QAMLENTEEF FGGTGSAGRT FAIPEKFLDI NNLVEEDQLV GGSNPKVKNH
     RPVAVVIDAS KMELGQPKIV SLYADQPLDV REGLEEAYHS LERHLFIAYN SIKNRSTNMD
     VLESPTMTVL SMAKAAPIAI IRPLIGATEA LSKALQGISN QLDKNQIENN KDKYKSTTII
     DRKLVE