ID   ATG2_PICAN              Reviewed;        1765 AA.
AC   A7KAI1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=ATG2;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=17204848; DOI=10.4161/auto.3595;
RA   Meijer W.H., van der Klei I.J., Veenhuis M., Kiel J.A.K.W.;
RT   "ATG genes involved in non-selective autophagy are conserved from yeast to
RT   man, but the selective Cvt and pexophagy pathways also require organism-
RT   specific genes.";
RL   Autophagy 3:106-116(2007).
CC   -!- FUNCTION: Lipid transfer protein required for autophagosome completion
CC       and peroxisome degradation and peroxisome degradation
CC       (PubMed:17204848). Tethers the edge of the isolation membrane (IM) to
CC       the endoplasmic reticulum (ER) and mediates direct lipid transfer from
CC       ER to IM for IM expansion. ATG2 binds to the ER exit site (ERES), which
CC       is the membrane source for autophagosome formation, using basic
CC       residues in its N-terminal region (NR) and to the expanding edge of the
CC       IM through its C-terminal region. The latter binding is assisted by an
CC       ATG18-PtdIns3P interaction. ATG2 then extracts phospholipids from the
CC       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, ECO:0000269|PubMed:17204848}.
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; EF102882; ABO31286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7KAI1; -.
DR   SMR; A7KAI1; -.
DR   PRIDE; A7KAI1; -.
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; Transport.
FT   CHAIN           1..1765
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000317811"
FT   REGION          218..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1188..1224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1746..1765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..243
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1765 AA;  195780 MW;  BD461261EEA9802E CRC64;
     MAPQWMPQNI QKRLLKYILQ QLSLFSEIDL PNLDVSLGTS SKVNLRNLEL DIEKFSIPGM
     YMRSGSIETL SLSLTISDGV NVDCAGVNIT LTPSLTPGKP NSTDQFSLAK STADLANSVM
     FEDNVVEDED IKETPSVDSN PLPPEIKDYR MSNMMAKAAD MALSRLQLTV RDVKITMILE
     TSHMEVCIEK VTLLSKEGTR YITVEGMTLN AIKPEVYSGE GVDNVDNSEE RDETESEESE
     DYDDELMQTS FMADNKDDIH NSLMESMMFA TQTSESVYMS ATSNVFSSTT PRASTYENHQ
     PSAVCVAYVS KCSVQFDGLQ NIENMQVNLG RIKIAASPIP ECLSSVIQSI RNLVRLSAMS
     TNETAGNTEK EPESDNTTLL NTLKIDEICV SFESALLKDG NFALDNTTCL SLSDIRFEQK
     NASFSFGSIA KIRLSRNDSK TELFCFDDSR APNVADLGLE ILNNDVSRIT LICPKSLNIV
     VDEHLLTLAA RYYSLMEPVI ETLISVISTQ TPYSYSNTHT SRFALHDTAN NQKSNEFHAQ
     TSSIHVKLQL NDFCITITIS PITYDSQEGR FDTSSILFEY NDPTLGEQYA SNQFLMISNL
     ETSSAGVNKI RSFDSSSLQE IWLKTKIKTI VEKATLKLNF DVLIKIISSF GKLADLVRKS
     MVTSLPVARQ KKVRMGSSLF LNATKMLKNC VEIKHCTIIF SHICPHFGDL KFSLKDIFVN
     FLQDGTLHSY VMSVLIQRIC DSVHESLLEA ADPRNKGYPM MFAKFKDNVG VHFKNCSFNY
     YGEWITLLES RERPREETNQ SSSASSATSK KRQVNFTFAD VSIGLVPVNL KSKIEVVIKK
     GIADLLIGTD GRSKLQSSFS SLTLLLIDDV ANILSDKESK SLRHWINANN NHAIWTLNAI
     LKSKGFVPVS YISSLFLNST FESERHLEKR MTQAFSGQKI FASIDTKIHA DALAVDLCAD
     SCQCLIQTLK DLKQPVQFSF NEKYKPMTDE VDVFKDVDET TFSASVSVDV DNLEQTEIPE
     NEKLEIVEDF FDKNLNSDSA EQSAIRSGSL SNSGTKSGAM SNIIFDDNHF GHSGEEFTTK
     VIPMAIGVSI SNVTIKLYDG YDWKETQTTI KNAIRRVEDK AAKIGDNMNE VTEGSTSEHV
     RSVSNDSTEL DTEAVNELLY ESIHVGLLAG QDPQSFYDNI NKSISNCGGS ENVSEHNNLS
     PGSSSPASVN TANSTRSAAS SHNIELGKVS SRRVRLKRSI YHKVLVELEN LDLSNLTMVN
     SEPHPTKNSI VFSEDESKDD SELVSRMDLS VGSFKVVDNV PTSSWNMFVG YLREAGDKEL
     GSSMLHAVID TVRPVSSLAA SELVISVSVL PLRLYVDQDT LDFLTRFGEF KDDRFTLPAL
     DEEEVFIEKF QVNSVRIKLD YKPKKVDYAG IRSGHTNEFM NFFILDESEM VLKKLVLYGI
     PGFARLHKML NDLWMPDIKR NQLGGVLSGL APVKSIVKIG SGFKELVAVP LKEYEKDGRV
     IRGLQKGALS FAKITGGELL KFGVKLAAGT QTILESTEEA LGGDGSAVRL PGYKKNTKSR
     RRTSPSEVIY ATSRERSLFG HNTMSGAVFH RNSFDSYGEE EEFLEGAPAL DGAGTQDAEQ
     HQKSRFLVPA VFKSTAELPD VLESDSDLDD YYDESDNEGQ KIVSLYSNQP ENLNEGLQTA
     YTSLGRNLDT AREAIVSAST RAARSGSAQT AAREFAKATP IMVIRPIIGT TEAISRTLQG
     GINILDPEEK RRSEEKYKNT KKEAG