ID   ATG2_USTMA              Reviewed;        2081 AA.
AC   Q4PFE7; A0A0D1E6P2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=ATG2; ORFNames=UMAG_01166;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003141; KIS71266.1; -; Genomic_DNA.
DR   RefSeq; XP_011387108.1; XM_011388806.1.
DR   AlphaFoldDB; Q4PFE7; -.
DR   STRING; 5270.UM01166P0; -.
DR   EnsemblFungi; KIS71266; KIS71266; UMAG_01166.
DR   GeneID; 23562264; -.
DR   KEGG; uma:UMAG_01166; -.
DR   VEuPathDB; FungiDB:UMAG_01166; -.
DR   eggNOG; KOG2993; Eukaryota.
DR   HOGENOM; CLU_000795_0_0_1; -.
DR   InParanoid; Q4PFE7; -.
DR   OMA; SSWQSLK; -.
DR   OrthoDB; 85474at2759; -.
DR   Proteomes; UP000000561; Chromosome 2.
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   InterPro; IPR026854; VPS13-like_N.
DR   PANTHER; PTHR13190; PTHR13190; 1.
DR   PANTHER; PTHR13190:SF1; PTHR13190:SF1; 1.
DR   Pfam; PF13329; ATG2_CAD; 1.
DR   Pfam; PF09333; ATG_C; 1.
DR   Pfam; PF12624; Chorein_N; 1.
PE   3: Inferred from homology;
KW   Autophagy; Endoplasmic reticulum; Lipid transport; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..2081
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000317814"
FT   DOMAIN          30..131
FT                   /note="Chorein N-terminal"
FT                   /evidence="ECO:0000255"
FT   REGION          226..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1324..1366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1324..1364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2081 AA;  226383 MW;  8663E2338B7ACE63 CRC64;
     MASYFLPSFL TGWDLSSVSA FSLSANLQKR ILSYLLKRTL GHLVDGGQLD LEQIDAGIGS
     GRIEVRNVQL DAQAISRHLP SLPITFVAGQ IGSILIQLPV PYFWNGELSI NVSDISIHAK
     PRSDNPEHTS SPQQDLSASF ASAASQLFVE DEEAKDLEQS IHESLYPENQ KQAQQRTEEE
     KGSLIATYVE ALLTRLKVSI EHVQIHLQSD ALDLSLKLSY ASMKSSNTRS EQQADASVSD
     SDQTCGTDSA AVPHRRLLSE TKRTLEMQSL ELWLQDNRKP SDSINAVSPS STDGSMDHLV
     SQPYKPSHEM SQSVASLQAS SASLYESAIG ESAFPESLEK PNQDPLHGDD ISSTAPPPLS
     GRHLLFSLGQ EAVLVTLKTT KERHEFLVSD TASRRVEQKL ISIVTDVDVQ IGNAGGIIFI
     DHLSLLMSLL QSFDLTSRHT QQESTLKGPK AQPMRTLSSA QTGGDFTLSC HIDSFNLIIG
     YDDPHVLQQD QSSLGAFWAR PSRAHPDFGH LRLRCNKLAA HYNHAQTGLS PAQSHAQIHF
     SVDDLGLFEQ LPTVLYQQCP PESSRVLPIL ILDPTLSQSG TDSPARAEHL QHDYASSTVD
     VSDWRYSPSH QTTGPRSHAT PDAQNAAKGA RFKSTSIRPG SSSSVPSSPL RTAYSDQGWK
     IKAPIKSQTQ ATAPEASLPC FVVSISLPQS CKDQGQVTAT VAPVHLFVDI SLVTRLMPGL
     RRFATAQIAA LQGVSEPDYE LTDSIATLGA SVATIQTSTD SLLGHHSTNQ AAAEPNPYKL
     DLQISFVRVD VRTPQVSYDA SALGGRSLSS VRLAGLDRRS GILVLQVQHL HLHLGLSETH
     QTASAVRFAS PSTSADGRHN RGPVVTGVIN AEKISAFLAL PSQSRALVLA LIEAIHDDAE
     VSTPFASSQN ALLPRVELSQ ITETAPGRGQ FDPRHGQAKD RCSILIPSIK VELEKTQLDS
     LQYMADDLTQ SVNLWTSDDP DESDSHDAEG LKILGSRFFG SRAGMSIMST STDSTATART
     STKNSSLLLT ITESSIRLWL PSLSPNTESV GDRRTRSAKS LLLTTTDFEL LFDSDKARNT
     NRIEIRIPDM QLSVEAGSAF AETSSTLLAF RTMERTLNDQ SRNMMLLLVL EAYAEPGTSY
     REQNIDLTLC SVTLAPSFDQ ELVPRIKRLL KAPAGVFENV EPNEVTRVSF KAKDCSVFVA
     PQGTQHRAAV AIGEASVKTK LTSHAPKTSI KLAIAGLDVF AIEAESSQSS SRRRAADKSA
     SDHWSKRGYA RLLHAPESKV SIHLNTLTRP EVDVKVTKLR VKLQATADTL NVVTGLVGAI
     TETQAAGSTE SRSASPLPHD SFMSSTDSEY SNRSNLSEKE VGPIQTSKTA DHFDRMAELL
     SGIEDDAYHL ASPLPVAADL VEDDVPSDAA FLGSKGRYHP DIVETTLDSD EFFGGESVAS
     LSLLAPRADT VIFADEDVTV RLLDPKGICP VQEYFTDPGL RPHVNSALGT AASSVRVRVS
     NFDLSVRLHS GYDWPSTRNA VQQEVKLVRK RLQKIKQLLA EGQVPDDSVE AATSNLLDSM
     HISLPNVAAE MDADEMMRAV EDEVGDCSDA ASTTDSDASA SWQALPFVRR DRQASRLDHR
     RAEASHTKLE RSAGSLIDFN LRGLEVEFDK ADASLAGNVV SRIAVNARRF EIIDNIKTST
     WRTFLTEMQD ANSALRHDVE SKMVKVEIVY VRPQGLEPEG ASVEQPEVRM RARLAPLRLH
     VDQDALDFLK KFFMFKPPGQ KETSGAAAAT SGSALPFVQF AEVLPIKIKL DYKPKRVDYN
     LLRQGKTIEL MNFFHFEGSE MVLRHVTLRG INGWARLFDT LNDIWTPDVK ANQLADFLSG
     LGPIRSLVNV GAGLADLVLL PIEQYHKDGR VLRGVQRGAA GFAKTTALEA VKLGARLATG
     TQVILEQAEH ILGGERMEES ITASAIGPES GQSFQSLSES VMVERMSRSG SVSRYAQQPL
     DMRDALAQAY SGLTDHLTSA AQTILAIPMD VFDASDLAGA PTTRSSEHTR SRPVVKAVPI
     AILRGAQGAS HAIAKTMQGV QVALGDRQNV DEQKYKLPPH T