ID   ATG2_NEUCR              Reviewed;        2051 AA.
AC   Q871L5; Q7S752;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=apg-2; Synonyms=atg2; ORFNames=20H10.030, NCU08926;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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. Atg-2 binds to the ER exit
CC       site (ERES), which is the membrane source for autophagosome formation,
CC       using basic residues in its N-terminal region (NR) and to the expanding
CC       edge of the IM through its C-terminal region. The latter binding is
CC       assisted by an atg-18-PtdIns3P interaction. Atg-2 then extracts
CC       phospholipids from the membrane source using its NR and transfers them
CC       to atg-9 to the IM through its predicted beta-sheet-rich structure for
CC       membrane expansion. {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=CAD70986.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; BX294024; CAD70986.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002240; EAA31372.2; -; Genomic_DNA.
DR   RefSeq; XP_960608.2; XM_955515.3.
DR   AlphaFoldDB; Q871L5; -.
DR   STRING; 5141.EFNCRP00000008074; -.
DR   EnsemblFungi; EAA31372; EAA31372; NCU08926.
DR   GeneID; 3876755; -.
DR   KEGG; ncr:NCU08926; -.
DR   VEuPathDB; FungiDB:NCU08926; -.
DR   HOGENOM; CLU_000626_1_0_1; -.
DR   InParanoid; Q871L5; -.
DR   OMA; HRWDSTQ; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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..2051
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000215834"
FT   DOMAIN          31..121
FT                   /note="Chorein N-terminal"
FT                   /evidence="ECO:0000255"
FT   REGION          108..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2051 AA;  224212 MW;  6BA27D937BBDA886 CRC64;
     MSFFYRSFAN SLLPKQLLRF ILARLDLLDS QALDLDNLNF ALGRNTVLEF RDVGLILSKL
     EALTNLPPTF KIQKAKVLLL RITIPVDIYN SPIIVEVEGV DTRIRVASKQ EQDEQTAKNK
     KGTHKDGDEV VPTAADLAQS FLQTEIPTDE QRRLEKALAE EAQEALSESM SDSETDDDGS
     FATFGTGQGL SLPTFLTNFL QGILDRLQIR IHKVTFQLDM QVPVEPGLST IELVTFQLAL
     DEVIAEGVTA PGQQKDGSPA IVPREGKRHI LLDNLRAFLI TEANVFSSLL PTQSAQSLVK
     PQGPAPHDVP STLRDMSGSM QSSVGGLDMS ISPDQMEALD MLAQSQYEVR DSEDALNIPY
     ESDTQYPEAE ENVAGSSPLS TPRASMYQEH DTPMLQDHAN SAIMQHQPEL WSSYERGIRS
     EPSLHPPTSF QPQTMPSGAV SPAPSEPSSS ASSVRSDDDT PSADTEDLAQ SHLYSHEEAE
     SMYMSAFSDA HSTLMPGAYM PGGWGAESEG GESASERDLS TTHPVAGEPQ SSTPVVSELA
     SPTPIPEQNP TAQGYEPQHE DTSTPRGITR MVKEIVSLDS ISVYVPSTRK QVLAPVTNLA
     KSNPNLPGAF SVHQSFHSST TDQSTLLTPE NLKEDRQDYA IEIVLKPLTL RFDSSVGFLL
     AMVVTRLLEA FKGSSDEGAE VKPSSTESIL PDIKVCLEQV TMQFLEELTG VADSAKRIYE
     TQKPNFGSDV LLEASLTNLN AFTHQSGSQT EVNVSIEKFA FGYADEAIVS FTGEADLFQS
     TATVDMLSVG KDIAVKATIT PDVTRVDVKT LPLYLKLDLQ RLDETFSWFG GLSGFLNMGA
     SEDSVAKAVQ IPAKPPQKTR GVRFETPIDP MEKRSGSKID VRINGVHVDV IGKDCRAVLN
     TSALKLVHRE EAIAAVLKTI RLSGPYVRNS HARAPVVLEL DSTRLDYILT PRTRDLERLL
     ELITPSKVKF DEDEDEIMVD TLLRQRRKGG VLGLEVKNFK VRAGNLALLD CIPSLVDDLA
     KLGTVAKYLP EDDRPGLLTL GQVTNVDCEV DVGGRFGVVN ARLTNLELAQ ITVPSLVAVA
     VGVVTVNRNE NSPIEEELVS TSTAHAPGSS KAPVLMMRMI DDIEPVLKIK LFGLNVDYRV
     PTIMDVLGLI QEETTPEEFE ANLAASVANL GGQATAALRR QDTPESPVVD KEFKPIKLDV
     AFRDCVVGLN PLGQDSKLAI VLADSHLEAI PGKDSTLDAT ATLKKACILL IDDVKTLQDV
     QINARGRAPA MSTPQALELC SKGFVSICEM SSAKAVVKVG KDENGESHVE VSVRDDLLVL
     ETCADSTQTL ISLANALTPP TPPSKEIKYR TSVLPVEDLF ASITPDAFGR AEGEYDFDDD
     FAGAQGIECG NEDDDDYYGI GSTEHLEIQS EGYGVAEELF DATNSSLLGD IEVENTNDGM
     LVSTANLDVP PVSSQSESDL DIQENYFSSE PVKNTTLRWN SRKNLYDQSS DAQVFKSPLV
     ICVRDVHVIW NLYDGYDWVR TREIITKAVQ DVEAKAYERK ARADRHTYED EGDEESVVDD
     CLFNSIYIAV GPNGDPSNLR RAINQELQYQ DTTTETESVA TTAFTTSTVR ASGHRQSRPR
     GKTLKLSRSK NHKITFELKG VNIDVVTFPP GNETINTIDV RIHDLDVFDH IRTSTWKKFA
     MYDIDAGERE LSKHMVHLEV LNVKPVPDLP ATELVVKVNI LPLRLHVDQD ALDFITRFFE
     FKDETQPIHQ SSSDVPFIQR CEVGDVPVRL DFKPKRVDYA GLRSGHTTEF MNFVILEDSR
     LVLRHVILYG VSGFDKLGKK LNDIWTADVK STQLPGVLAG VAPVRSLVNA GSGFKDLIEI
     PIREYKKDGR IFRSIGKGAT AFAKTTGTEV VKLGAKLAIG TQYALQGAEG MLAKNPPNYN
     HAGPSSSSAG VPAGVDYEVW DEEDFGDHHT PKAISLYADQ PLGIMQGMRG AYASLSRDIA
     IARDAIIAVP TEVMESSSAQ GAAKAVLMQA PTILFRPAIG VSKAIGQTLL GATNALDPNH
     RKRIEAKYKK H