ATG2_BOTFB
ID ATG2_BOTFB Reviewed; 2160 AA.
AC A6S7C7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Autophagy-related protein 2;
GN Name=atg2; ORFNames=BC1G_09010;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476893; EDN29064.1; -; Genomic_DNA.
DR RefSeq; XP_001552828.1; XM_001552778.1.
DR AlphaFoldDB; A6S7C7; -.
DR PRIDE; A6S7C7; -.
DR GeneID; 5433341; -.
DR KEGG; bfu:BCIN_14g01550; -.
DR OMA; HRWDSTQ; -.
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; 1.
DR PANTHER; PTHR13190:SF1; PTHR13190:SF1; 1.
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..2160
FT /note="Autophagy-related protein 2"
FT /id="PRO_0000317806"
FT REGION 113..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2160 AA; 235467 MW; 3E52224A35A14486 CRC64;
MASYFQLSSM PKRLLQYALS SLEVFETDAL DLENLDIAWG KNSTFEFKDV GLRLKKLETL
LQLPSTIALS KAKVLLLRLT IPVDIYSSPI LVEVDGVDVQ LRVREEKGVY NPRTNHDRFR
KKSTSKNQGL DPTLPTAEDL AASFLQTESR EEKEELEAAI LGETQDVSES VTSNEGGDSP
VGTGTALSLP AFMARFLQGI VDRLQVRVHG ITFNVDLDIP AEGPTSNRTT DPVTVQLKID
DVDIEGVTHD IESTQTRGGK DITSLFKEGK RLVCLSNIQG ALITEANLFQ TLSRSSSVVS
PVPPHSDITE PRRAAEKERS SEETQVMSVE SAGGFDRVAS PSPPSSPASS LRVSESSLPE
IKRPSPPLRP VKTSPSVKAS TVANDSGQFD DASEDGHSSP SGSGIGDVDT SEMGDSLLQS
SAILDQVTDS LLLDHPEGND MRSSQSQSEH STPGENSRTS TPRASAHISS PSSQTPEFNA
FHSVNRAHNM LQSTMLPPRA HTRFSVERIS HSQPTLPPTT APLDRTYLVQ QSRVPSEDSM
SESSSSTFNE EIGDDLAQSQ LFSHEEAESM YMSAVSFTSA APIPGGWADS GTESEDARSP
PLTPTDYNFR GEKLDNLENA RHYIPSDGAS DIDSLEKSTI LPLRPLHASS RSIGSMRSET
PRQSRLLHKV SSDVSVKSTV TSDDYNRMTK QIFSLDQVAI YIPAMNDPSS DPVDAAAESA
LFGSTFDGHS DSHSNTMDLP GAFSTHLPRE QRSRSSPKPT PRVPTQPPQK PEENKSIEVD
VGNLLAQFDI SIGRLIYKLV CQIQESMKKK TQAATVSSKP TSSSPEPHLR VSAQTVSLKF
LEHLKGTLGS RIAEPQTKAL DSDVLLKTTI KGLNVSRNPS DTTTKTSVTL QKFIFGYAQE
NIVSFDAGLQ MRASTRDLAA SAGIDVSANI YQSHDGTRFE VHTLPLHVAV DLQHLDETFS
WFGGLSSVLN LGSSMASNTT VISSPVIKPK SKGVKFNTPI EPDDQTMAVQ NKADVRIGGL
ILDLVGTECS VGVETSAVKL ISREEGIGIG IDKIRLSGPH LRHSVDDPAI VIDVSTTRIE
FLNAPKDNDI DRLLALIAPS NSKYDQDDDI LLDTLLRQRQ QGSVLRLTVD DLQAKIGRLN
ELSYLPELGE EVARLSTVTK YLPDDDRPGL LSLVKIKKLG IDVDVNNSVG SLQLKATDLD
MAQIPIPSLV ALSVGTVSAY RNYSEELIGA GTDQVFNRPE LRIPSIMARL IGDEMEPIVK
IKLWNLRVEY RVPTLMVLLG LADTATGNEM SASITASVAT LRDLAQPQTP KGKEKGVEKR
PASSSSPAKP MTIDVVLKDC IVGLNPLGLP SKILAVLTEA HVAAVLPKDQ NASVTAELSK
ASLLVIDNVA HLASTVQSDH NRNSFNGGSN QVADLTSTGY VSVSYISSAK ATVLLSVDDD
GQNCLDVELR DDLFVLESCA DSTQTLISVL GKLAPPGKPP KKEENTYQTK VVPLNNLLAS
VSIDAFGTPE GQYEFSNDFT ELGDLTEEGE SELGFDSDYC KGSSDDGYKQ AVLDDVEDSL
ASLNLTARDT RDGVLLDSFA EEPEIDNVAL SFHEDHFGTG SSLEHSAHRW NSARNTYDTS
NYSKVKKSPL RVRVRDVHII WNLFDGYDWQ DTRDTISKAV QDIESKAIEK RARNERRSTW
EQDIDDDEDT ERGTFLLNSM WIDIPNSRDP RELAAAINQQ LNDNATETES IATTSYTVTP
SRQGGGRAAK ELRLNRTKHH KIAFELKGVC VDLVTFPPLS GETQSSIDIR VNDLEVFDNI
RTSTWRKFAT YMQDAGEREK GSNMVHIEII NVKPVPTLAA TEMVIKVTIL PLRLHVDQDA
LDFITRFFEF KVESDIEPEA PGEKPFLQRV EVNSIDVKLD FKPKRVDYSG LRSGRTTEFM
NFMILDGADM TLRHCIIHGC SGFDKMGQVL NDIWTPDVKE NQLPGILAGL APVRSIVNVG
SGFKDLVVIP MNEYKKDGRI VRNISRGAAI FAKTTGTELV KLGAKVAIGV QTVLQGAEGL
LGPQDSSLPH ANSSDDEDER KQISLYANQP VGVMQGLRGG YASLQRDLIM ARDAIIAVPG
EVMEDGNAKG VLKAVRKHAP TVILRPVIGV AKGAGQVLMG ATNTLDKKNL ERVDAKYKKH
