ATG2_SCLS1
ID ATG2_SCLS1 Reviewed; 2159 AA.
AC A7E6F5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Autophagy-related protein 2;
GN Name=atg2; ORFNames=SS1G_00880;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476621; EDN91477.1; -; Genomic_DNA.
DR RefSeq; XP_001598791.1; XM_001598741.1.
DR AlphaFoldDB; A7E6F5; -.
DR STRING; 665079.A7E6F5; -.
DR EnsemblFungi; EDN91477; EDN91477; SS1G_00880.
DR GeneID; 5495034; -.
DR KEGG; ssl:SS1G_00880; -.
DR eggNOG; KOG2993; Eukaryota.
DR HOGENOM; CLU_000626_1_0_1; -.
DR InParanoid; A7E6F5; -.
DR OMA; HRWDSTQ; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
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 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; Reference proteome; Transport.
FT CHAIN 1..2159
FT /note="Autophagy-related protein 2"
FT /id="PRO_0000317813"
FT REGION 98..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2159 AA; 234930 MW; 21E312FC04B1D423 CRC64;
MPKRLLQYAL SRLEILDTDA LDLENLDIAW GKNSTFEFKD VGLRLKKLET LLQLPSTIAL
SKAKVLLLRL TIPVDVYSSP ILVEVDGVDV QLRVKEEKGA NSSRTNHDRL RKKSTSRSPG
PDPALPTAED LAASFLQTEP REEKAELEAA ILGETQDISE SITSSEDGDL EVPVGTGTAL
SLPAFMARFL QGIVDRLQVR VHGITFNVDV DIPAEGPTPN RTTDPVTVQL KIDDVDIEGV
THDIESAQTR GGKDITSLFK EGKKLICLSN IRGALITEAN LFQTLSRSSS ILSPAVPHSD
ISESRRTTEM RRSSEETQAM SVGSVRAFDG VASPSPRPSP ASSLRASETS LPEIRRPSTP
PRPLKISPSL KASIAASDGG RFDDASEDGH SNRSVSVHED IDSSEMGDSI LHNSAYLDQI
TESQLLDDHE GDDMRSSPSQ YEQERHSAPS ENSRTSTPRA STHISPSSSR TLGFNQFPSI
NRAHNMLQST MLPPRPHTRF SLERVSHSQP TLPSSTAPLD RSYPVQQPES PLEVDAMSEA
DSSVSSTLNE EAGDDLAQSQ LFSHEDAESM YMSAVSYTSA APIPGGWADS GTESEDAKSP
PATPRGPDAG REKLDNLENA RHAVPLDGAS DTTPLEQSTI LPSGSLHKSA RSISSMHPET
PRRSPPLYQA SSDISVESTA SADDYSRMTK QIFSLDQIAI YIPAMNNPSS DPVDAVAESA
LFGSTFDGHS DSSRSRTMDL PGAFSTHLPR EQPSRPSPRP ALRTPVQPAK KIEEEKLIEV
DVGNLLARFD VSVGRLIYKL VCQIQESMKQ EPQAVASSKP TSSSTEPHLK ISAKEISLRF
LEQLQGTLGS RAAESQAKTL DSDVLLRTTL KGLDVSRKPS DSITKTSITL QKFLFGYAQE
NIISFNANLQ MRASVRDLAA SAGIDVSVDM YQSSDGTRFE VQTLPLHVAV DLQRLDETFS
WFGGLSSVLN LGSSMASNAT VTSNPVPKPK SRGVRFNTPI GPDDKTAAAQ NKADVRIGGF
ILDLVGTECS VGVETSAVKL VSREEGIGVA INKIRLSGPH LKHSNEDPAI LVDVSSTRVE
LLNAPKDNDI DRLLALIAPS KSKYDQDDDI LLDTLLRQRQ QGSVLRLTMD DLQVKMGNLQ
ELSYLPDLGE EVARLSTVTK YLPDDDRPGL LSLVSVKKLG VNVDVNNTLG SLQLKATDLE
VAQIPIPSLV AFSVATVSAY RNYSEELIGA GTDQTFMEPS LRTPTIMARL IGDEMEPIVR
IKLWNLRIEY RVPTLMVLLG LADNATENDM SASIMASVAT LRDLAQPRTS KGKGKSVEKA
SASSNSAAKP MTIDVVLTDC IVGLNPLGLP SKILVVLTEA HVAAVLPKDQ NASATAELSK
ASLLVIDNVA HLATNVPSNR KRNSFDGGSN QVADLTTMGY VSVSYISSAK ATVLLSVDDD
GQNCLDVELR DDLFVLESCA DSTQTLIGVL GKLAPPAPPP SKESKYRTKV IPVKDLLASL
SGDAFGTAEG NYDFDNDFGD FGDVAEEHEG DLGFDSDYYK DETEEGYRQA VLEDIGEPLA
SLNLTTRDTR DGVLLDSFVE DSEIGNEALS FHEDHFGTGS VLEGSAHRWN SAKNTYDTSN
ESKVKKSPLK VCVRDVHIIW NLFDGYDWQA TRDAISKAVQ DVESKAIEKR ARNERRPAFE
QDIDDDEDTE IGDFLFNSIW VGIPNNRDPR ELAAAINQEL NDNATETESI ATTNYTITPS
RQGTGRKPKK LRLNRSKHHK ITFELRGVCV DLVAFPPFSG ETQSSIDVRV LDLEVFDHVP
TSTWRKFATY MQDAGEREKG SNMVHIEILN VKPVSYLAAS EIVLKVTILP LRLHVDQDAL
DFITRFFEFK EESDVIPGAP SEEPFLQRVE VNSVQVKLDF KPKRVDYAGL RSGHTTEFMN
FLILDEADMT LRHTIIYGIS GFEKMGKCLN DIWMPDIQRN QLPGILAGLA PVRSIVNVGG
GFKDLVVIPM HEYKKDGRIV RSISKGAAAF AKTTGTELVK LGAKVAIGVQ TVLQGAEDFL
GPQDASIPHG NSSEDEEERK QISLYANQPV GVFQGLKGGY AGLQRDLVMA RDAIIAVPGE
VMEGGSAKGV LRAVRKHAPT VILRPAIGVA KGAGQVLMGA TNSLDKRNLE RADAKYKKH
