ATG2_ASPFU
ID ATG2_ASPFU Reviewed; 2160 AA.
AC Q4WLK5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Autophagy-related protein 2;
GN Name=atg2; ORFNames=AFUA_6G13200;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000006; EAL89159.1; -; Genomic_DNA.
DR RefSeq; XP_751197.1; XM_746104.1.
DR AlphaFoldDB; Q4WLK5; -.
DR SMR; Q4WLK5; -.
DR STRING; 746128.CADAFUBP00000151; -.
DR EnsemblFungi; EAL89159; EAL89159; AFUA_6G13200.
DR GeneID; 3508504; -.
DR KEGG; afm:AFUA_6G13200; -.
DR eggNOG; KOG2993; Eukaryota.
DR HOGENOM; CLU_000626_1_0_1; -.
DR InParanoid; Q4WLK5; -.
DR OMA; HRWDSTQ; -.
DR OrthoDB; 54301at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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..2160
FT /note="Autophagy-related protein 2"
FT /id="PRO_0000215826"
FT REGION 100..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2160 AA; 235491 MW; E85A16249F0B69BB CRC64;
MAYFLPSFFQ KRLLRYALSR LELVDTEALD LDSLGIRWGQ RSTVELRDIG LRLELPASSE
LLSAKVQFLK ITVPADIYSS GIICEASGIN VHLQLPSEES FSTAKDGNPN SRSPSKAGTH
DSSSDHILPT PADLAESFLD AEPKEEKEEL QAAITSRSQM LQRTSASISD DEEELGLGNE
GVSLPSFVAA FLKGVAERLQ VRVDNVSIRV DMEMKQEGVV KREPENKPDN VTGLLTVREV
SVGAVSSATS SSEQEKLFRN RPIVISDINM ALISEPIVFS NYSRFAPPAS PTTPVQPKSS
EPSSRIPSPL PGHTPDADSF LAMTRSTILE TQQEHWIQDI EEPGVGRMEG SAYTYDGRFS
DADTDAEDRS DGYLEGAQQF LDNDKLLDNP AYLDSVIDSQ LHDDDLEPPE DLVPQDDQFP
PSSATPRPPK PEVHMYRETS PSGIDTEQTA PFSHYGDGFF MDRSPHGSQP YLGPDHVATR
NASHSASSPS GSLPSREISN RQTAPPSESG SIGSSDFANG GELSESKLFS TEEAQSMYMS
AISHGSSRSF VPNVPGAWDL WESTVAQDMH AGTQLTDAAD AKQDVQDETS ISTPKLTAQA
ASAFTEKRSF GEQSECLSEA REPDLAPLSP TLSKLSDVAK RFLRIDRISI SIPVGEDRRH
TDETVHSSDL NLASDSPKDS TVHSGHSSAE SEFLSSTMYA SARLRSDSIN LAPSFEGTLP
RSLPRQGKKA DHDPISKSQP GDIAVEISAV DIRFDNAVGW LVVKIGQRVL HAFRDGGNVS
SGKPAPESVQ TRHSLALTLH DFSIKYVDHI PGQTYALNDY DPHSSSFFGL PHEDIILRAE
ASGLTARYLA DKSATKFSLD VSKFVFGFAW DDLISFSESL KMRESTRDVL APVNGDISLS
LTKSSDSASL TITTLPLRLH LNVQRLEEIF GRVGGLSTIL ELGSSISSAS TGFSTAKNMQ
RDSPRRARGV HFESSPPPEN ILPANPQLSW KVNARVGGIV FDVVGETHYL RLKTTAVKVV
SRFEGIGVQI DKAKLSGPLP LDDSRDAPAK INLSNIRVEF LYSPKEPDLD RLLAIITPSK
DKYDEDDDIM LDTLFRQRRQ GSVLRTTVAD AKIIISRTSD LESLSQLEEE LGKLSTVAKY
LPEDDRPGIL TLTLIRELEC QVYLGGPVGN ITTHLRNAEA AYISMPSLIA AQLGTIKVVR
NGSEELVGEA LPASGSQGQN QSQLPILMAR YIADEMDPTI KIKSHNLRVE YTIPSIIAFL
GLSEDQTTGD VAANMANSLA NIAESQHLHR NASETSIGSK GRQASAKPRK LAFALRDCVL
ALNPRCTTAK GLVVLTNAKF SAAISDSGCS EAMLDLKKAS IMVIDDVKNM GLAENLQRGR
STIPQSDQIQ SFIDMGFVPV SSISSAMATV KLLQLDDDGT KSVDVELKDD LLILETCADS
TQTLISIING LQPPTPPSVA VKYRTEVLPI EDMLASFSGD AFAMDPPPGQ AEITEAPTIV
EPEDGGPRIE DELEYVSDFY PVKSGPDNLA PTGSAVPSES NELLDSFHSQ YYVSSSVSDL
EFKEDHFANH SAVGGTAHRW DSTQNTYGLT DDSKIRKSPL RIRVRDAHII WNLFDGYDWQ
RTRDTISKAV KDVEKRATER RARAGSRASP GFEEEEESVI GDCLFNSIYI GIPANKDPRE
LRNDINRNID DLVSETGSYA TTTTVTGATA RQAQSPSYRG RRLKLSRSKY HKMTFELKGI
CADFVVFPPG SEETQSSLDV RVNDLEIFDH VPTSTWKKFA TYMHEAGERE SGASMVHLEM
LTVRPVPELA ASELVLKATL LPLRLHVDQD ALDFICRFFE FRDDTAPTPS SPADIPFLQR
VEVNAVPVKL DFKPKRVDYA GLRSGRTTEF MNFFVLDGAD MVMRHVIIYG VSGFDKLGQT
LNDIWMPDIK RNQLPGVLAG LAPIRSLVNV GGGVKDLVVV PMREYRKDGR IVRSIQKGAL
AFAKTTSNEL VKLGAKLAIG TQTVLQGAEE MLTAPTATTL GSEEDMIDEE EANKISPYAD
QPVGVVQGLR GAFRGLERDL LLARDAIVAV PGEIVESGSA KAAAKAVLKR APTVILRPAI
GVSKAVGQTL LGAGNTLDPS NRRKIEDVSV MVKYVSRVCL LTSLLRNINA IKTVGHIGQL
