ATG2_AJECN
ID ATG2_AJECN Reviewed; 2105 AA.
AC A6R6E3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Autophagy-related protein 2;
GN Name=ATG2; ORFNames=HCAG_05201;
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC unclassified Histoplasma.
OX NCBI_TaxID=2059318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476659; EDN08702.1; -; Genomic_DNA.
DR RefSeq; XP_001539734.1; XM_001539684.1.
DR AlphaFoldDB; A6R6E3; -.
DR STRING; 339724.A6R6E3; -.
DR EnsemblFungi; EDN08702; EDN08702; HCAG_05201.
DR GeneID; 5446273; -.
DR KEGG; aje:HCAG_05201; -.
DR VEuPathDB; FungiDB:HCAG_05201; -.
DR HOGENOM; CLU_000626_1_0_1; -.
DR OMA; HRWDSTQ; -.
DR OrthoDB; 54301at2759; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
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; 2.
DR PANTHER; PTHR13190:SF1; PTHR13190:SF1; 2.
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..2105
FT /note="Autophagy-related protein 2"
FT /id="PRO_0000317801"
FT REGION 108..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2086..2105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2105 AA; 230425 MW; BC9877C6264F3F5A CRC64;
MSYFLPSFFQ KRLLRYALSR LELVDTDALD LESLGITWGQ RSTFELRDIG LRLEKLSSVL
QLPPSCKLTQ ATVSLIHVTI PADIYSSSIV VEVENVQVKL KLLSDDAASS GDDRELCRPF
DELSNNPKAN DPHPPGSHSH DRSSEKSSIL PSTTDLAQSF LESEPKEEKA ELEAAISSQS
QYSQCSDGLS DDGEEELGIG VEDGMSLPGF VAGFFQGVAD RLQLKVKDVV FKIDMEVGHD
RTSNSPQDLT VDTVTAMFTI QNISIDSVVS PMEENPELKP GKRFISFSQI NLIFLADAGV
FSNYSHFVPP SLKSPSVTHS TRSIHSKLSH SPLNVSSPAP TSSSSGSSLV MSRGTILDQP
SLLEDRPSNH QLADSVYTDD GRFSDAGTEY EYGAGSYLDH TRPMTENHYD ENILDNPIYL
DEAIRSNLAD EFQSSPPSIS DPTDPTDEPS GDTPRPRSPT SLPDDHMYHS MESSTHSTNH
PSQHLEIPPV EYQPEFSEPS GDEIEVSDSD NVPCTQEPSR SGSSTPQRSH SESASVVEDL
SKSKIFTHEE ATSIYMSVLS SISAGSLPDM PGGWESPKYE ASKRNVSSPS LAPSTDVEPT
STTSEGTPKA KPLVQLENGE TRDTSHVLGS PLLSNPNQSG LTEAEIKSPS RSPDYIPRIA
KRVFEIDKLA VWLPSLDPKI TKSQDVPTQN SPRNEFDHME TSTMSFTDSA TDEEPVSLSQ
HLAFQQPRRE LIFSQSLHQL ASPEQDDTSV PGFYAGTILV DVPTITIEVD IACGWLLTMM
GQRLVSTWNP TTQNEKCRSE SKHATILPLN LTLANCSIRF LEHLPIYRSA FNATSLHYNP
EVSEIILRVT LSGINFKSSV RGDTSEFILN VTKLTFGHAS EDIISFDDGL KMRDSIRDDF
HLKRGDISLS VLSTKGNTTV DLATLPVHFS FNLQRLDETL NWFGGLSTIL ELGNSISSTS
TIKGGKVAAN QRPRGVHFEV DSSKARPLPV GSSGVNPIPW KINARMKGFV MTLQGDRCSL
KLKTTAVKIF MFAPMEEDLD RLLLLLTPSK DRYGEDDDIM LDTLFRQRKQ GAVLRLTVGN
LKADFPEPEM LRPLSSLGNE LAKLSTVTKY LPQDDRPGIL TLVLVQECSC GVALGGRIGD
IEISLTGVEA AHVGIPSLMA ARVSTLVVSR NDDEELVGEA ANSQDETNIV ALPMIMARFI
ADEMDPTVKI KLSNVRFEYT VPSIVAFLGL DNDMSAEDFA ANIANSVVNL AELKSQETTI
HRLAESSMSS VSSRPSPVPS KLSITLRDCL VGLNPRKSPA RGIAVFTSAK FSGSLDKDVT
LDACLEIQKA TVMIINDSRN VGTRGSSHTR TSSDSQSNQV QLLHGMGYVP VCYLSSAAVV
VKVMQLDDNG EKSVDVEVRD DLLILETCAD STQTLITILN ELAPPSPPNK SLKYRTEVMP
IDDMLSSFTG NAFETSPIRE VGNLSNSYPV DEKEGDLAEE LEYVSDFYPV TLESGKHDPG
RNMHISGTSD ADDGLSGLAH GPKTLLESFY SEAHVSSSVS SLDFQEDHFA RKSAVGGTAH
RWDSTYNTYA LTNDAKLHGS PLRVRVRDVH FIWNLFDGFD WQHTRDAISK AVKDVEAKAS
EKFSRVGGRS SPQMGSEEDV IGDFLFNSIY IGIPSNRNPQ QLREDINAHI DDLASETGSF
ATTTTMTDGS AATIKAPSKR SKKLRLNRSK RQKMTFELKG ISADLVVFPP GSGETQSSLD
IRVNDLEIFD HVPSSNWRKF ATYMYDAGEK ENGTAELAAS EIILKATILP LRLHVDQDAL
DFMTRFFEFK DDSAPADTSP TEQPFLQRVE VNAVRVRLDF KPKRVDYGSL RSGRTTEFMN
FFVLEEADMV LRHVIIYGVS GFEKLGVTLN DIWMPDIKAN QLPGVLAGLA PIKSLVGVGS
GFKDLVVIPM REYKKDGRIV RSIQKGALAF AKTTTNELVK LGAKLAIGTQ TVLQGTEDFL
NAPGDVGSQR YVATTDDDSA DEEQQKQFSP YADQPVGVVQ GLRGAYASLE RDLLIARNAI
VAVPGEVIES GSAQGAARAL LKRAPTVILR PAIGASKALG QTLLGAGNSL DPTNRRRVED
KYKRH
