ID   ATG2_COCIM              Reviewed;        2100 AA.
AC   Q1E702; J3KJZ4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=ATG2; ORFNames=CIMG_01661;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
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).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704911; EAS36307.3; -; Genomic_DNA.
DR   RefSeq; XP_001247890.1; XM_001247889.2.
DR   AlphaFoldDB; Q1E702; -.
DR   STRING; 246410.Q1E702; -.
DR   EnsemblFungi; EAS36307; EAS36307; CIMG_01661.
DR   GeneID; 4567148; -.
DR   KEGG; cim:CIMG_01661; -.
DR   VEuPathDB; FungiDB:CIMG_01661; -.
DR   InParanoid; Q1E702; -.
DR   OMA; HRWDSTQ; -.
DR   OrthoDB; 54301at2759; -.
DR   Proteomes; UP000001261; 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; 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..2100
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000317808"
FT   REGION          101..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1474..1499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1969..1996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..442
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..561
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1969..1986
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2100 AA;  229993 MW;  FCF4D0E3B2D19C6B CRC64;
     MPFSLPSFAQ KLVLRYALSR LGLVDTDTLD LATLGITWGQ RSTFELRNVG LKLEKLSAHL
     PPYCTLTKGS VSLLRVTVPA NLHNSSIIVE VDGVDARVRL LPDKPEQNAP PTRSKGTAED
     EGQDGHSVLP STADLAQSFL ESEPKEETEE LQAAILSQSQ YPEHLDAQSD DGEEDLGLYD
     GLSLPAFIAG FLKGVIDRLQ LNIANVSLRV DTEVQRDGVL KDETQDPISG LFTIQEIAID
     STATSASEDS RLKIGKRMVS LSGIHAMIMS DAEVFSNYSR FNAPDIPSTV HSKSTHTPLR
     PRSPQPSSSG SDSCGDMSRS TILDPSSMYG SRLTVDSHGD ESRHLESSVY STTGRFSDAD
     SDDENDLEFY SQATTGMLDS HYDERLLDNP AYLDEALKSQ FDDHLEDSTI FPKDCPSTPV
     RDQTPRPHVS KSPSSSPEHY MYHSVHESNF PVGGGIRDNE PDSATSARGK TPDCQTEQES
     PSTSKICPAV SQPEDLSASR IFTHEEAQSM YMSAMSQSST TSFDPDMPGA WGSSKRIDTS
     DPDQKEQPLS GDTDTEAKGA SHDFDTSQNS PEAQTGEDDE RESVHNSPQY ISGVVKEILA
     IDRIIIWLPS VDSQDSEEIP KTDIDSKPVD PMVESTITLA DSVTPDLLAN TRSRLAQSAF
     RRGSVSSIVS SRHLPISRTK PTTQKHEDFD GLNDPQTTRA VEIDITSLTA KLDIASGWLL
     VKIGQRITDV STSTSKQTKI SEAASEESSP SFFRLNLTSC SLKFLERVPA QPYPLSSAPS
     LSQLQSGIPI EETILHLTLS GTSIDFAAIG NTTKLRLDVM KFVLGHMSYD IISFDESLRM
     RESTRDVTSP GQKDISLRVI KSSESTTVNL TTLPICLSLD LQELDETLGW FGGLSTVLEL
     GSSIASASTV KGEQPCSPPR PRRGVHFADP VPPSSPSTTN HAALKANCRI GGIVLRVIGE
     HCTVQLGTTA AKLVSRFEGI ALQIDKASVG GPHLRKEPSP SPPSLDFENI RFEYLYGPKE
     VDLDRLLGLL TPSKDKFDED DDIMLDTLFR QRRQGAVLRL TVGHADFAVP NPTALQPLSH
     LGEELAKLAT VAKYLPQDDR PGILILALVR EFEGRVHVNN EAGDITIISH NLEAGYVTFP
     SLLATRISTV TVVRNGSEEL VAEVIPEDTE EARTHDPLPM IMARFIADEM EPTVKIKLYN
     VRVEYTVPSI TAFLGLNNQM AAEDVAANMA QSVLNLADLK AHHEPGSDLS ERDSIGSGDD
     RSAMLPRLSV GMKDCGIGLN PRKSPAKALV IFTRASFSGA LHETKPSEAL LDIRKASVMI
     IDNVENLGSA ENYRHRMSSG ARSGQIQHLQ SIGFVPVCDI SSASVALKVM QLDVEGEKSL
     DIEVRDDLLV LETCADSTQT LISILSGLAP LSPPITERKY RTEVIRIEDM LNSLSGDAFA
     TDIVPDSDYE VEGENDGQDG DGAEEIEYVS VFYPSHGDSG PQGRGATTPR FGNEGSASAG
     TSRILGSFHS EAQMSSSIPE LEFQEDHFAK QSAVGDTAHR WDSSRNTYTL ATEVKLRDSP
     LRIRVRDVHV IWNLYDGYDW QRTRDTISKA VRDVQAKAAE KFARRPGNRL SADFEEDEES
     VIGDFLFNSV YIGIPANRDP RELSHDINRN IDDLASETMS FATSTTVTGL QNQVPGTKRE
     KLRLARSKHH KMTFELKGIS ADLIVFPPHS GETQSSLDIR VEDLEIFDHI PTSTWKKFAT
     YMRDVGEREI GTSMVHLEIL NVKPVPDLAA SEVVLKATVL PLRLHVDQDA LDFLSRFFEF
     KDDSAPSEPS PEDVPFLQRA EVNAIRVRLD FKPKRVDYAG LRSGRTTEFM NFFVLDEADM
     VLQHVIIYGV SGFDRLGRTL NDIWMPDIKA NQLPTVLAGI APVRSLVNIG GGVKDLVLVP
     MREYKKDGRI VRSIQKGAVQ FAKTTTNELL RFGAKLAIGT QTALQSAEDF LNSPRGSPSR
     PSTSDGRWDD NGVDEGERPR ISLYADQPLG VAQGLRGAYS SLERDILMTR DAIVAMPSEV
     LESGSATEAA RRLLGRTPTV VLRPAIGASK AVSQTLLGVS NALDPKNRRK IDDKYKKHKV