ID   ATG2_CANAL              Reviewed;        1856 AA.
AC   Q59X11; A0A1D8PHI8;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=SPO72; Synonyms=ATG2; OrderedLocusNames=CAALFM_C206010WA;
GN   ORFNames=CaO19.11601, CaO19.4119;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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/SPO72 binds to the ER
CC       exit site (ERES), which is the membrane source for autophagosome
CC       formation, using basic residues in its N-terminal region (NR) and to
CC       the expanding edge of the IM through its C-terminal region. The latter
CC       binding is assisted by an ATG18-PtdIns3P interaction. ATG2/SPO72 then
CC       extracts phospholipids from the membrane source using its NR and
CC       transfers them to ATG9 to the IM through its predicted beta-sheet-rich
CC       structure for membrane expansion. {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; CP017624; AOW27611.1; -; Genomic_DNA.
DR   RefSeq; XP_714289.2; XM_709196.2.
DR   AlphaFoldDB; Q59X11; -.
DR   STRING; 237561.Q59X11; -.
DR   PRIDE; Q59X11; -.
DR   GeneID; 3644072; -.
DR   KEGG; cal:CAALFM_C206010WA; -.
DR   CGD; CAL0000178327; SPO72.
DR   VEuPathDB; FungiDB:C2_06010W_A; -.
DR   eggNOG; KOG2993; Eukaryota.
DR   HOGENOM; CLU_000626_3_0_1; -.
DR   InParanoid; Q59X11; -.
DR   OrthoDB; 203302at2759; -.
DR   PRO; PR:Q59X11; -.
DR   Proteomes; UP000000559; Chromosome 2.
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..1856
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000215827"
FT   REGION          123..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1157..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1614..1647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1719..1741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..147
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1157..1176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1623..1639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1856 AA;  207364 MW;  1C68B14C7D691CC6 CRC64;
     MIPQWIPQNI QKRLLLYVLQ QLSLFSEIDL PNLEEVSLNN IILKDVALDP EKVGKLPGCN
     LRYGQIGSLE LTTISGISGV NIDVNDAEIV ISPDFDIDEN MTNQVAFSLA QSTANLANTI
     MLNTNDGSDM NETSDPASED DDEDDIDDKI TKPIPPKRRT SSVTGNKTTA LGGVMQKAVE
     IALSRLSIKV NSLKIKIVSD LTDLQMEVDS VSINSTNGTR TVSIKGVKLR TLKPNVNPGE
     GFQSGHAPQK KQQGSDNDSP TDANKHGSEN DNDDDDDDYG NESLMDSMVF SHEEASSIYM
     SATSRSFEKS AASGIPGEVD NKATDKEDYS EDPPIIFYMD DCTIEFDGLS TISNLEIEVG
     NINLAFTPLT PTLVSIFQGV AKSLKIKYYQ QKKKTKSRSA QRNEKFPQYT NDNDEIPEDQ
     SESDDASHEP FFNRFKVNSF VISATSALSE NGLFANKNGI NIIFFNINIK QKNELLLYGG
     VETFKIIRFE DDNTYEIFHF DKPQSAPSSA PSYSGSNDVA GTSSSLSSST GSATSKADIR
     FEVFKKSEES DDLEVTVLMA KSAHFNFDLQ SLLILSNFAK AVSSIYDEYG LLKSVIDKLD
     TRDKKWSGGT NNSKMSSKSE FILQTATIFV NFIISDDCQL QLIVFPIKFN LRQEQLTISK
     ILLNCTNGDT QVEGVIILTD VSLITKNQEF RAYFQSTNTT TSANTHPLPR KTTMNSKLSV
     IVQKFSSNVS MDRLKFIGEK LKNFSNEFIE RSPTQSNSLE NSFLNEPVER QRLESSLHMN
     SSLFSTRRPG RRLGLGFNNS PSVFLGSTRV TMASFQVCFK EATFNITGVF PKFGNFSVQM
     SDISFYKLKN DILGHILSVS VQRKKGDLVE NLIHQYQDLS PNSLEFPLLS IKCKLGDKTT
     KIEITARNLV LEYYTNWLLL MDKEESIIDA VEEEIIEKVT PSQHSSSQNK LDIRYSMYDC
     MVGLTPGRLS CKSYLIIGKG DSDISFGVDQ FYVKCSFRNI SMVLIDDTKN ILPFSEPSTS
     SSSSSSSATR QTPYVYIQPL DYYSKLGYIH LGLINVAHVG ITFNTDIEAL KDRNEKLGIK
     DSLTFVDLKT NLDECQFNLC ADTANTLIQL VNDLKLPLNF KDEDKMKVDF ADGINVMQGI
     DQNIFKGLTE TLTELNLNGT ENGSTSESSS QEASSLMFEE GHFDRGNRSL YDNSHVDPLH
     ININLSKVKI YLHDGYDWKD TRKAIRGAVK NFETAQTAKT VAKEKEKKRK VEFETRDIEV
     QEDVFQETLF QSIHVVAPRN QNARDMATSI NLDLQNDKDG ESRDVSTANS GKSYKNLKLR
     RSAKHKLLFD LKSIEVGVNV YSTRDPRRDK TDENMKYELL NFIELRVGTV DIYDNVSTST
     WNKFLSYMNI LGDREIGTSM VKVSILNVRP DPAMVSGEAI MNVSVLPLRL HIDQDALDFL
     VRFFEFKDER FELPPDEMVY IQKFEISSIK LKLDYKPKKV DYAGLRSGKA GEFANFFTLD
     GSTLTLPKVK LFGIPGAPKI GIGLGRAWLP VFQSTQVIGI ISGVSPLRSV VNIGGGFKDL
     VAIPISEYKK DGRLWRSIQK GTVSFAKTTG YEILNLGVKL ASGTQVLLEQ GEEMLGGEGS
     SVRSPNLGGS DNRRNSNASD ELPVEVAKPK SQNNLLVSSQ ILNKASTKIE THSYDTKKLY
     SNIELDDEDM DDNRINGINK ELLSKSIFLL APAEEKLAKL QPHTKGNHEG LTEEEEDEDE
     DEEYQLYAYE NEEELQEKLV SLYSNQPETI EQGLKSAYKS LGTNFKLTKK QLLKLRRELA
     ETDTIQDSMV TVLKNSPIIL MRPLIGSTEA VSKLLMGVGN QIDGKKLVEK KDKYPT