ID   ATG2_CRYNB              Reviewed;        1935 AA.
AC   P0CM31; Q55X62; Q5KMS0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=ATG2; OrderedLocusNames=CNBB5000;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(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; AAEY01000011; EAL22325.1; -; Genomic_DNA.
DR   RefSeq; XP_776972.1; XM_771879.1.
DR   AlphaFoldDB; P0CM31; -.
DR   SMR; P0CM31; -.
DR   EnsemblFungi; EAL22325; EAL22325; CNBB5000.
DR   GeneID; 4934595; -.
DR   KEGG; cnb:CNBB5000; -.
DR   VEuPathDB; FungiDB:CNBB5000; -.
DR   HOGENOM; CLU_000795_0_0_1; -.
DR   Proteomes; UP000001435; Chromosome 2.
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   InterPro; IPR026854; VPS13-like_N.
DR   PANTHER; PTHR13190; PTHR13190; 2.
DR   PANTHER; PTHR13190:SF1; PTHR13190:SF1; 2.
DR   Pfam; PF13329; ATG2_CAD; 1.
DR   Pfam; PF09333; ATG_C; 1.
DR   Pfam; PF12624; Chorein_N; 1.
PE   3: Inferred from homology;
KW   Autophagy; Endoplasmic reticulum; Lipid transport; Membrane;
KW   Protein transport; Transport.
FT   CHAIN           1..1935
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000410017"
FT   DOMAIN          30..121
FT                   /note="Chorein N-terminal"
FT                   /evidence="ECO:0000255"
FT   REGION          286..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..399
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1935 AA;  212636 MW;  A4B8BB1F2CE46B42 CRC64;
     MFSLPSFLTT FSFTLPSLPS ISLPANIQRR FLSYVLKRTL GRFVSHQALD AERIQAQVSE
     GWVEIENLEI ECSEINNYIP PPLPLSLTSG TINKLTAKLP FPNLWSDPLQ VSLDTLTLDF
     TLSSPSPLSR GRAATRPEHH DLAESVTSAA DDFLHHELDA YEEKELEGSI RQSLILSQTD
     PFISDVPGGF PLGSPGEISP GRPLPANMES TTVLAGMVER ILARLEFRVE KIKIRLVIED
     EEDVVELTVG RIRYADESEA QTNDDGKSTT RAIRISNISL DIVPSQRKPP SLVIPQRQSL
     EPSVSSSTST ASTSSGNDYS DMFMSQAVVD LRQSLLTPEQ ISEPANEQTV HESNMFYSAL
     SQPNESEPGA STGIKRSGIS QNPKLADEIE EERSRSETPT PETKPQPSGI PVLSFGQEDV
     VLHMRTTRPL ISAGHQTSFN DNKPTVEMNI TIGTITTVLL PSHLKLFISA LQTLQALCQK
     DDVPAAKDKP AQSTSPQTRL TATTKLKAFY VSLVYDLSAE TSLNLHSTMA SHLTRPTNPI
     PYPHLRFRLD TLVASYQSPG HSNPSRPAFT RPTPNMSTAN LRRKSSGHAR FGSLPSNLTV
     NVGDISLFEW MGEGMIAPVI LFDPGLKHQY DLPSAPPHKG QAGFPECECR DWREEKKTGS
     EKAWRVRPRG RGILKGGARA TTEDEGPVVH VRQDLGSDSA AVINLQSLHV FVDLSLIERL
     LPLLRSVTPL IHPPEPTPAW LQSVPSQSIS EEITPESIIS SLSAPPPTAR GKKMKADIRC
     DLVRLSVRCP APPPEPAERQ IGDGRQLRSG IVFVDVHGLK SRFMDTSRTG TRPASSEVAN
     VEFEQTLIFF ASVSQHYAYP FLIFAPLSPE PGEEDIPLLP SISLSSFPQA SSLPASSIAK
     TTLVTCKMPA IRASVHHPTV TGLQYFADDV TRWLDVAFAD GSAKPRDELK MIGSRFFGGS
     KGSEASSEID EPYDVEEVAA GMKVEIEISE IDMGLYVPRL DASGERVFSF KANDLGVRME
     THPEENETAL ELSIMDLDFS DVSSTPLRIL GRTTPFTLTS HQAPVVYLRF VSSTDLRTTL
     KESNISVALS HFTFAVHKEI AWLHEIAQFA KPPKGVFENL SPTDLTRLSI NLSSASFLLV
     PPNLPGSIVI LVREVEGKTE IPKGATDSVL EVGMSGLGAL AVEGESGPLE VSSDLADVWK
     KAGYAQLAEV MVLELRLMRE LVAAGEVSLD ITQAQFKVTA CADSLATFAE IATDFGHSLD
     ENAFNLLPEI VSHSDTDMIE DDLPHNLDYL DHATRISKHY PSMDRTTGEN LRAWHTPEEG
     LEEGEWENGE SGETIRAFGG EIEEEEGYWE GLPILNDVYS ADQKPGKIHI RVLDASLKIF
     LHDGYDWPRT RKAIEDEVRA VRRRLERIRQ LLASGQKADE SIENATSSVL FNSIYIGLEQ
     KGEMGLSTMG MGKMDEKALM AAIDEELDGM ETESGSSWQT LPAGVGAGPS AVHQAHKKTR
     LKGKRLVRSK KAQIEITLSG IKTDVDLYPT EESTSSRVHF TAKEMEILDH IKTSTWKKFL
     TEMKADNRGN IRETDADMLR IELVGVRLKE DEEELRLRAK ILPLRLHVDQ DALDFLKRFF
     SFKAPPMTSA RPLAQHTTSS TPDLYFQHVE IFPIQLKLDY KPKRVDFRAL REGKTIELMN
     FFHFEGAEMT LRHITLSGIT GLERLGTTLQ DLWTPDVKAN QLADVISGVS PIRSMVNVGS
     GVADLILLPI EQYRKDGRIA KGVQRGTNSF VKSTALEVMK LGARLATGTQ VILERAEGVL
     GGKSGEDVVG QVQGLSTNAF GVDSGMLEGG SSSEDEQEAI SRYADQPESM KEGVQAAYKS
     LSKNVNAAAQ TILAVPMEVY ERSGDDGPLK AVIRAVPIAV LKPMIGTTEA VSKTLLGMRN
     SLDPSARREL DDKYK