ID   ATG2_KLULA              Reviewed;        1502 AA.
AC   Q6CQ43;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Autophagy-related protein 2;
GN   Name=ATG2; OrderedLocusNames=KLLA0D19899g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382124; CAH01042.1; -; Genomic_DNA.
DR   RefSeq; XP_453946.1; XM_453946.1.
DR   AlphaFoldDB; Q6CQ43; -.
DR   STRING; 28985.XP_453946.1; -.
DR   PRIDE; Q6CQ43; -.
DR   EnsemblFungi; CAH01042; CAH01042; KLLA0_D19899g.
DR   GeneID; 2893307; -.
DR   KEGG; kla:KLLA0_D19899g; -.
DR   eggNOG; KOG2993; Eukaryota.
DR   HOGENOM; CLU_000626_3_0_1; -.
DR   InParanoid; Q6CQ43; -.
DR   OMA; YDWKYTR; -.
DR   Proteomes; UP000000598; Chromosome D.
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..1502
FT                   /note="Autophagy-related protein 2"
FT                   /id="PRO_0000215832"
FT   REGION          211..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1502 AA;  169517 MW;  103F6F20CF83C7BF CRC64;
     MSSWLPQNVQ KRLLLYVLQQ VSLFSNVDLT NLDVSLGSQS QFSFNDIDLN VKEIKLPNVD
     VLSGKIEKLN LQLAVAGNVD ISGEGLTFVL KPIDRFFEDD LSDQWASSLT KSVIDMTKSI
     MESDVTDSSE HSVEALEEVS KSPTALDSMR NKVLQMALGK LSLKMKRIEF QFLLSTEVTL
     KFTIDTITLL TVDNKRTVDM GGIEVAFSKT QLSPTNSHQN TDSDVEENEN TDSEDAMTAS
     ITYSKLEATS IYLSAMESLI LESSDDAVQV VLTIDKVNIQ FQGVTSINDL KVRDVIIRID
     EINIYLRKIS PIRKHLLSIL RASLDKTSSD GTRTENMRNY KRFQQEQNIK EEEVLTAILL
     KKVSLHLLDD LELNLIDISL KKSEGFTTSA SVFDLKLLYM SNEYFFSSPS AQPLFSMQPD
     QTTAEKKMFL NRDITLNVDS VLLNELLKLV EEYGSAYNYI QKITRASANQ KTAEVLHFKS
     QSINLKILMN NISLELSMDP IKSTLPHTLF DVEKISLLLI RGDKKVLIGT LSNLIISSKT
     NGCFHVESFD HKFGAIDINT RTKAVLESLH LFLSQAELEL ISSNLIAFCG SISSFTNPNT
     RNNGHENVTK KSVRLLHSSN VMNKRATLSN FVLQVHKAKM TITNTLENTF GDITIEAISC
     ILSQDQNKTL CGIVKEARLQ RLYMREKTDI ICNVNHDRSK PQLILNMPNS GKPKLYLKGL
     GLFIDSKWRD LVPSSSKGDI KQERKLTFRT MEVRLYDCSL SLKPYRICTG MVISIPKSII
     NFSPLGITVS LRSLETLLID DMKVLKERNT KVLENISLST WYQKQGYSPL IKVDVLSLHF
     SNTDSMAVSL KVQKVDVSVC SDSLNALMQT ALDLKPAETY PDTLKYQIEP EAVDIFNELC
     EDFFVTKENP NDKTEDDYET PPVSQGSVNF EEEHFSTERR TVVENDSKSS VFSILTTIKI
     HIEEVKLKLY DGYEWRHTRK EIKSAVDRIQ EDFNDGLELS ETKVFDSIYI PAPKDTVENI
     KDNINRKIHN EETNEGKMKL RPTKKYKVLI KGRDLCIEFK GGQDKIAERA SSLSSINDYC
     ILNNTFVKVS DLEIIDNLPT STWNKFLTRS RSNDKMAQEP AMLVIECSLI RPVPHLYATE
     LICNINIVPL TLHVDQDTLE FLTLFFQFKD NRFELLDEYP DILYIQRLEI NSVRLLLDYK
     PKKVDYAGLK SGKTKEFMNF FILDEARIKL KHVILYGVNG FPQLETILSD IWTPDITKTQ
     IPGILSALTP LKPLAGLSYG ARALISVPTE HYQQNGRFGG SLQNGGMVFL KTTGGEVIKL
     AVRLTSGTQT ILENTEKLLG GQGITGRNVP ITLVEGDEKV DALIDESLLR STALFNKEPD
     NKSNHLDVLL ADGNHQKVLS LYADQPKDFN SGLQDAYESM ERNLYLTFDS MKKAKKELKT
     AKGAQEAVST VAKAAPFVLI RPLIGVTEAL SKTLQGLNNQ YDEDRIAQIE EKYKSKKQNN
     NQ