ATG2_DEBHA
ID ATG2_DEBHA Reviewed; 1887 AA.
AC Q6BTX0; B5RTC2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Autophagy-related protein 2;
GN Name=ATG2; OrderedLocusNames=DEHA2C15268g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382135; CAR65584.1; -; Genomic_DNA.
DR RefSeq; XP_002770221.1; XM_002770175.1.
DR AlphaFoldDB; Q6BTX0; -.
DR STRING; 4959.XP_002770221.1; -.
DR PRIDE; Q6BTX0; -.
DR EnsemblFungi; CAR65584; CAR65584; DEHA2C15268g.
DR GeneID; 8998392; -.
DR KEGG; dha:DEHA2C15268g; -.
DR VEuPathDB; FungiDB:DEHA2C15268g; -.
DR eggNOG; KOG2993; Eukaryota.
DR HOGENOM; CLU_000626_3_0_1; -.
DR InParanoid; Q6BTX0; -.
DR OMA; YDWKYTR; -.
DR OrthoDB; 203302at2759; -.
DR Proteomes; UP000000599; Chromosome C.
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..1887
FT /note="Autophagy-related protein 2"
FT /id="PRO_0000215830"
FT REGION 125..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1659..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1275..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1887 AA; 210749 MW; F6148332B5C867DC CRC64;
MSPQWMPQNI QKRLLLYVLQ QLSLFSEIDL PNLEEVSLNN IVLKNVSIDP DKVGKLPGCN
LRYGQVGSLE LNGGVMGGVS IDANNVEIVI APDFDMKEEI SNNVQFSLAQ STADLANTLM
VDKSSNEYES SDDETDTVMP SVSSKSRSNS SSSGTSARTR PSALSGVMTK AVEMALSRLQ
VKVTNLNIKI VSESTDLVLK VDEALLNTIN GTRHVKIKGV KLITLKPEVN PGESSDDSPE
QESPKESENS NTSDDDEDND NDYGDESLMN SMVFTHDEAS SIYMSATSQS FNKPSNNDDT
APTETAPDNK ESPILLHIDD IDIEFEGLSN ITNLEIDVGE IKVAAVPITP TIISIFNNIS
HNLKLKYYQQ RKSNIHKQRF KSNLSFPQYA DDNDEIEDEN EQMPILDDNG ASSGPFFDKL
RIHNIIVSAT SALLPTGQFA SASNSLNFIF HNLNIKYKNE ALIYGGIEVF KIVKITNDQE
IEVLKFNNST APTNTEPNPS DEPAGSTSAP SNSSKADIRF EAFTKLDNEI KHLEFTSLFS
KQAFVNLDKS VLLLLSNFGI SVSSIYDSYN TMRSTMNSVN SFKANTNING EPRDASSIGV
AKESNLQIIL QTASTTINIK LSDNLNLKAV IYPISFNLLK QGMSINKILI STVSSGIETL
ISTLSNIQLS TKSQEFKSFS NKSGYSKGSN DSFPRETILG SNLTLSLSKI SSKASLKELK
LLIGDFADFA SSWQLLSLQV NSLKNSVKDK GFVMSSKSNK NESSSMLSNS MYFNQRRSRR
SNFNNPSLVN TNRSNLVSFR LYVDHIEFCI TNVLPKLGDF DFQLEKVSFY KLNNDIQGSI
HTVKVDRNLG NGEAVNDFIY EFQRKRCNKI NIPLILVNIK SNDKANTIDI SLRNFLIEYY
TRWLELLEKE IDENAVLHDI TGQKRESSSL NSPSKRLDIR FSLYDCVIGL NPGRLDCKSL
LIINKGNSDV TFGLHQFYIK SSLRNLSLLI IDDVKNINLS KTDREAASKP TSTAYISPLS
WFTSIGYISV GNINCIHLGI TVNTGIQEII ERNEKLGLQD NLALLDIKIN SDEHQLDLCA
DSAHVLIQMI NDLKPPLSFT DEEKIKVTVN DPINLLDEIG QNVFLNESIM KSASHSETFE
NSTISRKNSD ANDINIVEEY YDGSHTSSQS LENGFNKLSI SESDNAKDDA SSFSFDEEHF
SSNGADRNNT EVFPIKMNIN LSKTKIYLYD GFDWKGTRKT IKGAVKRVEA QALQELERVK
EHGSRKHLKR NMQVTFDEPE SNATEDNYGN DQENDDGNSS DNQSLIGETL FQSIHLSVPK
GSNPSSLTKN INKSVQNYFD NEDSNDSSIN YNVETGRNYK NLKLRRSKNH KISIDLKNIE
VNMAILTTRD PRRDKDVPDV KYEVTNSIDL RIEDIDIYDN IPNSTWNKFL SYMNSLGERE
IGTSMLKASI TNVRPNPELC STEAMIDISI LPIRLHVDQD ALDFFIRFFD FKDKRFELPI
DEIIYIQMFK MSSIKLKLDY KPKKIDYSGI RSGKVSEFVN FFILDGSELS LPKLTLYGIL
GMPMLGAELT KTWAPNIQQT QLSGLLAGLS PFRSIVNIGG GFKDLVAVPI KEYRKDGRLM
RSLQKGTSKF AKTTGYELLN LGAKLASGTQ VVLEQSEQVF GGEGSSARSP KNKNDKHGKI
EDDDNEDIYT SGNTSKGNSN LLASSQLLNK TIAVDNDPYG KKKLYSYIEL DESDDIDDKI
LENSLLLMNP KDIKESRQLQ VVSEESELQE LDEKEELDDE DAIKLVSLYS NQPENTQQGL
KLAYKSLGEN FEITKKAVNN LRKELNASSN VQESLKSMVK SSPILIIRPM IGTTEALSKA
LMGISNEIDS NHIIESKDKY RYDASEK
