ATG2_PICST
ID ATG2_PICST Reviewed; 1848 AA.
AC A3LT28;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Autophagy-related protein 2;
GN Name=ATG2; ORFNames=PICST_45331;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000498; ABN66339.2; -; Genomic_DNA.
DR RefSeq; XP_001384368.2; XM_001384331.1.
DR AlphaFoldDB; A3LT28; -.
DR SMR; A3LT28; -.
DR STRING; 4924.XP_001384368.2; -.
DR EnsemblFungi; ABN66339; ABN66339; PICST_45331.
DR GeneID; 4838982; -.
DR KEGG; pic:PICST_45331; -.
DR eggNOG; KOG2993; Eukaryota.
DR HOGENOM; CLU_000626_3_0_1; -.
DR InParanoid; A3LT28; -.
DR OMA; YDWKYTR; -.
DR OrthoDB; 203302at2759; -.
DR Proteomes; UP000002258; Chromosome 4.
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..1848
FT /note="Autophagy-related protein 2"
FT /id="PRO_0000317812"
FT REGION 129..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1717..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..272
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1848 AA; 206433 MW; 6F9613B23ABF67F4 CRC64;
MSPQWMPQNI QKRLLLYVLQ QLSLFSEIDL PNLEEVSLNN IVLRDISIDP EKVGKLPGCN
LRFGQVGTLE LNTVTGGTII GGGGGVNVDA RDVEVVISPD FDINEEVRKE VQFSLAQSTA
DLAKTIIKDS DSAAEDESDD TDEEIVVEPK KSRSSSSSSF SGSTSKPSAL SAVMSRAVEM
ALSRLQIKIT NMKIKLVSEM TDLLFEVDEV LINTVNGTRV VKITGVRSMT LKPNVNPGEL
VEKVVQSPQK DDTSDNEEDD SNYEDDNNDY GDESLMDSMV FTHEEASSIY LSATSQSFPR
PTSYNVDEGE VHVGNESVSS DPPAIFHMDY CDVEFDGLSN VSNLKIDIGT IKVATTPLAP
TIISILNGIT RSLKIKNHQK WTQQALKRQQ NSRFPQYAET TDELTDDEAS SKDGENTDPF
FNKLHIRDII ISTTSALSRD GVFASPDNSI NFVLHNSNIK QKNDMLIYGG VETFRIEQVK
EGVTTDIFTF ESPTAATHAE QSQSQPDSEG VSFAHGSPPP PIRPMSPSSI SSMSSSGSKS
STLKADLRFE IFKKLEENVV TIETTALLSK TALLTLDLNS SLILSNFITA MNSIHSNFKV
LMATIENLSK QQSPKKQKTH TNAAEAMTTK TQFILQTSPI IMSVKFTQDL LVKAIIFPIS
YNLQQNQLSI SKILINTTIR NERESTTITI SNIVLLTKLH EFKSFIKRIA NPSNANPIPR
EVQVTASSNL FISKIMVNIA LKELKFVISN IVSFYDSFAS LSAKQSNSLE NSVLDFVRDR
SHKLEISSIL QPPGQSRRRI GPGFASPHLS NPTFVNISRN NIASFRCSIK EVELNLVQVL
PKFGGLTLRL KDILLYEQKN DINGSILSFD IVRVDDGQLQ KFVYEFQELP LESIRLPLIM
IHCKNTEKIS TVDVVIRNVL VEYYTQWLLL LDDFEANEEK LAELVVEKVK PVNPSSSQNR
FDIRFSVFDC IIGLNPGRLP CKSYLVVGRG TSDFTFGVNQ FYIKSSFRDV SALLIDDVKN
KEKMPLKDNS TSRSRKSLPT SSYTSPLTFF SNLGYIMIGG LNVVHIGITF NTNIEEVMKR
NEKLGISDNL SLIDLKINSD EHHLELCADS THVLLQLIND LKLPLNFKDD EKMKVTVDSS
INLMDDLDEN QFQLKKRNIS VAPGVETSSS SAGSENENLE TIAFDEDHFS KARNKIPKGS
KVDPFKLNIN LSKTKIYLYD GYDWKDTRKA VRGAVKRVEA QAMKERLKKL KKQTDKDDYD
EEDEFIEETL FSSIHVGIPR DATDANLTDR INKRVQSSLQ ETDMTPEEAQ KAQINVELGK
NYKNLKLRRS RVHKIMADFT NIEVNVSVYS TRDPRKDPTD ENLPYELLND VEVRLGTADV
YDNVATSTWN KLLTYMNTSG EGEIGKSMLK LAITNVRPSP KLVSSEAIMK VQVLPVRLHI
DQDTLDFLMR FLEFKDSRFS LPLDEIVYIQ KFQISPVMLK LDYKPKRVDY VGIRSGNSAE
FMNFFILDGS TINLAEATVY GLLGMPSLGK ALGEVWGPQI QQTQIAGILA GLAPIRSIVN
IGGGVKDLIA IPISEYKKDG RLFRSIQKGT QKFAKTTGYE ILNLGVKLAS GTQVILEQGE
QLLGGEGSGA RLPASRGSNS QKCNVNKRSS YKVAAKVDFN KLLANSQVLN QSVRVDRDQY
ANKKFYSYID IDEDDDELVT GIDKELLSKS IFLLPRDDNS KKEGEEDEAD DSSADEEGEK
LISLYSNQPE NIQEGMKLAY KSFGNNLKIT KRQLINLKNE LNESENIQDS LKSILKSSPI
IFIRPIIGST EALSKALMGL GNEIDSKRIV ESRDKYRYIK RAKDEDVL
