ATG2_CHAGB
ID ATG2_CHAGB Reviewed; 2043 AA.
AC Q2GYD8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Autophagy-related protein 2;
GN Name=ATG2; ORFNames=CHGG_07016;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408033; EAQ85763.1; -; Genomic_DNA.
DR RefSeq; XP_001224672.1; XM_001224671.1.
DR AlphaFoldDB; Q2GYD8; -.
DR STRING; 38033.XP_001224672.1; -.
DR PRIDE; Q2GYD8; -.
DR EnsemblFungi; EAQ85763; EAQ85763; CHGG_07016.
DR GeneID; 4394055; -.
DR eggNOG; KOG2993; Eukaryota.
DR HOGENOM; CLU_000626_1_0_1; -.
DR InParanoid; Q2GYD8; -.
DR OMA; HRWDSTQ; -.
DR OrthoDB; 54301at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
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..2043
FT /note="Autophagy-related protein 2"
FT /id="PRO_0000317807"
FT REGION 111..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1392
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2043 AA; 221553 MW; DA33AC1F6C745A8E CRC64;
MASFFQSFRS SSMAKQLLRF ALSRLDLLDT QALDLENLDF ALGRNTVLEF RDVGLILQKL
ERLLGLPPAF SLQKAKVLIL RVTIPMDFYA SPITAEIDGV DIRLKVASKK EKDRQDAGKR
GKGMAGSEAV PTAADLAQSF LETQPVAEKE ELEQALAAET QDLAASMAAS EPESDDDSPV
GTGQPLSLPV FLTNFLHGIV DRIQIRVQSV TFQADVEVAV DSNSPVPEPV TFQLSLDNIN
VEGVTSTSET PDEASTIVHK EGKRHVLLDN IRAALITETN VLSSLARSAS MPSSSASRSP
VAPRSPVDNE TTAFNPSGLS RSVGSSAMAG SRDSSDDLPQ SQHLQDNEAA FNIPYDFGDS
NEPNEADEAS PLSTPRASLY RGSPPPTITD HAKSAVLEPS PLIWSTAERE AQSVPFLRPP
EGFPLSNDPS PAASVHSSST NRSSGSSARD DLAESHIYSH EDAESMYMSA FSQTGSQGLR
TGMPGAWDAF DDAEESETEA GPSTSTQAAP YDGSFDPPQP DRIPSPEQPS QDQKRNSPSF
YAQDSSAEVP EPPQDDIPTP RGPTRLVKQL LSLSSISIYL PSSHKHVKID TPDDGKSISP
NIPGAFSMHS AAATSPKPTP ADEPAGETTP IDPSIEIVLK PVEIQFDASI GFLLAMVVAQ
LLEAAQGGSK DAAGPTAAKP PSASPDVKVT VEQLSVLFLE KLAGVADVPQ RFFEKSTPDL
SSDVLLQAQV VDLRGSVSHD GPQTEMDFSI EKLKFGYAND DIVSFDRSVL MFESVANTFP
SAGQDISVKA TMGPEISRLE VNTLPLYVQL DLQKLDEVFG WFGGLSSFLN MGTSITANTS
RADKSPANPV QKPKGVRFDE PVHPDDQAVT RENKTDLRIN GLQVDVLGKD CSVMLNTSAF
KLVSREGGIG IHLSRIRLSG PYFKNSRAEP PIVSEVLDTR VEFLPSPRAK DLERLLELIT
PSSNKFDEDE DEIMVDTLLR QRRKGSVLSL AIGKVRFDAG NLPQLTCLPS LIDDLAKLGT
VAKYLPEDDR PGLLTLCHVK NAECRVDFGG RFGAILTSLT DLEVAHISMP QLAAVALGEI
AVTRNKIEEL VVTSPPPQTG PWQNLPVFRL RLIDDMEPVL KIKLMGLGLE YRVPTIMDLL
NLGQDVTPED YEAGLAASVA SLGEQAHTVI KRASSGSLTS TGQAKAPRSL KVDVAFRDCL
IGLNPLALPS KLTVALTDAH LEMVPGPQEL VAVTTMKRVS VLLIDDISIL ESPGVRFTTS
RRPPVVISTQ VAELCTMGYV NICQISSAKA TVTVSRDSQG DTQLEVEVRD DLLVLETCAD
STQTLITLAN ALTPPTPPST EIKYRTTVFP VEDLLASIRA ETFGRAEGEY DLDNDFDVPQ
ELGDDADSDL DFDAGPSDSP LNLDSQYLEE NIVQEELFDA TSSSMLREGA TKFEDTNDGV
LLSTAGLDNP SSSGLEISSS DLSITDDYFD KGPVGRGTAH RWDSKTDRYD QHNEIKLQRS
PLKLCVRDVH VIWHLFDGYD WERTREVIAK AVKEVEAKAY ERRAKTDRRG GFDPEFGEDE
PIIGDCLFNS IYIGIPSNRD PKELAQAINH GLHDFGDTES IATSTVTTST LRAAGQRRRS
KSLRLDRSRR HKITFELKGV SADVVMFPPG SGETVNSLDI RLRDVDVFDH VPESTWKKFA
TYDLDAGERE LGADMVHAEI ITTKPADTPA TEMVISATIL PLRLHVDQDA LDFITRFFTF
RDETAPIHAS PSDVPFIQRI VVNSIPIQLD FKPKRVDYAG LRSGKTTEFM NFMILEGARL
VLRRVILYGV SGFDRLGDQL NDIWTVDVKR NQLPGVLAGL APVRSLVNAG SGFRDLIEIP
IREYRKDGRI VRSLRKGATA FAKTTGTEVV KLGAKLAIGT QNVLQGAEGL LVPQTGESSS
NAAAVAAVLG DDWDEAEYEE EINRKFSLYA DQPLGIVQGV RGAYASLARD LSVARDAIIA
VPAEIMESEG AQGAAAAVLK KAPTIILRPA IGATKAIGQT LLGATNSLDP MHRKRVDAKY
KKH
