ATG2_CAEEL
ID ATG2_CAEEL Reviewed; 2290 AA.
AC Q21480;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Autophagy-related protein 2 {ECO:0000305};
GN Name=atg-2 {ECO:0000312|WormBase:M03A8.2};
GN ORFNames=M03A8.2 {ECO:0000312|WormBase:M03A8.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH EPG-6, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 715-TRP--LYS-2290.
RX PubMed=21802374; DOI=10.1016/j.devcel.2011.06.024;
RA Lu Q., Yang P., Huang X., Hu W., Guo B., Wu F., Lin L., Kovacs A.L., Yu L.,
RA Zhang H.;
RT "The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates progression of
RT omegasomes to autophagosomes.";
RL Dev. Cell 21:343-357(2011).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=25124690; DOI=10.15252/embr.201438618;
RA Wu Y., Cheng S., Zhao H., Zou W., Yoshina S., Mitani S., Zhang H., Wang X.;
RT "PI3P phosphatase activity is required for autophagosome maturation and
RT autolysosome formation.";
RL EMBO Rep. 15:973-981(2014).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF 715-TRP--LYS-2290.
RX PubMed=30102152; DOI=10.7554/elife.36588;
RA Liu Y., Zou W., Yang P., Wang L., Ma Y., Zhang H., Wang X.;
RT "Autophagy-dependent ribosomal RNA degradation is essential for maintaining
RT nucleotide homeostasis during C. elegans development.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Lipid transfer protein involved in autophagosome assembly and
CC in the distribution of atg-9 and atg-13 during the autophagy-mediated
CC degradation of protein aggregates (PubMed:21802374, PubMed:25124690).
CC Tethers the edge of the isolation membrane (IM) to the endoplasmic
CC reticulum (ER) and mediates direct lipid transfer from ER to IM for IM
CC expansion (By similarity). Binds to the ER exit site (ERES), which is
CC the membrane source for autophagosome formation, and extracts
CC phospholipids from the membrane source to the IM for membrane expansion
CC (By similarity). Involved in autophagy-mediated degradation of
CC ribosomal RNA and ribosomal proteins in lysosomes, which is essential
CC for maintaining nucleotide homeostasis (PubMed:30102152).
CC {ECO:0000250|UniProtKB:Q2TAZ0, ECO:0000269|PubMed:21802374,
CC ECO:0000269|PubMed:25124690, ECO:0000269|PubMed:30102152}.
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:Q2TAZ0};
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:Q2TAZ0};
CC -!- SUBUNIT: Interacts with epg-6; the interaction is direct.
CC {ECO:0000269|PubMed:21802374}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q96BY7}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96BY7}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q96BY7}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P53855}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53855}. Cytoplasm
CC {ECO:0000305|PubMed:21802374}.
CC -!- SIMILARITY: Belongs to the ATG2 family. {ECO:0000305}.
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DR EMBL; BX284606; CCD70983.2; -; Genomic_DNA.
DR RefSeq; NP_509145.3; NM_076744.6.
DR AlphaFoldDB; Q21480; -.
DR ComplexPortal; CPX-3823; epg-6-atg-2 complex.
DR STRING; 6239.M03A8.2; -.
DR EPD; Q21480; -.
DR PaxDb; Q21480; -.
DR PeptideAtlas; Q21480; -.
DR EnsemblMetazoa; M03A8.2.1; M03A8.2.1; WBGene00019748.
DR EnsemblMetazoa; M03A8.2.2; M03A8.2.2; WBGene00019748.
DR GeneID; 180949; -.
DR KEGG; cel:CELE_M03A8.2; -.
DR CTD; 180949; -.
DR WormBase; M03A8.2; CE47193; WBGene00019748; atg-2.
DR eggNOG; KOG2993; Eukaryota.
DR GeneTree; ENSGT00620000087966; -.
DR HOGENOM; CLU_001781_0_0_1; -.
DR InParanoid; Q21480; -.
DR OMA; VKRPIID; -.
DR OrthoDB; 196897at2759; -.
DR PhylomeDB; Q21480; -.
DR PRO; PR:Q21480; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00019748; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IEA:InterPro.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0016236; P:macroautophagy; IC:ComplexPortal.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR InterPro; IPR026849; ATG2.
DR InterPro; IPR026886; ATG2_fungi/plants.
DR InterPro; IPR015412; Autophagy-rel_C.
DR InterPro; IPR026854; VPS13-like_N.
DR InterPro; IPR031645; VPS13_C.
DR PANTHER; PTHR13190; PTHR13190; 1.
DR PANTHER; PTHR13190:SF1; PTHR13190:SF1; 1.
DR Pfam; PF09333; ATG_C; 1.
DR Pfam; PF12624; Chorein_N; 1.
DR Pfam; PF16909; VPS13_C; 1.
PE 1: Evidence at protein level;
KW Autophagy; Coiled coil; Cytoplasm; Endoplasmic reticulum; Lipid droplet;
KW Lipid transport; Membrane; Reference proteome; Transport.
FT CHAIN 1..2290
FT /note="Autophagy-related protein 2"
FT /id="PRO_0000446906"
FT DOMAIN 10..99
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT REGION 829..1549
FT /note="Required for epg-6 binding"
FT /evidence="ECO:0000269|PubMed:21802374"
FT REGION 1678..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1805..1851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1898..1919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1967..2003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1972..2011
FT /evidence="ECO:0000255"
FT COMPBIAS 1681..1695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1722
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1809..1848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1899..1914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1967..1981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1982..2000
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 715..2290
FT /note="Missing: In bp576; Accumulation of early autophagic
FT structures and defective degradation of P-granules and
FT protein aggregates. Irregular distribution of protein
FT aggregates containing the autophagy protein atg-9.
FT Suppresses the lysosomal accumulation of ribosomal RNA and
FT ribosomal proteins in a rnst-2 qx245 mutant background."
FT /evidence="ECO:0000269|PubMed:21802374,
FT ECO:0000269|PubMed:30102152"
SQ SEQUENCE 2290 AA; 256298 MW; 1696F3EAC361808E CRC64;
MTLSTFNRVW CKVMLQRYMG AWLDNNLSVD QLSLELANGC LELDNLDINT KAVSNGFLQC
NIPLKLIDGY LGKIKIEIPW LSLMTDPTRM CIEDLQLTFR GAEVMKINDI ETLTSMIESV
LMGLSTDDMA RSVYEEVSKE NNVASELLGP DDTADSFSGF IDAVYSRFCL KIKHLTLRFE
TDPKNRSTMA TALEIRVETI TFMDEQMRSC EMDHTNATDL VTTQPHGVVS TTNLRKNLTF
SGVTFHTDVF SQINNDGMGD EENVLITSMH IRREKAKQMS PTKSVQNSLH PEMFQSAMSD
MDAFHSCYDK LTQDYCSPDQ LETLRTAPAE PELFSAPIQC AEVVGDISCV FRIKNGANDV
NYADVDESKV ETDVFIKGIN VFATPSQIEI VNRFFSSIVT PKELVVHEQG KPMSKEDYEN
MTKNMEPNQS NEPPMAGASF GGNWNVGEVF REFDDLKSIK EKEKSEKEKF KSLKASGNIK
EEFTVNTHIG TVLMYIPHCD YMSSDYAQQH GGYANVLNYL KKESESFFKS IQGYSFMSKH
GLANIRQQSD SFYPKDHLRI VGGSLGITSS CKRVGNVDSF LCRVVATHFD MLEYLTPESA
PENSTPIRIG LLDYSEQENL ESDPNFKMVL STSSEQKGLT KVDILLGAVK TELDFSIIDR
ISNLIACRPF FDEALTNYGN RNTVPQLKDD LYSDVLIAED DVKSKTLVNL KCSNWQVDLR
IPKADLRDPT GSRLPFSQRH VHNEFLRLGI KEIDVSIPIE KSVTLIEILC TEMIGDFCGE
GLNIPKQQQR ILHASKNGFD KINLKLTLCS DAKKLPGCGR KTSTSGIPDS MMKSVSADIM
MAHPKKEGPF SKVPRSYCSH DGEETEEIIQ AGTRKEILDF QEECQNFAST FMLFTVPVLK
LHIPEKNFLE ILYNRLVNDL ALFQPAAPAF RNNQSTNSNV QPLESFQECV SPKNYAESEH
SDLDDDVATL HESIESLNFD RDIPHTFVMT LNANKCTVLC NTAIKEAEKQ PESSQVSLDL
EKVHIGTTAG YHGDINHTYF HFTSSKAAAG SIDSPRAPRI PNLISAKDFG KWTKDCNQLE
HVPITDELSS GSTEDAFAVA LHMHFRPDVN MKDVLLGIAL RNSQLQAKPF RHWGAFWITQ
LADLFTLQDY AIPGYELPSV STDLHICFEN AIIGYDHAWV NPNSKLKLRA TLGQCNLASS
IVSDMNISKT LCIFESCRLY MSNDLTKDAV RFEGYGTQKV SPKKFIPFLD LGSVQLDILF
AVGDETGLRT NPTFEIRCQN DIINAWACAD SLATFMKTVM EYTSHEQIPI KTPEEESQEL
MKSTKTDDIN KSVAGESVWS DASTGSKHIQ KMTVGANLPD DVEKRIQAMI QEAVNENDER
DGIAIGEDAV REFATIQPKH DANETNESFE HVASRNFSVT DDEFCMVDDN IFGSGITIQP
GESRTRPMPA KQLPEEPLIN GSEFFQTIED SGSDALYQTM SGQINPVLRY FLKDVTVRLS
LYAGNDLSTS PSPIKTYCTE EYRNGFGPEQ KIEQNSTGGP NRDHSAFVVF ELSKITYLKQ
IFDKTAPMLS TTLFQVNDIV IKDCVRASDI KEMLYQYSVT NQPRRATAPI VTVRMSETHS
KEGKMRVSML PIKINVDQDT LEFLTDFFEE TSKLLDLPKN QMSMPLIQRP VIEVPADIGS
KKTTPKTSVS SSEGDIARMY PSIPSPSLTL EPLRPSPVQP PTPLGDLTYL EKISSNHQSP
VKRPIIDAPL TASAVSIGKI FERDAHSDED EEEIIDPIQM AAALEIRELN EELGRIEQLE
KKKTDDLFKQ SYSSSSSETE SESSAPQSSQ VRRLHESLDA SNPTGLSDLT GDWADDHDLT
YTHHDVVRQE SPSFNCNISP IKGYSPPAEL RPLNLMDSET ERDSSASPVT SSPIKPARNI
KKELPPLKMP RQPLSNDDIL MRSTMMGSVH PSQSVHNLVD TSDDLEEHGN FLDSIDNEDD
NEKQKIEEEM EEDEKEEEEE RNKEIQEAVE RGETFFKQFV FSPSVNIYVD YQGKRKITME
KAGALVGLLM AFGQLNQMPI NLRKIDTRTG LLGTGRCMQH AIGEWSGDLL TNMPSVIASY
GPISPLVQIG RGVVDLFLMP VAEFRKDDGN VMKGVQRGVG SFSVSSAAGI VGMAQTVTGF
VQSLAEMTMK EIKPDDPSTR RVARRYNRNH GMNPTDVRHS LQLAYGILYD GYHQTRDDLE
LAAQEDRASG NSVVRSAFRY AVPTFLGPIV MATQVTYQLL GGLRNQLRPD TYQDERRKWG
EKDVPGGVNK
