ATG2A_XENTR
ID ATG2A_XENTR Reviewed; 1997 AA.
AC Q08D51;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Autophagy-related protein 2 homolog A {ECO:0000250|UniProtKB:Q2TAZ0};
GN Name=atg2a {ECO:0000250|UniProtKB:Q2TAZ0};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lipid transfer protein involved in autophagosome assembly.
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. Binds to the ER exit site (ERES), which is the membrane
CC source for autophagosome formation, and extracts phospholipids from the
CC membrane source and transfers them to atg9 (atg9a or atg9b) to the IM
CC for membrane expansion. Also regulates lipid droplets morphology and
CC distribution within the cell. {ECO:0000250|UniProtKB:Q2TAZ0}.
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 -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q2TAZ0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96BY7}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q96BY7}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q2TAZ0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53855}. Note=Localizes to endoplasmic
CC reticulum-autophagosome contact sites. {ECO:0000250|UniProtKB:Q2TAZ0}.
CC -!- DOMAIN: The chorein N-terminal domain mediates lipid transfer activity.
CC {ECO:0000250|UniProtKB:Q2TAZ0}.
CC -!- SIMILARITY: Belongs to the ATG2 family. {ECO:0000305}.
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DR EMBL; BC123939; AAI23940.1; -; mRNA.
DR RefSeq; NP_001072654.1; NM_001079186.1.
DR AlphaFoldDB; Q08D51; -.
DR DNASU; 780111; -.
DR Ensembl; ENSXETT00000062409; ENSXETP00000060540; ENSXETG00000031818.
DR GeneID; 780111; -.
DR KEGG; xtr:780111; -.
DR CTD; 23130; -.
DR Xenbase; XB-GENE-5818802; atg2a.
DR InParanoid; Q08D51; -.
DR OrthoDB; 196897at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000031818; Expressed in skeletal muscle tissue and 12 other tissues.
DR ExpressionAtlas; Q08D51; differential.
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:0044232; C:organelle membrane contact site; ISS:UniProtKB.
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:0120013; F:lipid transfer activity; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR InterPro; IPR026849; ATG2.
DR InterPro; IPR015412; Autophagy-rel_C.
DR InterPro; IPR026854; VPS13-like_N.
DR PANTHER; PTHR13190; PTHR13190; 1.
DR Pfam; PF09333; ATG_C; 1.
DR Pfam; PF12624; Chorein_N; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid droplet; Lipid transport; Membrane;
KW Reference proteome; Transport.
FT CHAIN 1..1997
FT /note="Autophagy-related protein 2 homolog A"
FT /id="PRO_0000315236"
FT DOMAIN 17..119
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT REGION 241..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1684..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1494..1534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1997 AA; 221925 MW; F2BD7E2701ED1ACF CRC64;
MSRWLFPWSS SIKTRACRYL LQHYLGHYLE ERLSLEQLSL DLYNGSGRLT DIHLDIWSVN
ELLDSAGAPL EIIDGFIGSI SVTIPWSALV TENCTLEVSK LQVTCRPKYR GAAQGTESQS
WSSCMTTSMQ LAQECLKEQP EEPSEPPQPI EGLEMFAQTI ETVLRRIKVT FIDTIVRIEN
NPGDSNLGTA LEIHIKRLDY CDEAVRDSPH TVPVDIHQPP AFIQKILQLS GVSLHYEEFK
TSVQTPSPTP ENPLESEPVQ PSKTPSWPEE PQPAPSPIQQ IGSCSGCTEL TIKLKQNDLF
PGPKLDIDGK IGSVHLFLTP RQISNLQEIL DALSISESSA IREKLLKSRP LDLEDLKLIE
QDLNQQLQSG PGSLFVPDPE LVPFQTIENG DMFYSMAAMT NSMTSIRSAN ELSDIDLESS
MYSDYSSQQI PSLTPGIMLS SPRKYGRTPF SATLPQNLHK LPGKSSHPPS MELLKPEMLL
RLTLGGLTVT VPHISTYISP QEDPACPEVA RHFFRELGYF KDSAFSGRDF SHLRGQFEKA
CHLSNIRVTA VAVQLVCEQR VGGGTHQSSV DLSCGRLEIL ECLRQGESTS RRTKNTEYTK
LMTFCSPSTS SRPCAQIHYK RSQKTPTRSS RKKQEIKVSS EILVELEEFQ TDIDLGLLDR
LGSIFQNGAC RESYSQNDLH MTDVPQSSED MEIRVVASKS HICLQFPVPD LRPSLERRPW
AEKAVRKDCL QMEVADLDIH SQSKTGTDEA RKIEITFSDL HGVYTDGEKL NVPCIRVSKG
ADPLAKAGGK KFIFPSILVA ILPQSKVSPW YLAQDKIDDI DHPSVESPCE LKQPEPSPFS
SKRTMFETEE MVIPADPNEM ADFQHVTLAS SQYTLEITLP RAHVFFPSKE VYESLYNRLC
NDLLMWEPVP ELGASISDSL LSAEPHTTSN YQQDTFRMCK SAFKLDSDSD DEDSHFYSVD
EAARHRRGAQ DGQSYFSASV TILKGRITAW TEAKGEGAKK LDDHHGEVVL DVENGCIFSV
SKYRGKEDLS YLCIQSESVA LYHKATVKDY LAPVSLEIPT FLHPTNLDPT IYLSEEGVSA
QLSGARKDRN QKMLSLAVRI DLNLVKNVKE FLVALRLDGA TLRHHMALPY QSWHSQILDF
LDVVDEPILG YSPPAVITVL HTHLFSCAVD YRPLYLPIRV LITAETFTLS SNIVVDTSTF
LLRFILDDSA LYLSDKCDAE VTDLRKDYVC VLDVDLLELV ITTWKGNASS KLTQPLFELR
CSNNVLHIHT CADSCAMLVN LTQYVMNNGD LHCPPKPEPP TEIAGQKLQP PEGPSSLPPC
LPAETAQINQ GDLTDALIDT GRTGKEQPET AISVDAALLE ESPVSVYLFP EEIKSGNKRQ
TTSPSPPPLT EGRVSQESLG LSDTSGDSEL TDTDDFCILD APGIGVPPKD GEPVVRKLVD
SPIAVRDGHF SRPLGSTDLL KPPAKFPVPE TRIVLREISV VWHLYGGKDF GSSRPNSARA
QSPRSRTSFH NARGSPSRSS VTNRPQNTWR TQGGNGRIHD ILMEIQLTKV SFQHESYPEP
LADGEEKLHT GDLDELPLAR QVFIVQELEI RDRLASSHIN KFLYLYTSEK MPRRAHSNML
TIKALHVRPE AGLGGPECYL RMSLMPLRLN IDQDALFFLK DFFTSLASGI QTIVPMELGS
EASRLDGPAK SSSDCELEQE TSQGSTEDET MSPSSSTDQP IYFREFRFTS EVPIWLDYQG
KHVTTEQVGT FAGILIGLAQ LNCSELKLKR LYCRHGLLGA DKVVSYALNE WLTDIRKNQL
PGILGGVGPM HSVVQLFHGV RDLFWLPIEQ YRKDGRIIRG LQRGAASFGT STASAALELS
NRLVQAIQAT AETVYDILSP TPPVSRCALD VRQSRKLRRG QQPADLREGV AKAYDTVREG
VIDTAHTICE VASRGHEQKG LTGAVGGVLR QIPPTVVKPF IVATEATSNL LGGMRNQIRP
DAHKEDALKW RADEGQD
