ATG2A_MOUSE
ID ATG2A_MOUSE Reviewed; 1914 AA.
AC Q6P4T0; Q3U9I1; Q6PHN0; Q6ZQC4; Q8R213;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Autophagy-related protein 2 homolog A {ECO:0000303|PubMed:21698225};
GN Name=Atg2a {ECO:0000303|PubMed:21698225};
GN Synonyms=Kiaa0404 {ECO:0000303|PubMed:14621295};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1696-1914.
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875 AND SER-877, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-869; SER-875; SER-877 AND
RP SER-1246, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=21698225; DOI=10.1371/journal.ppat.1002078;
RA Qin Q.M., Luo J., Lin X., Pei J., Li L., Ficht T.A., de Figueiredo P.;
RT "Functional analysis of host factors that mediate the intracellular
RT lifestyle of Cryptococcus neoformans.";
RL PLoS Pathog. 7:E1002078-E1002078(2011).
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. Lipid transfer activity is enhanced by WIPI1
CC and WDR45/WIPI4, which promote ATG2A-association with
CC phosphatidylinositol 3-monophosphate (PI3P)-containing membranes. Also
CC regulates lipid droplets morphology and distribution within the cell.
CC {ECO:0000250|UniProtKB:Q2TAZ0}.
CC -!- FUNCTION: (Microbial infection) Mediates the intracellular lifestyle of
CC Cryptococcus neoformans by supporting infection.
CC {ECO:0000269|PubMed:21698225}.
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 ATG9A (via C-terminus). Interacts with TMEM41B.
CC Interacts with VMP1. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97942.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE30685.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK129132; BAC97942.1; ALT_INIT; mRNA.
DR EMBL; BC022657; AAH22657.1; -; mRNA.
DR EMBL; BC056482; AAH56482.2; -; mRNA.
DR EMBL; BC063264; AAH63264.2; -; mRNA.
DR EMBL; AK151782; BAE30685.1; ALT_FRAME; mRNA.
DR CCDS; CCDS29500.1; -.
DR RefSeq; NP_919329.2; NM_194348.3.
DR AlphaFoldDB; Q6P4T0; -.
DR BioGRID; 236694; 5.
DR IntAct; Q6P4T0; 16.
DR MINT; Q6P4T0; -.
DR STRING; 10090.ENSMUSP00000046412; -.
DR iPTMnet; Q6P4T0; -.
DR PhosphoSitePlus; Q6P4T0; -.
DR EPD; Q6P4T0; -.
DR MaxQB; Q6P4T0; -.
DR PaxDb; Q6P4T0; -.
DR PRIDE; Q6P4T0; -.
DR ProteomicsDB; 265176; -.
DR Antibodypedia; 44102; 188 antibodies from 24 providers.
DR DNASU; 329015; -.
DR Ensembl; ENSMUST00000045351; ENSMUSP00000046412; ENSMUSG00000024773.
DR GeneID; 329015; -.
DR KEGG; mmu:329015; -.
DR UCSC; uc008ghu.1; mouse.
DR CTD; 23130; -.
DR MGI; MGI:1916291; Atg2a.
DR VEuPathDB; HostDB:ENSMUSG00000024773; -.
DR eggNOG; KOG2993; Eukaryota.
DR GeneTree; ENSGT00620000087966; -.
DR HOGENOM; CLU_001781_0_0_1; -.
DR InParanoid; Q6P4T0; -.
DR OMA; LQYVMSA; -.
DR OrthoDB; 196897at2759; -.
DR PhylomeDB; Q6P4T0; -.
DR TreeFam; TF313482; -.
DR BioGRID-ORCS; 329015; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Atg2a; mouse.
DR PRO; PR:Q6P4T0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6P4T0; protein.
DR Bgee; ENSMUSG00000024773; Expressed in granulocyte and 61 other tissues.
DR ExpressionAtlas; Q6P4T0; baseline and differential.
DR Genevisible; Q6P4T0; MM.
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 1: Evidence at protein level;
KW Autophagy; Endoplasmic reticulum; Lipid droplet; Lipid transport; Membrane;
KW Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..1914
FT /note="Autophagy-related protein 2 homolog A"
FT /id="PRO_0000315235"
FT DOMAIN 14..112
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT REGION 1222..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1383
FT /note="WIPI-interacting"
FT /evidence="ECO:0000250|UniProtKB:Q2TAZ0"
FT REGION 1427..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1803..1822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2TAZ0"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2TAZ0"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2TAZ0"
FT MOD_RES 1381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2TAZ0"
FT CONFLICT 285
FT /note="L -> M (in Ref. 1; BAC97942)"
FT /evidence="ECO:0000305"
FT CONFLICT 1738
FT /note="R -> G (in Ref. 3; BAE30685)"
FT /evidence="ECO:0000305"
FT CONFLICT 1865
FT /note="V -> M (in Ref. 3; BAE30685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1914 AA; 210939 MW; 16742111A5534572 CRC64;
MSRWLWPWSN CVKERVCRYL LQHYLGHFFQ EHLSLDQLSL DLYKGSVALR DIHLETWSVN
EFLRSMESPL ELVEGFVSSI EVAVPWAALL TDHCTVCVSG LQLTLQPRQG SGPGAADSQS
WASCMTTSLQ LAQECLREGL PEPSEPPQPL EGLEMFAQTI ETVLRRIKVT FLNTVVRVEH
SLGDEDRSVA VEVRVQRLEY CDEAVRDPSQ APPVDVHQPP AFLHKLLQLS GVCLYFEELP
SQADPPQPPL QIGSCTGYVE LMVRLKQNEA FPGPKLEVSG QLGSLHLLLT PRQLQQLQRL
LSAVNLADPA GLADKLNKSR PLGAEDLWLI EQDLNQQLQA GAVAESLSLY PITNPLNLDS
TDLFFSMAGL TSSVTSAVSE LSVYSVDLGS SVHSNMAFHR PSTPPHSGGK MAPTPLLDTT
RPDSLVKMTL GGVSLTLLQT ASPSSGPSDL PTHFFAEFDA AKDGPFGSRD FSHLRPRFQR
ACPCSHVRLT GTAVQLSWEL RTGSHSRRTS STEVHFGQLE VLECLWPRAA TEPEYTEILS
FPSHSGSEAS ARPCAHLRHT QTIRRVLKSR SRRSTACHCH SELSLDLADF QSDVELGSLD
RLAALFRQVT TPSEPPAGLL TEPPQATELQ TVFRLSAPRA TLRLRFPIPD LRPDRDPWAG
QAVRAEQLRL ELSEPQFRSE LNSGPGPPAP TRLELTCSDL QGIYEDGEKP PVPCLRVSKA
LNPRSTEAKY FLPQVVVTLN PQSSGTQWET AYEKGRDLEL STESPCELQQ PEPSPFSSKR
TMYETEEMVI PGDPEEMRTF QSRTLALSRC TLDVIMPSAH IFLPSKEVYE SIYNRINNDL
LMWEPADLLP TSSAAARPPG SSGFKMCKSA FKLDSDSDEE DAQFFSMASG VPQTPAPEPS
RRQSQSTFST LVTVLKGRIT ALCEAKDETG KRLDVTHGEL VLDVEQGTIF SVAQYRGQPG
LGYFCLEAEK AKLYHRAAIE DYLLPTHLEV PSFAPPAQLA PTIYPSEEGV TERGTLGRKG
QGPPMLSAAV RIHLDPHKNV KEFLVTVRLH KATLRHYMAP PEQSWHSQLL DFLDVLDDPV
LGYLPPTVIT VLHTHLFSCA VDYRPLYLPV RVLVTAETFT LSSNIVMDTS TFLLRFILDD
SALYLSDKCE VESLDLRRDY VCVLDIDLLE LVIKTWKGST EGRLSQPLFE LRCSNNVVHV
HSCADSCALL VNLLQYLTSS GDLHPPPRPP SPTEIAGQKL SESPASLPSC LPVETALINQ
RDLTDALLDT ERRGLQELAQ SSGGPLPQAS PVSVYLFPGE RSGAQAPLPP PGASSHTLGS
KAKEHENEEE GDGDTLDSDE FCILDAPGLG IAPRDGEPIV TQLHPGPIIV HDGHFSQPLG
STDLLRAPAH FPVPSSRVVL REVSFIWHLY GGRDFGLHPT YRARVGLTGP RVSPSRSSGP
NRPQNSWRTQ GGIGRQHQVL MEIQLSKVSF QHEVYPEESA IAGGLGQELD ERPLSRQVLI
VQELEIRDRL ATSKINKFLH LHTSERLPRR THSNMLTIKA LHVAPTSSVG GPECCLRVSM
MPLRLNVDQD ALFFLKDFFT SLAASINPMV PGDTSEAPRE THSRPGSPQE GQSEDTETAS
NPPEAPGSSH SSSDQQPIYF REFRFTSEVP ICLDYHGKHV TVDQVGTFMG LLIGLAQLNC
SELKLKRLCC RHGLLGVDKV LCYALNEWLQ DIRKNQLPGL LGGVGPMHSV VQLFQGFRDL
LWLPIEQYRK DGRLIRGLQR GAASFGSSTA SAALELSNRL VQAIQATAET VYDILSPASP
VSRSLQDKRS SRKLRRGQQP ADLREGMAKA YDAVREGILD TAQTICDVAS RGHEQKGLTG
AVGGVIRQLP PTVVKPIIVA TEATSNVLGG MRNQILPDAH KDHALKWRLE EAQD
