ATG2A_HUMAN
ID ATG2A_HUMAN Reviewed; 1938 AA.
AC Q2TAZ0; O43154; Q14DM2; Q6ZTV2; Q7Z6K8; Q8IVY5; Q8TAI8; Q96HH7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Autophagy-related protein 2 homolog A {ECO:0000303|PubMed:21887408};
GN Name=ATG2A {ECO:0000303|PubMed:21887408, ECO:0000312|HGNC:HGNC:29028};
GN Synonyms=KIAA0404 {ECO:0000303|PubMed:9455477};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-656.
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1189-1938 (ISOFORM 2), AND VARIANT ARG-656.
RC TISSUE=Cervix, Hippocampus, and Skin;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=21887408;
RA Romanyuk D., Polak A., Maleszewska A., Sienko M., Grynberg M., Zoladek T.;
RT "Human hAtg2A protein expressed in yeast is recruited to preautophagosomal
RT structure but does not complement autophagy defects of atg2Delta strain.";
RL Acta Biochim. Pol. 58:365-374(2011).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22219374; DOI=10.1091/mbc.e11-09-0785;
RA Velikkakath A.K., Nishimura T., Oita E., Ishihara N., Mizushima N.;
RT "Mammalian Atg2 proteins are essential for autophagosome formation and
RT important for regulation of size and distribution of lipid droplets.";
RL Mol. Biol. Cell 23:896-909(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1301; SER-1309 AND SER-1402,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP INTERACTION WITH WDR45.
RX PubMed=28820312; DOI=10.1080/15548627.2017.1359381;
RA Zheng J.X., Li Y., Ding Y.H., Liu J.J., Zhang M.J., Dong M.Q., Wang H.W.,
RA Yu L.;
RT "Architecture of the ATG2B-WDR45 complex and an aromatic Y/HF motif crucial
RT for complex formation.";
RL Autophagy 13:1870-1883(2017).
RN [11]
RP FUNCTION, AND INTERACTION WITH WDR45.
RX PubMed=28561066; DOI=10.1038/ncomms15637;
RA Bakula D., Mueller A.J., Zuleger T., Takacs Z., Franz-Wachtel M.,
RA Thost A.K., Brigger D., Tschan M.P., Frickey T., Robenek H., Macek B.,
RA Proikas-Cezanne T.;
RT "WIPI3 and WIPI4 beta-propellers are scaffolds for LKB1-AMPK-TSC signalling
RT circuits in the control of autophagy.";
RL Nat. Commun. 8:15637-15637(2017).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31271352; DOI=10.7554/elife.45777;
RA Maeda S., Otomo C., Otomo T.;
RT "The autophagic membrane tether ATG2A transfers lipids between membranes.";
RL Elife 8:0-0(2019).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS
RP OF LEU-54; ILE-80; VAL-82; LEU-101; LEU-103; ILE-167; PHE-171; VAL-193;
RP TYR-200; LEU-223; MET-259; LEU-285; VAL-304 AND TRP-328.
RX PubMed=30952800; DOI=10.1083/jcb.201811139;
RA Valverde D.P., Yu S., Boggavarapu V., Kumar N., Lees J.A., Walz T.,
RA Reinisch K.M., Melia T.J.;
RT "ATG2 transports lipids to promote autophagosome biogenesis.";
RL J. Cell Biol. 218:1787-1798(2019).
RN [14]
RP INTERACTION WITH ATG9A.
RX PubMed=32610138; DOI=10.1016/j.celrep.2020.107837;
RA Guardia C.M., Tan X.F., Lian T., Rana M.S., Zhou W., Christenson E.T.,
RA Lowry A.J., Faraldo-Gomez J.D., Bonifacino J.S., Jiang J., Banerjee A.;
RT "Structure of human ATG9A, the only transmembrane protein of the core
RT autophagy machinery.";
RL Cell Rep. 31:107837-107837(2020).
RN [15]
RP INTERACTION WITH ATG9A.
RX PubMed=33106659; DOI=10.1038/s41594-020-00520-2;
RA Maeda S., Yamamoto H., Kinch L.N., Garza C.M., Takahashi S., Otomo C.,
RA Grishin N.V., Forli S., Mizushima N., Otomo T.;
RT "Structure, lipid scrambling activity and role in autophagosome formation
RT of ATG9A.";
RL Nat. Struct. Mol. Biol. 27:1194-1201(2020).
RN [16]
RP INTERACTION WITH ATG9A; TMEM41B AND VMP1.
RX PubMed=33850023; DOI=10.1073/pnas.2101562118;
RA Ghanbarpour A., Valverde D.P., Melia T.J., Reinisch K.M.;
RT "A model for a partnership of lipid transfer proteins and scramblases in
RT membrane expansion and organelle biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
RN [17] {ECO:0007744|PDB:6KLR}
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 1374-1404 IN COMPLEX WITH WDR45B,
RP INTERACTION WITH WDR45 AND WDR45B, AND MUTAGENESIS OF VAL-1381; THR-1382;
RP ILE-1389; TYR-1395 AND PHE-1396.
RX PubMed=32483132; DOI=10.1038/s41467-020-16523-y;
RA Ren J., Liang R., Wang W., Zhang D., Yu L., Feng W.;
RT "Multi-site-mediated entwining of the linear WIR-motif around WIPI beta-
RT propellers for autophagy.";
RL Nat. Commun. 11:2702-2702(2020).
CC -!- FUNCTION: Lipid transfer protein involved in autophagosome assembly
CC (PubMed:28561066, PubMed:31271352, PubMed:30952800). Tethers the edge
CC of the isolation membrane (IM) to the endoplasmic reticulum (ER) and
CC mediates direct lipid transfer from ER to IM for IM expansion
CC (PubMed:31271352, PubMed:30952800). Binds to the ER exit site (ERES),
CC which is the membrane source for autophagosome formation, and extracts
CC phospholipids from the membrane source and transfers them to ATG9
CC (ATG9A or ATG9B) to the IM for membrane expansion (PubMed:31271352,
CC PubMed:30952800). Lipid transfer activity is enhanced by WIPI1 and
CC WDR45/WIPI4, which promote ATG2A-association with phosphatidylinositol
CC 3-monophosphate (PI3P)-containing membranes (PubMed:31271352). Also
CC regulates lipid droplets morphology and distribution within the cell
CC (PubMed:22219374, PubMed:28561066). {ECO:0000269|PubMed:22219374,
CC ECO:0000269|PubMed:28561066, ECO:0000269|PubMed:30952800,
CC ECO:0000269|PubMed:31271352}.
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:0000269|PubMed:30952800};
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:0000269|PubMed:30952800,
CC ECO:0000269|PubMed:31271352};
CC -!- SUBUNIT: Interacts with ATG9A (via C-terminus) (PubMed:32610138,
CC PubMed:33106659, PubMed:33850023). Interacts (via WIPI-interacting
CC region) with WDR45B/WIPI3 (PubMed:32483132). Interacts (via WIPI-
CC interacting region) with WDR45/WIPI4 (PubMed:28820312,
CC PubMed:32483132). Interacts with TMEM41B (PubMed:33850023). Interacts
CC with VMP1 (PubMed:33850023). {ECO:0000269|PubMed:28820312,
CC ECO:0000269|PubMed:32483132, ECO:0000269|PubMed:32610138,
CC ECO:0000269|PubMed:33106659, ECO:0000269|PubMed:33850023}.
CC -!- INTERACTION:
CC Q2TAZ0; Q7Z3C6: ATG9A; NbExp=4; IntAct=EBI-2514077, EBI-727146;
CC Q2TAZ0; O95166: GABARAP; NbExp=2; IntAct=EBI-2514077, EBI-712001;
CC Q2TAZ0; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-2514077, EBI-746969;
CC Q2TAZ0; P60520: GABARAPL2; NbExp=2; IntAct=EBI-2514077, EBI-720116;
CC Q2TAZ0; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-2514077, EBI-373144;
CC Q2TAZ0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2514077, EBI-16439278;
CC Q2TAZ0; O96008: TOMM40; NbExp=7; IntAct=EBI-2514077, EBI-1057581;
CC Q2TAZ0; Q9Y484: WDR45; NbExp=5; IntAct=EBI-2514077, EBI-2682844;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:30952800}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96BY7}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q96BY7}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:30952800}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53855}. Note=Localizes to endoplasmic
CC reticulum-autophagosome contact sites. {ECO:0000269|PubMed:30952800}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q2TAZ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2TAZ0-3; Sequence=VSP_030515;
CC Name=3;
CC IsoId=Q2TAZ0-4; Sequence=VSP_030510, VSP_030516;
CC Name=4;
CC IsoId=Q2TAZ0-5; Sequence=VSP_030511, VSP_030512;
CC -!- DOMAIN: The chorein N-terminal domain mediates lipid transfer activity.
CC {ECO:0000269|PubMed:30952800}.
CC -!- SIMILARITY: Belongs to the ATG2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA23700.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB007864; BAA23700.1; ALT_INIT; mRNA.
DR EMBL; AK126181; BAC86477.1; -; mRNA.
DR EMBL; AP001187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008593; AAH08593.1; -; mRNA.
DR EMBL; BC027481; AAH27481.1; -; mRNA.
DR EMBL; BC053596; AAH53596.1; -; mRNA.
DR EMBL; BC110650; AAI10651.1; -; mRNA.
DR EMBL; BC113091; AAI13092.1; -; mRNA.
DR CCDS; CCDS31602.1; -. [Q2TAZ0-1]
DR PIR; T00051; T00051.
DR RefSeq; NP_055919.2; NM_015104.2. [Q2TAZ0-1]
DR RefSeq; XP_011543165.1; XM_011544863.2. [Q2TAZ0-3]
DR PDB; 6KLR; X-ray; 2.21 A; A/B=1374-1404.
DR PDBsum; 6KLR; -.
DR AlphaFoldDB; Q2TAZ0; -.
DR SMR; Q2TAZ0; -.
DR BioGRID; 116748; 41.
DR IntAct; Q2TAZ0; 101.
DR STRING; 9606.ENSP00000366475; -.
DR TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; Q2TAZ0; -.
DR PhosphoSitePlus; Q2TAZ0; -.
DR BioMuta; ATG2A; -.
DR DMDM; 296439433; -.
DR EPD; Q2TAZ0; -.
DR jPOST; Q2TAZ0; -.
DR MassIVE; Q2TAZ0; -.
DR MaxQB; Q2TAZ0; -.
DR PaxDb; Q2TAZ0; -.
DR PeptideAtlas; Q2TAZ0; -.
DR PRIDE; Q2TAZ0; -.
DR ProteomicsDB; 61475; -. [Q2TAZ0-1]
DR ProteomicsDB; 61476; -. [Q2TAZ0-3]
DR ProteomicsDB; 61477; -. [Q2TAZ0-4]
DR ProteomicsDB; 61478; -. [Q2TAZ0-5]
DR Antibodypedia; 44102; 188 antibodies from 24 providers.
DR DNASU; 23130; -.
DR Ensembl; ENST00000377264.8; ENSP00000366475.3; ENSG00000110046.13. [Q2TAZ0-1]
DR Ensembl; ENST00000421419.3; ENSP00000410522.3; ENSG00000110046.13. [Q2TAZ0-4]
DR GeneID; 23130; -.
DR KEGG; hsa:23130; -.
DR MANE-Select; ENST00000377264.8; ENSP00000366475.3; NM_015104.3; NP_055919.2.
DR UCSC; uc001obx.4; human. [Q2TAZ0-1]
DR CTD; 23130; -.
DR DisGeNET; 23130; -.
DR GeneCards; ATG2A; -.
DR HGNC; HGNC:29028; ATG2A.
DR HPA; ENSG00000110046; Low tissue specificity.
DR MIM; 616225; gene.
DR neXtProt; NX_Q2TAZ0; -.
DR OpenTargets; ENSG00000110046; -.
DR PharmGKB; PA162377101; -.
DR VEuPathDB; HostDB:ENSG00000110046; -.
DR eggNOG; KOG2993; Eukaryota.
DR GeneTree; ENSGT00620000087966; -.
DR HOGENOM; CLU_001781_0_0_1; -.
DR InParanoid; Q2TAZ0; -.
DR OMA; LQYVMSA; -.
DR OrthoDB; 196897at2759; -.
DR PhylomeDB; Q2TAZ0; -.
DR TreeFam; TF313482; -.
DR PathwayCommons; Q2TAZ0; -.
DR SignaLink; Q2TAZ0; -.
DR SIGNOR; Q2TAZ0; -.
DR BioGRID-ORCS; 23130; 40 hits in 1086 CRISPR screens.
DR ChiTaRS; ATG2A; human.
DR GenomeRNAi; 23130; -.
DR Pharos; Q2TAZ0; Tbio.
DR PRO; PR:Q2TAZ0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q2TAZ0; protein.
DR Bgee; ENSG00000110046; Expressed in right lobe of liver and 190 other tissues.
DR ExpressionAtlas; Q2TAZ0; baseline and differential.
DR Genevisible; Q2TAZ0; HS.
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; IDA: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; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IMP: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; IDA:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR DisProt; DP02142; -.
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 3D-structure; Alternative splicing; Autophagy; Endoplasmic reticulum;
KW Lipid droplet; Lipid transport; Membrane; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..1938
FT /note="Autophagy-related protein 2 homolog A"
FT /id="PRO_0000315234"
FT DOMAIN 14..111
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT REGION 1242..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1404
FT /note="WIPI-interacting"
FT /evidence="ECO:0000269|PubMed:32483132"
FT REGION 1438..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1614..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1359
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4T0"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4T0"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4T0"
FT MOD_RES 1266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4T0"
FT MOD_RES 1301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1607
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030510"
FT VAR_SEQ 58..121
FT /note="SVNEVLESMESPLELVEGFVGSIEVAVPWAALLTDHCTVRVSGLQLTLQPRR
FT GPAPGAADSQSW -> VRSQARVQEVCERGAGVNGVTAGAGGRLRGLHRGGRALGCSAH
FT RPLHSARVRPPAHLAAPPGSR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030511"
FT VAR_SEQ 122..1938
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030512"
FT VAR_SEQ 1259
FT /note="K -> KVQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030515"
FT VAR_SEQ 1608..1724
FT /note="INPVVPGETSAEARPETRAQPSSPLEGQAEGVETTGSQEAPGGGHSPSPPDQ
FT QPIYFREFRFTSEVPIWLDYHGKHVTMDQVGTFAGLLIGLAQLNCSELKLKRLCCRHGL
FT LGVDKV -> MAVAMVKLCERAGLPLLAAPLLRSLLPRAPQPGPAQPRSVQGQRCPARH
FT PPGNLVCERGAGVNGVTAGAGGRLRGLHRGGRALGCSAHRPLHSARVRPPAHLAAPPGS
FT SARGCRLTE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030516"
FT VARIANT 175
FT /note="V -> I (in dbSNP:rs12293826)"
FT /id="VAR_038158"
FT VARIANT 394
FT /note="R -> C (in dbSNP:rs35115827)"
FT /id="VAR_061027"
FT VARIANT 404
FT /note="A -> V (in dbSNP:rs60711419)"
FT /id="VAR_061028"
FT VARIANT 627
FT /note="A -> V (in dbSNP:rs2285347)"
FT /id="VAR_038159"
FT VARIANT 656
FT /note="P -> R (in dbSNP:rs656195)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9455477"
FT /id="VAR_061029"
FT VARIANT 948
FT /note="G -> R (in dbSNP:rs11827140)"
FT /id="VAR_038160"
FT MUTAGEN 54
FT /note="L->R: In Mutant 1; abolished lipid transfer
FT activity; when associated with R-82, E-101, R-167, E-171,
FT R-193, R-200, E-223, R-285, R-304 and R-328."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 80
FT /note="I->E: In Mutant 2; abolished lipid transfer
FT activity; when associated with D-103, K-167, R-171, E-193,
FT K-259, E-285 and R-304."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 82
FT /note="V->R: In Mutant 1; abolished lipid transfer
FT activity; when associated with R-54, E-101, R-167, E-171,
FT R-193, R-200, E-223, R-285, R-304 and R-328."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 101
FT /note="L->E: In Mutant 1; abolished lipid transfer
FT activity; when associated with R-54, R-82, R-167, E-171, R-
FT 193, R-200, E-223, R-285, R-304 and R-328."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 103
FT /note="L->D: In Mutant 2; abolished lipid transfer
FT activity; when associated with E-80,K-167, R-171, E-193, K-
FT 259, E-285 and R-304."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 167
FT /note="I->K: In Mutant 2; abolished lipid transfer
FT activity; when associated with E-80, D-103, R-171, E-193,
FT K-259, E-285 and R-304."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 167
FT /note="I->R: In Mutant 1; abolished lipid transfer
FT activity; when associated with R-54, R-82, E-101, E-171, R-
FT 193, R-200, E-223, R-285, R-304 and R-328."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 171
FT /note="F->E: In Mutant 1; abolished lipid transfer
FT activity; when associated with R-54, R-82, E-101, R-167, R-
FT 193, R-200, E-223, R-285, R-304 and R-328."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 171
FT /note="F->R: In Mutant 2; abolished lipid transfer
FT activity; when associated with E-80, D-103, K-167, E-193,
FT K-259, E-285 and R-304."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 193
FT /note="V->E: In Mutant 2; abolished lipid transfer
FT activity; when associated with E-80, D-103, K-167, R-171,
FT K-259, E-285 and R-304."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 193
FT /note="V->R: In Mutant 1; abolished lipid transfer
FT activity; when associated with R-54, R-82, E-101, R-167, E-
FT 171, R-200, E-223, R-285, R-304 and R-328."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 200
FT /note="Y->R: In Mutant 1; abolished lipid transfer
FT activity; when associated with R-54, R-82, E-101, R-167, E-
FT 171, R-193, E-223, R-285, R-304 and R-328."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 223
FT /note="L->E: In Mutant 1; abolished lipid transfer
FT activity; when associated with R-54, R-82, E-101, R-167, E-
FT 171, R-193, R-200, R-285, R-304 and R-328."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 259
FT /note="M->K: In Mutant 2; abolished lipid transfer
FT activity; when associated with E-80, D-103, K-167, R-171,
FT E-193, E-285 and R-304."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 285
FT /note="L->E: In Mutant 2; abolished lipid transfer
FT activity; when associated with E-80, D-103, K-167, R-171,
FT E-193, K-259 and R-304."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 285
FT /note="L->R: In Mutant 1; abolished lipid transfer
FT activity; when associated with R-54, R-82, E-101, R-167, E-
FT 171, R-193, R-200, E-223, R-304 and R-328."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 304
FT /note="V->R: In Mutant 1; abolished lipid transfer
FT activity; when associated with R-54, R-82, E-101, R-167, E-
FT 171, R-193, R-200, E-223, R-285 and R-328. In Mutant 2;
FT abolished lipid transfer activity; when associated with E-
FT 80, D-103, K-167, R-171, E-193, K-259 and E-285."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 328
FT /note="W->R: In Mutant 1; abolished lipid transfer
FT activity; when associated with R-54, R-82, E-101, R-167, E-
FT 171, R-193, R-200, E-223, R-285 and R-304."
FT /evidence="ECO:0000269|PubMed:30952800"
FT MUTAGEN 1381
FT /note="V->Q: Decreased interaction with WDR45/WIPI4 and
FT ability to promote autophagy."
FT /evidence="ECO:0000269|PubMed:32483132"
FT MUTAGEN 1382
FT /note="T->Q: Decreased interaction with WDR45/WIPI4 and
FT ability to promote autophagy."
FT /evidence="ECO:0000269|PubMed:32483132"
FT MUTAGEN 1389
FT /note="I->Q: Decreased interaction with WDR45/WIPI4 and
FT ability to promote autophagy."
FT /evidence="ECO:0000269|PubMed:32483132"
FT MUTAGEN 1395
FT /note="Y->A: Decreased interaction with WDR45/WIPI4 and
FT ability to promote autophagy."
FT /evidence="ECO:0000269|PubMed:32483132"
FT MUTAGEN 1396
FT /note="F->A: Decreased interaction with WDR45/WIPI4 and
FT ability to promote autophagy."
FT /evidence="ECO:0000269|PubMed:32483132"
FT CONFLICT 1286
FT /note="A -> S (in Ref. 4; AAI10651)"
FT /evidence="ECO:0000305"
FT STRAND 1380..1383
FT /evidence="ECO:0007829|PDB:6KLR"
SQ SEQUENCE 1938 AA; 212860 MW; B0072E075E305A33 CRC64;
MSRWLWPWSN CVKERVCRYL LHHYLGHFFQ EHLSLDQLSL DLYKGSVALR DIHLEIWSVN
EVLESMESPL ELVEGFVGSI EVAVPWAALL TDHCTVRVSG LQLTLQPRRG PAPGAADSQS
WASCMTTSLQ LAQECLRDGL PEPSEPPQPL EGLEMFAQTI ETVLRRIKVT FLDTVVRVEH
SPGDGERGVA VEVRVQRLEY CDEAVRDPSQ APPVDVHQPP AFLHKLLQLA GVRLHYEELP
AQEEPPEPPL QIGSCSGYME LMVKLKQNEA FPGPKLEVAG QLGSLHLLLT PRQLQQLQEL
LSAVSLTDHE GLADKLNKSR PLGAEDLWLI EQDLNQQLQA GAVAEPLSPD PLTNPLLNLD
NTDLFFSMAG LTSSVASALS ELSLSDVDLA SSVRSDMASR RLSAQAHPAG KMAPNPLLDT
MRPDSLLKMT LGGVTLTLLQ TSAPSSGPPD LATHFFTEFD ATKDGPFGSR DFHHLRPRFQ
RACPCSHVRL TGTAVQLSWE LRTGSRGRRT TSMEVHFGQL EVLECLWPRG TSEPEYTEIL
TFPGTLGSQA SARPCAHLRH TQILRRVPKS RPRRSVACHC HSELALDLAN FQADVELGAL
DRLAALLRLA TVPAEPPAGL LTEPLPAMEQ QTVFRLSAPR ATLRLRFPIA DLRPEPDPWA
GQAVRAEQLR LELSEPQFRS ELSSGPGPPV PTHLELTCSD LHGIYEDGGK PPVPCLRVSK
ALDPKSTGRK YFLPQVVVTV NPQSSSTQWE VAPEKGEELE LSVESPCELR EPEPSPFSSK
RTMYETEEMV IPGDPEEMRT FQSRTLALSR CSLEVILPSV HIFLPSKEVY ESIYNRINND
LLMWEPADLL PTPDPAAQPS GFPGPSGFWH DSFKMCKSAF KLANCFDLTP DSDSDDEDAH
FFSVGASGGP QAAAPEAPSL HLQSTFSTLV TVLKGRITAL CETKDEGGKR LEAVHGELVL
DMEHGTLFSV SQYCGQPGLG YFCLEAEKAT LYHRAAVDDY PLPSHLDLPS FAPPAQLAPT
IYPSEEGVTE RGASGRKGQG RGPHMLSTAV RIHLDPHKNV KEFLVTLRLH KATLRHYMAL
PEQSWHSQLL EFLDVLDDPV LGYLPPTVIT ILHTHLFSCS VDYRPLYLPV RVLITAETFT
LSSNIIMDTS TFLLRFILDD SALYLSDKCE VETLDLRRDY VCVLDVDLLE LVIKTWKGST
EGKLSQPLFE LRCSNNVVHV HSCADSCALL VNLLQYVMST GDLHPPPRPP SPTEIAGQKL
SESPASLPSC PPVETALINQ RDLADALLDT ERSLRELAQP SGGHLPQASP ISVYLFPGER
SGAPPPSPPV GGPAGSLGSC SEEKEDEREE EGDGDTLDSD EFCILDAPGL GIPPRDGEPV
VTQLHPGPIV VRDGYFSRPI GSTDLLRAPA HFPVPSTRVV LREVSLVWHL YGGRDFGPHP
GHRARTGLSG PRSSPSRCSG PNRPQNSWRT QGGSGRQHHV LMEIQLSKVS FQHEVYPAEP
ATGPAAPSQE LEERPLSRQV FIVQELEVRD RLASSQINKF LYLHTSERMP RRAHSNMLTI
KALHVAPTTN LGGPECCLRV SLMPLRLNVD QDALFFLKDF FTSLVAGINP VVPGETSAEA
RPETRAQPSS PLEGQAEGVE TTGSQEAPGG GHSPSPPDQQ PIYFREFRFT SEVPIWLDYH
GKHVTMDQVG TFAGLLIGLA QLNCSELKLK RLCCRHGLLG VDKVLGYALN EWLQDIRKNQ
LPGLLGGVGP MHSVVQLFQG FRDLLWLPIE QYRKDGRLMR GLQRGAASFG SSTASAALEL
SNRLVQAIQA TAETVYDILS PAAPVSRSLQ DKRSARRLRR GQQPADLREG VAKAYDTVRE
GILDTAQTIC DVASRGHEQK GLTGAVGGVI RQLPPTVVKP LILATEATSS LLGGMRNQIV
PDAHKDHALK WRSDSAQD
