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Microtubule-associated proteins 1A/1B light chain 3A (Autophagy-related protein LC3 A) (Autophagy-related ubiquitin-like modifier LC3 A) (MAP1 light chain 3-like protein 1) (MAP1A/MAP1B light chain 3 A) (MAP1A/MAP1B LC3 A) (Microtubule-associated protein 1 light chain 3 alpha)

 MLP3A_MOUSE             Reviewed;         121 AA.
Q91VR7; A2AVS1; Q9DC74;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
12-SEP-2018, entry version 134.
RecName: Full=Microtubule-associated proteins 1A/1B light chain 3A;
AltName: Full=Autophagy-related protein LC3 A;
AltName: Full=Autophagy-related ubiquitin-like modifier LC3 A;
AltName: Full=MAP1 light chain 3-like protein 1;
AltName: Full=MAP1A/MAP1B light chain 3 A;
Short=MAP1A/MAP1B LC3 A;
AltName: Full=Microtubule-associated protein 1 light chain 3 alpha;
Flags: Precursor;
Name=Map1lc3a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Heart;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION.
PubMed=11266458; DOI=10.1083/jcb.152.4.657;
Mizushima N., Yamamoto A., Hatano M., Kobayashi Y., Kabeya Y.,
Suzuki K., Tokuhisa T., Ohsumi Y., Yoshimori T.;
"Dissection of autophagosome formation using Apg5-deficient mouse
embryonic stem cells.";
J. Cell Biol. 152:657-668(2001).
[5]
SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
PubMed=12207896; DOI=10.1016/S0006-291X(02)02057-0;
Tanida I., Nishitani T., Nemoto T., Ueno T., Kominami E.;
"Mammalian Apg12p, but not the Apg12p.Apg5p conjugate, facilitates LC3
processing.";
Biochem. Biophys. Res. Commun. 296:1164-1170(2002).
[6]
CLEAVAGE BY ATG4B, AND SUBCELLULAR LOCATION.
PubMed=14530254; DOI=10.1074/jbc.M308762200;
Hemelaar J., Lelyveld V.S., Kessler B.M., Ploegh H.L.;
"A single protease, Apg4B, is specific for the autophagy-related
ubiquitin-like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L.";
J. Biol. Chem. 278:51841-51850(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Ubiquitin-like modifier involved in formation of
autophagosomal vacuoles (autophagosomes). Whereas LC3s are
involved in elongation of the phagophore membrane, the
GABARAP/GATE-16 subfamily is essential for a later stage in
autophagosome maturation. {ECO:0000250|UniProtKB:Q9H492}.
-!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate
with MAP1A and MAP1B proteins (By similarity). Interacts with
TP53INP1 and TP53INP2. Directly interacts with SQSTM1; this
interaction leads to MAP1LC3A recruitment to inclusion bodies
containing polyubiquitinated protein aggregates and to inclusion
body degradation by autophagy. Interacts with ATG13. Interacts
with ULK1. Interacts with TBC1D5. Found in a complex with UBQLN1
and UBQLN2. Interacts with UBQLN4 (via STI1 1 and 2 domains).
Interacts with UBQLN1 in the presence of UBQLN4. Interacts with
TRIM5. Interacts with MEFV. Interacts with RETREG1, RETREG2 and
RETREG3 (By similarity). {ECO:0000250|UniProtKB:Q9H492}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Endomembrane
system; Lipid-anchor. Cytoplasmic vesicle, autophagosome membrane
{ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasmic vesicle,
autophagosome {ECO:0000250|UniProtKB:Q9H492}. Note=LC3-II binds to
the autophagic membranes. {ECO:0000250}.
-!- PTM: The precursor molecule is cleaved by ATG4B to form the
cytosolic form, LC3-I. This is activated by APG7L/ATG7,
transferred to ATG3 and conjugated to phospholipid to form the
membrane-bound form, LC3-II. {ECO:0000269|PubMed:12207896,
ECO:0000269|PubMed:14530254}.
-!- PTM: Phosphorylation at Ser-12 by PKA inhibits conjugation to
phosphatidylethanolamine (PE). Interaction with MAPK15 reduces the
inhibitory phosphorylation and increases autophagy activity.
{ECO:0000250|UniProtKB:Q9H492}.
-!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AK003122; BAB22582.1; -; mRNA.
EMBL; AL929588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010596; AAH10596.1; -; mRNA.
CCDS; CCDS16945.1; -.
RefSeq; NP_080011.1; NM_025735.3.
UniGene; Mm.196239; -.
ProteinModelPortal; Q91VR7; -.
SMR; Q91VR7; -.
BioGrid; 211680; 13.
IntAct; Q91VR7; 4.
MINT; Q91VR7; -.
STRING; 10090.ENSMUSP00000029128; -.
iPTMnet; Q91VR7; -.
PhosphoSitePlus; Q91VR7; -.
MaxQB; Q91VR7; -.
PaxDb; Q91VR7; -.
PeptideAtlas; Q91VR7; -.
PRIDE; Q91VR7; -.
Ensembl; ENSMUST00000029128; ENSMUSP00000029128; ENSMUSG00000027602.
GeneID; 66734; -.
KEGG; mmu:66734; -.
UCSC; uc012cha.2; mouse.
CTD; 84557; -.
MGI; MGI:1915661; Map1lc3a.
eggNOG; KOG1654; Eukaryota.
eggNOG; ENOG4111JAT; LUCA.
GeneTree; ENSGT00390000012937; -.
HOGENOM; HOG000232034; -.
HOVERGEN; HBG051706; -.
InParanoid; Q91VR7; -.
KO; K10435; -.
OMA; RTFADRC; -.
OrthoDB; EOG091G18ST; -.
PhylomeDB; Q91VR7; -.
TreeFam; TF312964; -.
Reactome; R-MMU-1632852; Macroautophagy.
Reactome; R-MMU-5205685; Pink/Parkin Mediated Mitophagy.
Reactome; R-MMU-8934903; Receptor Mediated Mitophagy.
ChiTaRS; Map1lc3a; mouse.
PRO; PR:Q91VR7; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027602; Expressed in 295 organ(s), highest expression level in ear.
Genevisible; Q91VR7; MM.
GO; GO:0044754; C:autolysosome; ISO:MGI.
GO; GO:0005776; C:autophagosome; IDA:MGI.
GO; GO:0000421; C:autophagosome membrane; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005770; C:late endosome; ISO:MGI.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
GO; GO:0031090; C:organelle membrane; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; ISO:MGI.
GO; GO:0008429; F:phosphatidylethanolamine binding; ISO:MGI.
GO; GO:0005543; F:phospholipid binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
GO; GO:0097352; P:autophagosome maturation; ISO:MGI.
GO; GO:0006914; P:autophagy; ISO:MGI.
GO; GO:0000422; P:autophagy of mitochondrion; ISO:MGI.
GO; GO:0034198; P:cellular response to amino acid starvation; IEA:Ensembl.
GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
GO; GO:0016236; P:macroautophagy; ISO:MGI.
GO; GO:0010040; P:response to iron(II) ion; IEA:Ensembl.
GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
CDD; cd01611; GABARAP; 1.
InterPro; IPR004241; Atg8-like.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR10969; PTHR10969; 1.
Pfam; PF02991; Atg8; 1.
SUPFAM; SSF54236; SSF54236; 1.
1: Evidence at protein level;
Autophagy; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Cytoskeleton; Lipoprotein; Membrane; Microtubule; Phosphoprotein;
Reference proteome; Ubl conjugation pathway.
CHAIN 1 120 Microtubule-associated proteins 1A/1B
light chain 3A.
/FTId=PRO_0000017194.
PROPEP 121 121 Removed in mature form. {ECO:0000305}.
/FTId=PRO_0000017195.
REGION 49 53 Important for interaction with ATG13 and
for autophagosome formation.
{ECO:0000250|UniProtKB:Q9H492}.
SITE 120 121 Cleavage; by ATG4B. {ECO:0000250}.
MOD_RES 12 12 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q9H492}.
LIPID 120 120 Phosphatidylethanolamine amidated
glycine. {ECO:0000250|UniProtKB:Q9H492}.
CONFLICT 12 12 S -> T (in Ref. 1; BAB22582).
{ECO:0000305}.
SEQUENCE 121 AA; 14272 MW; 48C1FBE8F7892AF3 CRC64;
MPSDRPFKQR RSFADRCKEV QQIRDQHPSK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM
SELVKIIRRR LQLNPTQAFF LLVNQHSMVS VSTPIADIYE QEKDEDGFLY MVYASQETFG
F


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