MLP3A_RAT
ID MLP3A_RAT Reviewed; 121 AA.
AC Q6XVN8;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Microtubule-associated proteins 1A/1B light chain 3A;
DE AltName: Full=Autophagy-related protein LC3 A;
DE AltName: Full=Autophagy-related ubiquitin-like modifier LC3 A;
DE AltName: Full=MAP1 light chain 3-like protein 1;
DE AltName: Full=MAP1A/MAP1B light chain 3 A;
DE Short=MAP1A/MAP1B LC3 A;
DE AltName: Full=Microtubule-associated protein 1 light chain 3 alpha;
DE Flags: Precursor;
GN Name=Map1lc3a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Dang Y., Yu L., Wu J., Pei Y.;
RT "Cloning and characterization of rat lc3 orthologs.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 PROTEIN SEQUENCE OF 31-37, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP CLEAVAGE BY ATG4B.
RX PubMed=16874114; DOI=10.4161/auto.2744;
RA Yoshimura K., Shibata M., Koike M., Gotoh K., Fukaya M., Watanabe M.,
RA Uchiyama Y.;
RT "Effects of RNA interference of Atg4B on the limited proteolysis of LC3 in
RT PC12 cells and expression of Atg4B in various rat tissues.";
RL Autophagy 2:200-208(2006).
RN [5]
RP INTERACTION WITH TP53INP1 AND SQSTM1.
RX PubMed=22421968; DOI=10.1038/cdd.2012.30;
RA Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M.,
RA Carrier A., Iovanna J.L., Dusetti N.J.;
RT "TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins
RT through the LC3-interacting region (LIR) and promotes autophagy-dependent
RT cell death.";
RL Cell Death Differ. 19:1525-1535(2012).
CC -!- FUNCTION: Ubiquitin-like modifier involved in formation of
CC autophagosomal vacuoles (autophagosomes). While LC3s are involved in
CC elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is
CC essential for a later stage in autophagosome maturation. Through its
CC interaction with the reticulophagy receptor TEX264, participates in the
CC remodeling of subdomains of the endoplasmic reticulum into
CC autophagosomes upon nutrient stress, which then fuse with lysosomes for
CC endoplasmic reticulum turnover. {ECO:0000250|UniProtKB:Q9H492}.
CC -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with
CC MAP1A and MAP1B proteins (By similarity). Interacts with TP53INP2 (By
CC similarity). Interacts with TP53INP1 and SQSTM1 (PubMed:22421968).
CC Directly interacts with SQSTM1; this interaction leads to MAP1LC3A
CC recruitment to inclusion bodies containing polyubiquitinated protein
CC aggregates and to inclusion body degradation by autophagy (By
CC similarity). Interacts with ATG13 and ULK1 (By similarity). Interacts
CC with TBC1D5 (By similarity). Found in a complex with UBQLN1 and UBQLN2
CC (By similarity). Interacts with UBQLN4 (via STI1 1 and 2 domains) (By
CC similarity). Interacts with UBQLN1 in the presence of UBQLN4 (By
CC similarity). Interacts with TRIM5 (By similarity). Interacts with MEFV.
CC Interacts with RETREG1, RETREG2 and RETREG3 (By similarity). Interacts
CC with PICALM (By similarity). Interacts with the reticulophagy receptor
CC TEX264 (By similarity). Interacts with MOAP1 (via LIR motif) (By
CC similarity). {ECO:0000250|UniProtKB:Q62625,
CC ECO:0000250|UniProtKB:Q9H492, ECO:0000269|PubMed:22421968}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:Q9H492}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9H492}. Cytoplasmic vesicle, autophagosome
CC membrane {ECO:0000250|UniProtKB:Q9H492}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9H492}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000250|UniProtKB:Q9H492}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q91VR7}. Note=LC3-II binds to the autophagic
CC membranes. {ECO:0000250|UniProtKB:Q9H492}.
CC -!- PTM: The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or
CC ATG4D) to expose the glycine at the C-terminus and form the cytosolic
CC form, LC3-I (PubMed:16874114). The processed form is then activated by
CC APG7L/ATG7, transferred to ATG3 and conjugated to
CC phosphatidylethanolamine (PE) phospholipid to form the membrane-bound
CC form, LC3-II. During non-canonical autophagy, the processed form is
CC conjugated to phosphatidylserine (PS) phospholipid. ATG4 proteins also
CC mediate the delipidation of PE-conjugated forms. In addition, ATG4B and
CC ATG4D mediate delipidation of ATG8 proteins conjugated to PS during
CC non-canonical autophagy. ATG4B constitutes the major protein for
CC proteolytic activation (By similarity). ATG4D is the main enzyme for
CC delipidation activity (By similarity). {ECO:0000250|UniProtKB:Q91VR7,
CC ECO:0000250|UniProtKB:Q9H492, ECO:0000269|PubMed:16874114}.
CC -!- PTM: Phosphorylation at Ser-12 by PKA inhibits conjugation to
CC phosphatidylethanolamine (PE). {ECO:0000250|UniProtKB:Q9H492}.
CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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DR EMBL; AY206668; AAP42560.1; -; mRNA.
DR EMBL; BC086389; AAH86389.1; -; mRNA.
DR RefSeq; NP_955794.1; NM_199500.2.
DR AlphaFoldDB; Q6XVN8; -.
DR SMR; Q6XVN8; -.
DR BioGRID; 263296; 1.
DR IntAct; Q6XVN8; 5.
DR MINT; Q6XVN8; -.
DR STRING; 10116.ENSRNOP00000032429; -.
DR iPTMnet; Q6XVN8; -.
DR PhosphoSitePlus; Q6XVN8; -.
DR SwissPalm; Q6XVN8; -.
DR jPOST; Q6XVN8; -.
DR PaxDb; Q6XVN8; -.
DR PRIDE; Q6XVN8; -.
DR Ensembl; ENSRNOT00000035060; ENSRNOP00000032429; ENSRNOG00000025443.
DR GeneID; 362245; -.
DR KEGG; rno:362245; -.
DR UCSC; RGD:735183; rat.
DR CTD; 84557; -.
DR RGD; 735183; Map1lc3a.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000158853; -.
DR HOGENOM; CLU_119276_1_0_1; -.
DR InParanoid; Q6XVN8; -.
DR OMA; VNERSMV; -.
DR OrthoDB; 1508198at2759; -.
DR PhylomeDB; Q6XVN8; -.
DR TreeFam; TF312964; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-RNO-8934903; Receptor Mediated Mitophagy.
DR PRO; PR:Q6XVN8; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000025443; Expressed in heart and 19 other tissues.
DR Genevisible; Q6XVN8; RN.
DR GO; GO:0044754; C:autolysosome; ISO:RGD.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005770; C:late endosome; IDA:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031090; C:organelle membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0000045; P:autophagosome assembly; IDA:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; ISO:RGD.
DR GO; GO:0006914; P:autophagy; IDA:RGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISO:RGD.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IEP:RGD.
DR GO; GO:0071280; P:cellular response to copper ion; IEP:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; ISO:RGD.
DR GO; GO:0016236; P:macroautophagy; ISO:RGD.
DR GO; GO:0010040; P:response to iron(II) ion; IEP:RGD.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR GO; GO:0043278; P:response to morphine; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR InterPro; IPR004241; Atg8-like.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10969; PTHR10969; 1.
DR Pfam; PF02991; ATG8; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Lipoprotein; Membrane; Microtubule;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..120
FT /note="Microtubule-associated proteins 1A/1B light chain
FT 3A"
FT /id="PRO_0000017196"
FT PROPEP 121
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000017197"
FT REGION 49..53
FT /note="Important for interaction with ATG13 and for
FT autophagosome formation"
FT /evidence="ECO:0000250|UniProtKB:Q9H492"
FT SITE 120..121
FT /note="Cleavage; by ATG4B"
FT /evidence="ECO:0000250|UniProtKB:Q9H492"
FT MOD_RES 12
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9H492"
FT LIPID 120
FT /note="Phosphatidylethanolamine amidated glycine;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H492"
FT LIPID 120
FT /note="Phosphatidylserine amidated glycine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9H492"
SQ SEQUENCE 121 AA; 14272 MW; 48C1FBE8F7892AF3 CRC64;
MPSDRPFKQR RSFADRCKEV QQIRDQHPSK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM
SELVKIIRRR LQLNPTQAFF LLVNQHSMVS VSTPIADIYE QEKDEDGFLY MVYASQETFG
F
