ID MLP3B_RAT Reviewed; 142 AA. AC Q62625; Q6XVN7; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 179. DE RecName: Full=Microtubule-associated proteins 1A/1B light chain 3B {ECO:0000305}; DE AltName: Full=Autophagy-related protein LC3 B; DE AltName: Full=Autophagy-related ubiquitin-like modifier LC3 B; DE AltName: Full=MAP1 light chain 3-like protein 2; DE AltName: Full=MAP1A/MAP1B light chain 3 B; DE Short=MAP1A/MAP1B LC3 B; DE AltName: Full=Microtubule-associated protein 1 light chain 3 beta; DE Flags: Precursor; GN Name=Map1lc3b {ECO:0000312|RGD:621315}; Synonyms=Map1alc3, Map1lc3; 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] (ISOFORM 1), SUBUNIT, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=7908909; DOI=10.1016/s0021-9258(19)78150-2; RA Mann S.S., Hammarback J.A.; RT "Molecular characterization of light chain 3. A microtubule binding subunit RT of MAP1A and MAP1B."; RL J. Biol. Chem. 269:11492-11497(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=Sprague-Dawley; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=Sprague-Dawley; RA Zhou G., Dai F., Yu L.; RT "Rattus norvegicus microtubule-associated protein 1 light chain 3 RT (Map1lc3)."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Heart, and Pituitary; 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 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 [6] RP SUBCELLULAR LOCATION, CLEAVAGE, AND MUTAGENESIS OF GLY-120. RX PubMed=11060023; DOI=10.1093/emboj/19.21.5720; RA Kabeya Y., Mizushima N., Ueno T., Yamamoto A., Kirisako T., Noda T., RA Kominami E., Ohsumi Y., Yoshimori T.; RT "LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome RT membranes after processing."; RL EMBO J. 19:5720-5728(2000). RN [7] RP REVIEW. RX PubMed=15325588; DOI=10.1016/j.biocel.2004.05.009; RA Tanida I., Ueno T., Kominami E.; RT "LC3 conjugation system in mammalian autophagy."; RL Int. J. Biochem. Cell Biol. 36:2503-2518(2004). RN [8] RP INTERACTION WITH CABP1. RX PubMed=15095872; DOI=10.1016/j.jmb.2003.12.054; RA Seidenbecher C.I., Landwehr M., Smalla K.H., Kreutz M., Dieterich D.C., RA Zuschratter W., Reissner C., Hammarback J.A., Bockers T.M., RA Gundelfinger E.D., Kreutz M.R.; RT "Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an RT association with the microtubule cytoskeleton highlighting exclusive RT binding partners for neuronal Ca(2+)-sensor proteins."; RL J. Mol. Biol. 336:957-970(2004). RN [9] RP CLEAVAGE BY ATG4B, AND MUTAGENESIS OF GLN-116; PHE-119 AND GLY-120. RX PubMed=16183633; DOI=10.1074/jbc.m509158200; RA Sugawara K., Suzuki N.N., Fujioka Y., Mizushima N., Ohsumi Y., Inagaki F.; RT "Structural basis for the specificity and catalysis of human Atg4B RT responsible for mammalian autophagy."; RL J. Biol. Chem. 280:40058-40065(2005). RN [10] 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 [11] RP INTERACTION WITH PLCL1. RX PubMed=23399561; DOI=10.1016/j.bbrc.2013.01.119; RA Umebayashi H., Mizokami A., Matsuda M., Harada K., Takeuchi H., Tanida I., RA Hirata M., Kanematsu T.; RT "Phospholipase C-related catalytically inactive protein, a novel RT microtubule-associated protein 1 light chain 3-binding protein, negatively RT regulates autophagosome formation."; RL Biochem. Biophys. Res. Commun. 432:268-274(2013). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-120. RX PubMed=15265004; DOI=10.1111/j.1356-9597.2004.00750.x; RA Sugawara K., Suzuki N.N., Fujioka Y., Mizushima N., Ohsumi Y., Inagaki F.; RT "The crystal structure of microtubule-associated protein light chain 3, a RT mammalian homologue of Saccharomyces cerevisiae Atg8."; RL Genes Cells 9:611-618(2004). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-124 IN COMPLEX WITH ATG4B. RX PubMed=19322194; DOI=10.1038/emboj.2009.80; RA Satoo K., Noda N.N., Kumeta H., Fujioka Y., Mizushima N., Ohsumi Y., RA Inagaki F.; RT "The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing RT and delipidation during autophagy."; RL EMBO J. 28:1341-1350(2009). CC -!- FUNCTION: Ubiquitin-like modifier involved in formation of CC autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy CC which contributes to regulate mitochondrial quantity and quality by CC eliminating the mitochondria to a basal level to fulfill cellular CC energy requirements and preventing excess ROS production. In response CC to cellular stress and upon mitochondria fission, binds C-18 ceramides CC and anchors autophagolysosomes to outer mitochondrial membranes to CC eliminate damaged mitochondria. While LC3s are involved in elongation CC of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential CC for a later stage in autophagosome maturation. Promotes primary CC ciliogenesis by removing OFD1 from centriolar satellites via the CC autophagic pathway. Through its interaction with the reticulophagy CC receptor TEX264, participates in the remodeling of subdomains of the CC endoplasmic reticulum into autophagosomes upon nutrient stress, which CC then fuse with lysosomes for endoplasmic reticulum turnover. Upon CC nutrient stress, directly recruits cofactor JMY to the phagophore CC membrane surfaces and promotes JMY's actin nucleation activity and CC autophagosome biogenesis during autophagy. CC {ECO:0000250|UniProtKB:Q9GZQ8}. CC -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with CC MAP1A and MAP1B proteins (PubMed:7908909). Interacts at microtubules CC with CABP1 (via EF-hands 1 and 2) but not with calmodulin CC (PubMed:15095872). Interacts with FYCO1 (via C-terminus). Interacts CC with TP53INP1 and TP53INP2. Interacts with TBC1D25. Directly interacts CC with SQSTM1; this interaction leads to MAP1LC3B recruitment to CC inclusion bodies containing polyubiquitinated protein aggregates and to CC inclusion body degradation by autophagy (By similarity). Interacts with CC ATG4B (PubMed:19322194). Interacts with MAPK15 and BNIP3. Interacts CC with MAPB1, KEAP1, PCM1, OFD1, CEP131, and TECPR2. Interacts with CC TBC1D5. Found in a complex with UBQLN1 and UBQLN2. Interacts with CC UBQLN4 (via STI1 1 and 2 domains). Interacts with UBQLN1 in the CC presence of UBQLN4. Interacts with ATG13. Interacts with reticulophagy CC regulators RETREG1, RETREG2 and RETREG3 (By similarity). Interacts with CC PLCL1; the interaction inhibits autophagosome formation CC (PubMed:23399561). Interacts with TRIM16 (By similarity). Interacts CC with CRY1 and PER2 (By similarity). Interacts with the reticulophagy CC receptor TEX264 (By similarity). Membrane-bound form LC3-II interacts CC with PHB1 and PHB2; the interaction takes place upon Parkin-mediated CC mitochondrial damage (By similarity). Interacts with PJVK; the CC interaction is direct (By similarity). Interacts with KBTBD6 and CC KBTBD7; the interaction is direct (By similarity). Interacts with CC AMBRA1 (via LIR motif) (By similarity). Interacts with JMY; the CC interaction results in the activation of JYM's nucleation activity in CC the cytoplasm (By similarity). Interacts with MOAP1 (via LIR motif) (By CC similarity). Interacts with TAX1BP1 (By similarity). Interacts with CC IRGM (By similarity). Interacts with STX17 (By similarity). Interacts CC (the lipidate and non-lipidated LC3 form) with DNM2; this interaction CC mediates recycling endosome scission leading to autophagosome release CC (By similarity). {ECO:0000250|UniProtKB:Q9CQV6, CC ECO:0000250|UniProtKB:Q9GZQ8, ECO:0000269|PubMed:15095872, CC ECO:0000269|PubMed:19322194, ECO:0000269|PubMed:23399561, CC ECO:0000269|PubMed:7908909}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane CC {ECO:0000269|PubMed:11060023}; Lipid-anchor CC {ECO:0000269|PubMed:11060023}. Endomembrane system CC {ECO:0000269|PubMed:11060023}; Lipid-anchor CC {ECO:0000269|PubMed:11060023}. Mitochondrion membrane CC {ECO:0000250|UniProtKB:Q9GZQ8}; Lipid-anchor CC {ECO:0000250|UniProtKB:Q9GZQ8}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:11060023}. Cytoplasmic vesicle CC {ECO:0000250|UniProtKB:Q9GZQ8}. Note=LC3-II binds to the autophagic CC membranes. LC3-II localizes with the mitochondrial inner membrane CC during Parkin-mediated mitophagy (By similarity). Localizes also to CC discrete punctae along the ciliary axoneme (By similarity). CC {ECO:0000250|UniProtKB:Q9GZQ8}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q62625-1; Sequence=Displayed; CC Name=2; CC IsoId=Q62625-2; Sequence=VSP_012092; CC -!- TISSUE SPECIFICITY: Abundant only in neurons. Detected in testes. CC {ECO:0000269|PubMed:7908909}. 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:11060023, PubMed:16183633, PubMed:16874114). The CC processed form is then activated by APG7L/ATG7, transferred to ATG3 and CC conjugated to phosphatidylethanolamine (PE) phospholipid to form the CC membrane-bound form, LC3-II. During non-canonical autophagy, the CC processed form is conjugated to phosphatidylserine (PS) phospholipid. CC ATG4 proteins also mediate the delipidation of PE-conjugated forms. In CC addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins CC conjugated to PS during non-canonical autophagy. ATG4B constitutes the CC major protein for proteolytic activation (By similarity). ATG4D is the CC main enzyme for delipidation activity (By similarity). CC {ECO:0000250|UniProtKB:Q9CQV6, ECO:0000250|UniProtKB:Q9GZQ8, CC ECO:0000269|PubMed:11060023, ECO:0000269|PubMed:16183633, CC ECO:0000269|PubMed:16874114}. CC -!- PTM: Phosphorylation by PKA inhibits conjugation of CC phosphatidylethanolamine (PE). Interaction with MAPK15 reduces the CC inhibitory phosphorylation and increases autophagy activity. CC {ECO:0000250|UniProtKB:Q9GZQ8}. CC -!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U05784; AAA20645.1; -; mRNA. DR EMBL; AY206669; AAP42561.1; -; mRNA. DR EMBL; AY392036; AAQ94605.1; -; mRNA. DR EMBL; BC058144; AAH58144.1; -; mRNA. DR EMBL; BC083556; AAH83556.1; -; mRNA. DR PIR; A53624; A53624. DR RefSeq; NP_074058.2; NM_022867.2. [Q62625-2] DR RefSeq; XP_017456840.1; XM_017601351.1. [Q62625-1] DR PDB; 1UGM; X-ray; 2.05 A; A=1-120. DR PDB; 2K6Q; NMR; -; A=1-120. DR PDB; 2Z0D; X-ray; 1.90 A; B=1-120. DR PDB; 2Z0E; X-ray; 1.90 A; B=1-124. DR PDB; 2ZZP; X-ray; 2.05 A; B=1-124. DR PDBsum; 1UGM; -. DR PDBsum; 2K6Q; -. DR PDBsum; 2Z0D; -. DR PDBsum; 2Z0E; -. DR PDBsum; 2ZZP; -. DR AlphaFoldDB; Q62625; -. DR BMRB; Q62625; -. DR SMR; Q62625; -. DR BioGRID; 249213; 5. DR ELM; Q62625; -. DR IntAct; Q62625; 8. DR MINT; Q62625; -. DR STRING; 10116.ENSRNOP00000075089; -. DR PhosphoSitePlus; Q62625; -. DR jPOST; Q62625; -. DR PaxDb; 10116-ENSRNOP00000049421; -. DR Ensembl; ENSRNOT00055035566; ENSRNOP00055028846; ENSRNOG00055020808. [Q62625-1] DR Ensembl; ENSRNOT00065001486; ENSRNOP00065001041; ENSRNOG00065001119. [Q62625-1] DR GeneID; 64862; -. DR KEGG; rno:64862; -. DR UCSC; RGD:621315; rat. [Q62625-1] DR AGR; RGD:621315; -. DR CTD; 81631; -. DR RGD; 621315; Map1lc3b. DR VEuPathDB; HostDB:ENSRNOG00000017905; -. DR eggNOG; KOG1654; Eukaryota. DR HOGENOM; CLU_119276_1_0_1; -. DR InParanoid; Q62625; -. DR OrthoDB; 652940at2759; -. DR Reactome; R-RNO-1632852; Macroautophagy. DR Reactome; R-RNO-5205685; PINK1-PRKN Mediated Mitophagy. DR Reactome; R-RNO-8854214; TBC/RABGAPs. DR Reactome; R-RNO-8934903; Receptor Mediated Mitophagy. DR Reactome; R-RNO-9664873; Pexophagy. DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway. DR EvolutionaryTrace; Q62625; -. DR PRO; PR:Q62625; -. DR Proteomes; UP000002494; Chromosome 19. DR Bgee; ENSRNOG00000017905; Expressed in cerebellum and 20 other cell types or tissues. DR ExpressionAtlas; Q62625; baseline and differential. DR GO; GO:0044754; C:autolysosome; ISO:RGD. DR GO; GO:0005776; C:autophagosome; ISO:RGD. DR GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB. DR GO; GO:0030424; C:axon; IDA:RGD. DR GO; GO:0005930; C:axoneme; ISO:RGD. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0030425; C:dendrite; IDA:RGD. DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005875; C:microtubule associated complex; IDA:RGD. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; ISO:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0097001; F:ceramide binding; ISO:RGD. DR GO; GO:0008017; F:microtubule binding; IDA:RGD. DR GO; GO:0008429; F:phosphatidylethanolamine binding; ISO:RGD. DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD. DR GO; GO:0015631; F:tubulin binding; IDA:RGD. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD. DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central. DR GO; GO:0097352; P:autophagosome maturation; ISO:RGD. DR GO; GO:0006914; P:autophagy; ISO:RGD. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central. DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB. DR GO; GO:0051649; P:establishment of localization in cell; ISO:RGD. DR GO; GO:0016236; P:macroautophagy; ISO:RGD. DR GO; GO:0000423; P:mitophagy; ISS:UniProtKB. DR GO; GO:0070254; P:mucus secretion; ISO:RGD. DR GO; GO:0070257; P:positive regulation of mucus secretion; ISO:RGD. DR CDD; cd17235; Ubl_ATG8_MAP1LC3B; 1. DR IDEAL; IID50112; -. DR InterPro; IPR004241; Atg8-like. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10969; MICROTUBULE-ASSOCIATED PROTEINS 1A/1B LIGHT CHAIN 3-RELATED; 1. DR PANTHER; PTHR10969:SF15; MICROTUBULE-ASSOCIATED PROTEINS 1A_1B LIGHT CHAIN 3 BETA 2-RELATED; 1. DR Pfam; PF02991; ATG8; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR Genevisible; Q62625; RN. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Autophagy; Cytoplasm; KW Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing; Lipoprotein; KW Membrane; Microtubule; Mitochondrion; Phosphoprotein; Reference proteome; KW Ubl conjugation pathway. FT CHAIN 1..120 FT /note="Microtubule-associated proteins 1A/1B light chain FT 3B" FT /id="PRO_0000017202" FT PROPEP 121..142 FT /note="Removed in mature form" FT /id="PRO_0000017203" FT SITE 120..121 FT /note="Cleavage; by ATG4B" FT /evidence="ECO:0000269|PubMed:11060023, FT ECO:0000269|PubMed:16183633" FT LIPID 120 FT /note="Phosphatidylethanolamine amidated glycine; FT alternate" FT /evidence="ECO:0000250|UniProtKB:Q9GZQ8" FT LIPID 120 FT /note="Phosphatidylserine amidated glycine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9GZQ8" FT VAR_SEQ 126..142 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2, FT ECO:0000303|Ref.3" FT /id="VSP_012092" FT MUTAGEN 116 FT /note="Q->A: No processing of precursor." FT /evidence="ECO:0000269|PubMed:16183633" FT MUTAGEN 119 FT /note="F->A: No processing of precursor." FT /evidence="ECO:0000269|PubMed:16183633" FT MUTAGEN 120 FT /note="G->A: No processing of precursor." FT /evidence="ECO:0000269|PubMed:11060023, FT ECO:0000269|PubMed:16183633" FT HELIX 7..10 FT /evidence="ECO:0007829|PDB:2Z0D" FT HELIX 13..26 FT /evidence="ECO:0007829|PDB:2Z0D" FT STRAND 30..37 FT /evidence="ECO:0007829|PDB:2Z0D" FT STRAND 51..55 FT /evidence="ECO:0007829|PDB:2Z0D" FT HELIX 60..70 FT /evidence="ECO:0007829|PDB:2Z0D" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:2K6Q" FT STRAND 80..83 FT /evidence="ECO:0007829|PDB:2Z0D" FT STRAND 91..94 FT /evidence="ECO:0007829|PDB:1UGM" FT HELIX 95..102 FT /evidence="ECO:0007829|PDB:2Z0D" FT STRAND 109..114 FT /evidence="ECO:0007829|PDB:2Z0D" SQ SEQUENCE 142 AA; 16394 MW; D07E9D063C125E32 CRC64; MPSEKTFKQR RSFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SERDEDGFLY MVYASQETFG TALAVTYMSA LKATATGREP CL //