MLP3B_BOVIN
ID MLP3B_BOVIN Reviewed; 125 AA.
AC O41515; Q6PZ01;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Microtubule-associated proteins 1A/1B light chain 3B;
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; Synonyms=MAP1ALC3, MAP1LC3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15140988; DOI=10.1128/jvi.78.11.5900-5912.2004;
RA Fricke J., Voss C., Thumm M., Meyers G.;
RT "Processing of a pestivirus protein by a cellular protease specific for
RT light chain 3 of microtubule-associated proteins.";
RL J. Virol. 78:5900-5912(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-21.
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 6-120.
RX PubMed=9557703; DOI=10.1128/jvi.72.5.4139-4148.1998;
RA Meyers G., Stoll D., Gunn M.;
RT "Insertion of a sequence encoding light chain 3 of microtubule-associated
RT proteins 1A and 1B in a pestivirus genome: connection with virus
RT cytopathogenicity and induction of lethal disease in cattle.";
RL J. Virol. 72:4139-4148(1998).
RN [5]
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).
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 (By similarity). Interacts at microtubules
CC with CABP1 (via EF-hands 1 and 2) but not with calmodulin. Interacts
CC with FYCO1 (via C-terminus). Interacts with TP53INP1 and TP53INP2 (By
CC similarity). Interacts with TBC1D25 (By similarity). 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. Interacts with ATG4B, MAPK15
CC and BNIP3. Interacts with MAPB1, KEAP1, PCM1, OFD1, CEP131, and TECPR2.
CC Interacts with TBC1D5. Found in a complex with UBQLN1 and UBQLN2.
CC Interacts with UBQLN4 (via STI1 1 and 2 domains). Interacts with UBQLN1
CC in the presence of UBQLN4. Interacts with ATG13. Interacts with
CC RETREG1, RETREG2 and RETREG3 (By similarity). Interacts with PLCL1; the
CC interaction inhibits autophagosome formation. Interacts with TRIM16.
CC Interacts with CRY1 and PER2 (By similarity). Interacts with the
CC reticulophagy receptor TEX264 (By similarity). Membrane-bound form LC3-
CC II interacts with PHB1 and PHB2; the interaction takes place upon
CC Parkin-mediated mitochondrial damage (By similarity). Interacts with
CC PJVK; the interaction is direct (By similarity). Interacts with KBTBD6
CC and 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). {ECO:0000250|UniProtKB:Q62625,
CC ECO:0000250|UniProtKB:Q9CQV6, ECO:0000250|UniProtKB:Q9GZQ8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:Q9CQV6}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9GZQ8}. Endomembrane system
CC {ECO:0000250|UniProtKB:Q9CQV6}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9GZQ8}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q9GZQ8}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9GZQ8}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9CQV6}. 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 -!- 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. The processed form is then activated by APG7L/ATG7,
CC transferred to ATG3 and conjugated to phosphatidylethanolamine (PE)
CC phospholipid to form the membrane-bound form, LC3-II. During non-
CC canonical autophagy, the processed form is conjugated to
CC phosphatidylserine (PS) phospholipid. ATG4 proteins also mediate the
CC delipidation of PE-conjugated forms. In addition, ATG4B and ATG4D
CC mediate delipidation of ATG8 proteins conjugated to PS during non-
CC 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:Q9CQV6,
CC ECO:0000250|UniProtKB:Q9GZQ8}.
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 -!- CAUTION: PubMed:9557703 sequence originates from strain Jacp of
CC pestivirus type 1 which seems to contain a cellular insertion of part
CC of the bovine host MAP1LC3 gene. {ECO:0000305}.
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DR EMBL; AY570553; AAS78585.1; -; mRNA.
DR EMBL; BC102891; AAI02892.1; -; mRNA.
DR EMBL; U80885; AAB72082.1; ALT_SEQ; Genomic_RNA.
DR RefSeq; NP_001001169.1; NM_001001169.1.
DR AlphaFoldDB; O41515; -.
DR BMRB; O41515; -.
DR SMR; O41515; -.
DR IntAct; O41515; 1.
DR STRING; 9913.ENSBTAP00000015449; -.
DR MEROPS; S31.001; -.
DR PaxDb; O41515; -.
DR PRIDE; O41515; -.
DR Ensembl; ENSBTAT00000015449; ENSBTAP00000015449; ENSBTAG00000011632.
DR GeneID; 408001; -.
DR KEGG; bta:408001; -.
DR CTD; 81631; -.
DR VEuPathDB; HostDB:ENSBTAG00000011632; -.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000154158; -.
DR HOGENOM; CLU_119276_1_0_1; -.
DR InParanoid; O41515; -.
DR OMA; EFSHDER; -.
DR OrthoDB; 1508198at2759; -.
DR TreeFam; TF312964; -.
DR Reactome; R-BTA-1632852; Macroautophagy.
DR Reactome; R-BTA-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-BTA-8854214; TBC/RABGAPs.
DR Reactome; R-BTA-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-BTA-9755511; KEAP1-NFE2L2 pathway.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000011632; Expressed in occipital lobe and 103 other tissues.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031090; C:organelle membrane; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
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:0016236; P:macroautophagy; IBA:GO_Central.
DR GO; GO:0000423; P:mitophagy; ISS:UniProtKB.
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 Mitochondrion; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7908909"
FT CHAIN 2..120
FT /note="Microtubule-associated proteins 1A/1B light chain
FT 3B"
FT /id="PRO_0000438650"
FT PROPEP 121..125
FT /note="Removed in mature form"
FT /id="PRO_0000212361"
FT SITE 120..121
FT /note="Cleavage; by ATG4B"
FT /evidence="ECO:0000250|UniProtKB:Q9GZQ8"
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 CONFLICT 4..5
FT /note="EK -> DR (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="T -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="T -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 14..16
FT /note="EQR -> DDV (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 18..21
FT /note="EDVR -> KEVQ (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="M -> T (in Ref. 4; AAB72082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 125 AA; 14704 MW; BB141DEC7642E92F CRC64;
MPSEKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM
SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPICEVYE SEKDEDGFLY MVYASQETFG
MKLSV
