MLP3A_BOVIN
ID MLP3A_BOVIN Reviewed; 121 AA.
AC Q2HJ23;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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 TP53INP1 and
CC TP53INP2. Directly interacts with SQSTM1; this interaction leads to
CC MAP1LC3A recruitment to inclusion bodies containing polyubiquitinated
CC protein aggregates and to inclusion body degradation by autophagy.
CC Interacts with ATG13. Interacts with ULK1. Interacts with TBC1D5. Found
CC in a complex with UBQLN1 and UBQLN2. Interacts with UBQLN4 (via STI1 1
CC and 2 domains). Interacts with UBQLN1 in the presence of UBQLN4.
CC Interacts with TRIM5. Interacts with MEFV. Interacts with RETREG1,
CC RETREG2 and RETREG3. Interacts with PICALM. Interacts with the
CC reticulophagy receptor TEX264. Interacts with MOAP1 (via LIR motif) (By
CC similarity). {ECO:0000250|UniProtKB:Q62625,
CC ECO:0000250|UniProtKB:Q9H492}.
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. 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:Q91VR7,
CC ECO:0000250|UniProtKB:Q9H492}.
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; BC113348; AAI13349.1; -; mRNA.
DR RefSeq; NP_001039640.1; NM_001046175.1.
DR RefSeq; XP_005214753.1; XM_005214696.1.
DR AlphaFoldDB; Q2HJ23; -.
DR SMR; Q2HJ23; -.
DR STRING; 9913.ENSBTAP00000008072; -.
DR PaxDb; Q2HJ23; -.
DR PRIDE; Q2HJ23; -.
DR Ensembl; ENSBTAT00000008072; ENSBTAP00000008072; ENSBTAG00000006135.
DR GeneID; 514547; -.
DR KEGG; bta:514547; -.
DR CTD; 84557; -.
DR VEuPathDB; HostDB:ENSBTAG00000006135; -.
DR VGNC; VGNC:31179; MAP1LC3A.
DR eggNOG; KOG1654; Eukaryota.
DR GeneTree; ENSGT00940000158853; -.
DR HOGENOM; CLU_119276_1_0_1; -.
DR InParanoid; Q2HJ23; -.
DR OMA; VNERSMV; -.
DR OrthoDB; 1508198at2759; -.
DR TreeFam; TF312964; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000006135; Expressed in Ammon's horn and 107 other tissues.
DR ExpressionAtlas; Q2HJ23; baseline and differential.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031090; C:organelle membrane; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
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:0016236; P:macroautophagy; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Lipoprotein;
KW Membrane; Microtubule; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..120
FT /note="Microtubule-associated proteins 1A/1B light chain
FT 3A"
FT /id="PRO_0000286935"
FT PROPEP 121
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000286936"
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; 14286 MW; 496B4A43ED388043 CRC64;
MPSDRPFKQR RSFADRCKEV QQIREQHPSK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM
SELVKIIRRR LQLNPTQAFF LLVNQHSMVS VSTPIADIYE QEKDEDGFLY MVYASQETFG
F
