Q5E9A1 · NACA_BOVIN
- ProteinNascent polypeptide-associated complex subunit alpha
- GeneNACA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids215 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nascent polypeptide-associated complex | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | TBP-class protein binding | |
Molecular Function | transcription coactivator activity | |
Molecular Function | unfolded protein binding | |
Biological Process | protein targeting to membrane | |
Biological Process | protein transport |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameNascent polypeptide-associated complex subunit alpha
- Short namesNAC-alpha
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionQ5E9A1
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000135574 | 1-215 | Nascent polypeptide-associated complex subunit alpha | |||
Sequence: MPGEATDTVPATEQELPQPQAETGSGTESDSDESVPELEEQDSTQATTQQAQLAAAAEIDEEPVSKAKQSRSEKKARKAMSKLGLRQVTGVTRVTIRKSKNILFVITKPDVYKSPASDTYIVFGEAKIEDLSQQAQLAAAEKFKVQGEAVSNIQENTQTPTVQEESEEEEVDETGVEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMELTM | ||||||
Modified residue | 43 | Phosphoserine; by ILK1 | ||||
Sequence: S | ||||||
Modified residue | 132 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 142 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 142 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 159 | Phosphothreonine; by GSK3-beta | ||||
Sequence: T | ||||||
Modified residue | 161 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 166 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 186 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 191 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 203 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation of Ser-43 by ILK during cell adhesion may promote nuclear localization. Phosphorylation of Thr-159 by GSK3B may promote proteasome mediated degradation.
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Part of the nascent polypeptide-associated complex (NAC), which is a heterodimer of NACA and BTF3 (via NAC-A/B domains). NAC associates with ribosomes through the BTF3/NACB subunit and contacts the ribosomal protein L23, which is positioned near the exiting site. Both subunits can contact nascent polypeptide chains. NACA may also form homodimers, and only this form binds DNA. Interacts with TBP and JUN (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-81 | Disordered | ||||
Sequence: MPGEATDTVPATEQELPQPQAETGSGTESDSDESVPELEEQDSTQATTQQAQLAAAAEIDEEPVSKAKQSRSEKKARKAMS | ||||||
Compositional bias | 11-31 | Polar residues | ||||
Sequence: ATEQELPQPQAETGSGTESDS | ||||||
Compositional bias | 40-54 | Polar residues | ||||
Sequence: EQDSTQATTQQAQLA | ||||||
Compositional bias | 61-80 | Basic and acidic residues | ||||
Sequence: EEPVSKAKQSRSEKKARKAM | ||||||
Region | 69-80 | Required for DNA-binding | ||||
Sequence: QSRSEKKARKAM | ||||||
Domain | 70-135 | NAC-A/B | ||||
Sequence: SRSEKKARKAMSKLGLRQVTGVTRVTIRKSKNILFVITKPDVYKSPASDTYIVFGEAKIEDLSQQA | ||||||
Region | 93-108 | RNA/DNA-binding | ||||
Sequence: RVTIRKSKNILFVITK | ||||||
Domain | 176-213 | UBA | ||||
Sequence: VEVKDIELVMSQANVSRAKAVRALKNNSNDIVNAIMEL |
Domain
The positively charged inner surface of the NAC-A/B domain is crucial for NACA localization in the nucleus and DNA-binding. This region is blocked from binding nucleic acids in the heterodimeric complex by a helix region in the beta-subunit, it also displays much higher affinity for RNA than DNA (By similarity).
Sequence similarities
Belongs to the NAC-alpha family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length215
- Mass (Da)23,370
- Last updated2005-03-15 v1
- ChecksumA507EC80FA348A0D
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAA9TEH8 | A0AAA9TEH8_BOVIN | NACA | 295 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-31 | Polar residues | ||||
Sequence: ATEQELPQPQAETGSGTESDS | ||||||
Compositional bias | 40-54 | Polar residues | ||||
Sequence: EQDSTQATTQQAQLA | ||||||
Compositional bias | 61-80 | Basic and acidic residues | ||||
Sequence: EEPVSKAKQSRSEKKARKAM |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BT021019 EMBL· GenBank· DDBJ | AAX09036.1 EMBL· GenBank· DDBJ | mRNA | ||
BC102357 EMBL· GenBank· DDBJ | AAI02358.1 EMBL· GenBank· DDBJ | mRNA |