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Protein

Nascent polypeptide-associated complex subunit alpha

Gene

NACA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Transcription, Transport

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nascent polypeptide-associated complex subunit alpha
Short name:
NAC-alpha
Alternative name(s):
Alpha-NAC
Gene namesi
Name:NACA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: The heterodimer is located mainly in the cytosol, and the homodimer in the nucleus.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Nascent polypeptide-associated complex subunit alphaPRO_0000135574Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431Phosphoserine; by ILK1By similarity
Modified residuei132 – 1321PhosphoserineBy similarity
Modified residuei142 – 1421N6-acetyllysineBy similarity
Modified residuei159 – 1591Phosphothreonine; by GSK3-betaBy similarity
Modified residuei161 – 1611PhosphothreonineBy similarity
Modified residuei166 – 1661PhosphoserineBy similarity
Modified residuei186 – 1861PhosphoserineBy similarity
Modified residuei191 – 1911PhosphoserineBy similarity
Modified residuei203 – 2031PhosphoserineBy similarity

Post-translational modificationi

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 - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ5E9A1.
PeptideAtlasiQ5E9A1.
PRIDEiQ5E9A1.

Interactioni

Subunit structurei

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).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000014162.

Structurei

3D structure databases

ProteinModelPortaliQ5E9A1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 13566NAC-A/BPROSITE-ProRule annotationAdd
BLAST
Domaini176 – 21338UBAAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni69 – 8012Required for DNA-bindingBy similarityAdd
BLAST
Regioni93 – 10816RNA/DNA-bindingBy similarityAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the NAC-alpha family.Curated
Contains 1 NAC-A/B (NAC-alpha/beta) domain.PROSITE-ProRule annotation
Contains 1 UBA domain.Curated

Phylogenomic databases

eggNOGiKOG2239. Eukaryota.
COG1308. LUCA.
GeneTreeiENSGT00440000033468.
HOGENOMiHOG000239674.
HOVERGENiHBG082004.
InParanoidiQ5E9A1.
KOiK03626.
OMAiLEEHDST.
OrthoDBiEOG7RNK24.
TreeFamiTF313348.

Family and domain databases

InterProiIPR016641. EGD2/NACA.
IPR002715. Nas_poly-pep-assoc_cplx_dom.
[Graphical view]
PANTHERiPTHR21713. PTHR21713. 1 hit.
PfamiPF01849. NAC. 1 hit.
[Graphical view]
PIRSFiPIRSF015901. NAC_alpha. 1 hit.
SMARTiSM01407. NAC. 1 hit.
[Graphical view]
PROSITEiPS51151. NAC_AB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5E9A1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGEATDTVP ATEQELPQPQ AETGSGTESD SDESVPELEE QDSTQATTQQ
60 70 80 90 100
AQLAAAAEID EEPVSKAKQS RSEKKARKAM SKLGLRQVTG VTRVTIRKSK
110 120 130 140 150
NILFVITKPD VYKSPASDTY IVFGEAKIED LSQQAQLAAA EKFKVQGEAV
160 170 180 190 200
SNIQENTQTP TVQEESEEEE VDETGVEVKD IELVMSQANV SRAKAVRALK
210
NNSNDIVNAI MELTM
Length:215
Mass (Da):23,370
Last modified:March 15, 2005 - v1
Checksum:iA507EC80FA348A0D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021019 mRNA. Translation: AAX09036.1.
BC102357 mRNA. Translation: AAI02358.1.
RefSeqiNP_001014916.1. NM_001014916.3.
XP_005206634.1. XM_005206577.2.
XP_005206635.1. XM_005206578.1.
XP_015326573.1. XM_015471087.1.
UniGeneiBt.24178.

Genome annotation databases

EnsembliENSBTAT00000014162; ENSBTAP00000014162; ENSBTAG00000010701.
GeneIDi513312.
KEGGibta:513312.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021019 mRNA. Translation: AAX09036.1.
BC102357 mRNA. Translation: AAI02358.1.
RefSeqiNP_001014916.1. NM_001014916.3.
XP_005206634.1. XM_005206577.2.
XP_005206635.1. XM_005206578.1.
XP_015326573.1. XM_015471087.1.
UniGeneiBt.24178.

3D structure databases

ProteinModelPortaliQ5E9A1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000014162.

Proteomic databases

PaxDbiQ5E9A1.
PeptideAtlasiQ5E9A1.
PRIDEiQ5E9A1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000014162; ENSBTAP00000014162; ENSBTAG00000010701.
GeneIDi513312.
KEGGibta:513312.

Organism-specific databases

CTDi4666.

Phylogenomic databases

eggNOGiKOG2239. Eukaryota.
COG1308. LUCA.
GeneTreeiENSGT00440000033468.
HOGENOMiHOG000239674.
HOVERGENiHBG082004.
InParanoidiQ5E9A1.
KOiK03626.
OMAiLEEHDST.
OrthoDBiEOG7RNK24.
TreeFamiTF313348.

Family and domain databases

InterProiIPR016641. EGD2/NACA.
IPR002715. Nas_poly-pep-assoc_cplx_dom.
[Graphical view]
PANTHERiPTHR21713. PTHR21713. 1 hit.
PfamiPF01849. NAC. 1 hit.
[Graphical view]
PIRSFiPIRSF015901. NAC_alpha. 1 hit.
SMARTiSM01407. NAC. 1 hit.
[Graphical view]
PROSITEiPS51151. NAC_AB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  3. "A protein complex required for signal-sequence-specific sorting and translocation."
    Wiedmann B., Sakai H., Davis T.A., Wiedmann M.
    Nature 370:434-440(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BTF3, ASSOCIATION WITH RIBOSOMES.
  4. "Unregulated exposure of the ribosomal M-site caused by NAC depletion results in delivery of non-secretory polypeptides to the Sec61 complex."
    Moeller I., Beatrix B., Kreibich G., Sakai H., Lauring B., Wiedmann M.
    FEBS Lett. 441:1-5(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "The alpha and beta subunit of the nascent polypeptide-associated complex have distinct functions."
    Beatrix B., Sakai H., Wiedmann M.
    J. Biol. Chem. 275:37838-37845(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BTF3, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiNACA_BOVIN
AccessioniPrimary (citable) accession number: Q5E9A1
Secondary accession number(s): Q3T0K5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: March 15, 2005
Last modified: July 6, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.