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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

Keywordsi

Molecular functionChaperone, DNA-binding
Biological processProtein transport, Transcription, Transport

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001355741 – 215Nascent polypeptide-associated complex subunit alphaAdd BLAST215

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43Phosphoserine; by ILK1By similarity1
Modified residuei132PhosphoserineBy similarity1
Modified residuei142N6-acetyllysine; alternateBy similarity1
Cross-linki142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei159Phosphothreonine; by GSK3-betaBy similarity1
Modified residuei161PhosphothreonineBy similarity1
Modified residuei166PhosphoserineBy similarity1
Modified residuei186PhosphoserineBy similarity1
Modified residuei191PhosphoserineBy similarity1
Modified residuei203PhosphoserineBy similarity1
Modified residuei214PhosphothreonineBy similarity1

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, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ5E9A1.
PeptideAtlasiQ5E9A1.
PRIDEiQ5E9A1.

Expressioni

Gene expression databases

BgeeiENSBTAG00000010701.

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.
SMRiQ5E9A1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini70 – 135NAC-A/BPROSITE-ProRule annotationAdd BLAST66
Domaini176 – 213UBAAdd BLAST38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni69 – 80Required for DNA-bindingBy similarityAdd BLAST12
Regioni93 – 108RNA/DNA-bindingBy similarityAdd BLAST16

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

Phylogenomic databases

eggNOGiKOG2239. Eukaryota.
COG1308. LUCA.
GeneTreeiENSGT00440000033468.
HOGENOMiHOG000239674.
HOVERGENiHBG082004.
InParanoidiQ5E9A1.
KOiK03626.
OMAiMANPRVE.
OrthoDBiEOG091G0292.
TreeFamiTF313348.

Family and domain databases

InterProiView protein in InterPro
IPR016641. EGD2/NACA.
IPR002715. Nas_poly-pep-assoc_cplx_dom.
PANTHERiPTHR21713. PTHR21713. 1 hit.
PfamiView protein in Pfam
PF01849. NAC. 1 hit.
PIRSFiPIRSF015901. NAC_alpha. 1 hit.
SMARTiView protein in SMART
SM01407. NAC. 1 hit.
PROSITEiView protein in PROSITE
PS51151. NAC_AB. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiNACA_BOVIN
AccessioniPrimary (citable) accession number: Q5E9A1
Secondary accession number(s): Q3T0K5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: March 15, 2005
Last modified: August 30, 2017
This is version 93 of the entry and version 1 of the sequence. See 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