NACA_PONAB
ID NACA_PONAB Reviewed; 215 AA.
AC Q5R9I9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Nascent polypeptide-associated complex subunit alpha;
DE Short=NAC-alpha;
DE AltName: Full=Alpha-NAC;
GN Name=NACA;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Prevents inappropriate targeting of non-secretory
CC polypeptides to the endoplasmic reticulum (ER). Binds to nascent
CC polypeptide chains as they emerge from the ribosome and blocks their
CC interaction with the signal recognition particle (SRP), which normally
CC targets nascent secretory peptides to the ER. Also reduces the inherent
CC affinity of ribosomes for protein translocation sites in the ER
CC membrane (M sites). May act as a specific coactivator for JUN, binding
CC to DNA and stabilizing the interaction of JUN homodimers with target
CC gene promoters (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the nascent polypeptide-associated complex (NAC),
CC which is a heterodimer of NACA and BTF3 (via NAC-A/B domains). NAC
CC associates with ribosomes through the BTF3/NACB subunit and contacts
CC the ribosomal protein L23, which is positioned near the exiting site.
CC Both subunits can contact nascent polypeptide chains. NACA may also
CC form homodimers, and only this form binds DNA. Interacts with TBP and
CC JUN (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=The heterodimer is located mainly in the cytosol, and the
CC homodimer in the nucleus. {ECO:0000250}.
CC -!- DOMAIN: The positively charged inner surface of the NAC-A/B domain is
CC crucial for NACA localization in the nucleus and DNA-binding. This
CC region is blocked from binding nucleic acids in the heterodimeric
CC complex by a helix region in the beta-subunit, it also displays much
CC higher affinity for RNA than DNA (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylation of Ser-43 by ILK during cell adhesion may promote
CC nuclear localization. Phosphorylation of Thr-159 by GSK3B may promote
CC proteasome mediated degradation.
CC -!- SIMILARITY: Belongs to the NAC-alpha family. {ECO:0000305}.
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DR EMBL; CR859398; CAH91571.1; -; mRNA.
DR RefSeq; NP_001125923.1; NM_001132451.2.
DR AlphaFoldDB; Q5R9I9; -.
DR SMR; Q5R9I9; -.
DR STRING; 9601.ENSPPYP00000005320; -.
DR GeneID; 100172857; -.
DR KEGG; pon:100172857; -.
DR CTD; 4666; -.
DR eggNOG; KOG2239; Eukaryota.
DR InParanoid; Q5R9I9; -.
DR OrthoDB; 1331328at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.20.70.30; -; 1.
DR InterPro; IPR016641; EGD2/NACA.
DR InterPro; IPR044034; NAC-like_UBA.
DR InterPro; IPR038187; NAC_A/B_dom_sf.
DR InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR PANTHER; PTHR21713; PTHR21713; 1.
DR Pfam; PF19026; HYPK_UBA; 1.
DR Pfam; PF01849; NAC; 1.
DR PIRSF; PIRSF015901; NAC_alpha; 1.
DR SMART; SM01407; NAC; 1.
DR PROSITE; PS51151; NAC_AB; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chaperone; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Transcription;
KW Transport; Ubl conjugation.
FT CHAIN 1..215
FT /note="Nascent polypeptide-associated complex subunit
FT alpha"
FT /id="PRO_0000135579"
FT DOMAIN 70..135
FT /note="NAC-A/B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT DOMAIN 176..213
FT /note="UBA"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..80
FT /note="Required for DNA-binding"
FT /evidence="ECO:0000250"
FT REGION 93..108
FT /note="RNA/DNA-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 11..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine; by ILK1"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 142
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 159
FT /note="Phosphothreonine; by GSK3-beta"
FT /evidence="ECO:0000250|UniProtKB:Q60817"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
SQ SEQUENCE 215 AA; 23442 MW; 062F99058BEF307C CRC64;
MPGEATETVP ATEQELPQPQ AETGSGTESD SDESVPELEE QDSTQATTQQ AQLAAAAEID
EEPVSKAKQS RSEKKARKAM SKLGLRQVTG VTRVTIRKSK NILFVITKPD VYKSPASDTY
IVFGEAKIED LSQQAQLAAA EKFKVQGEAV SNIQENTQTP TVQEESEEEE VDETDVEVKD
IELVMSQANV SRAKAVRALK NNSNDIVNAI MELTM
