NAA11_RAT
ID NAA11_RAT Reviewed; 246 AA.
AC Q4V8K3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=N-alpha-acetyltransferase 11;
DE EC=2.3.1.255 {ECO:0000250|UniProtKB:P41227};
DE AltName: Full=N-terminal acetyltransferase complex ARD1 subunit homolog B;
DE AltName: Full=NatA catalytic subunit Naa11;
GN Name=Naa11; Synonyms=Ard1b, Ard2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION.
RX PubMed=16638120; DOI=10.1186/1471-2091-7-13;
RA Arnesen T., Betts M.J., Pendino F., Liberles D.A., Anderson D., Caro J.,
RA Kong X., Varhaug J.E., Lillehaug J.R.;
RT "Characterization of hARD2, a processed hARD1 gene duplicate, encoding a
RT human protein N-alpha-acetyltransferase.";
RL BMC Biochem. 7:13-13(2006).
CC -!- FUNCTION: Displays alpha (N-terminal) acetyltransferase activity.
CC Proposed alternative catalytic subunit of the N-terminal
CC acetyltransferase A (NatA) complex. {ECO:0000250|UniProtKB:Q9BSU3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496,
CC Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133369; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500,
CC Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718,
CC ChEBI:CHEBI:83683; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504,
CC Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC ChEBI:CHEBI:83690; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508,
CC Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741,
CC ChEBI:CHEBI:133371; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) +
CC N-terminal N(alpha)-acetyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-
CC terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516,
CC Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739,
CC ChEBI:CHEBI:133375; EC=2.3.1.255;
CC Evidence={ECO:0000250|UniProtKB:P41227};
CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA) complex
CC composed of NAA11 and NAA15. Interacts with HIF1A.
CC {ECO:0000250|UniProtKB:Q9BSU3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BSU3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9BSU3}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC097350; AAH97350.1; -; mRNA.
DR RefSeq; NP_001019913.1; NM_001024742.1.
DR AlphaFoldDB; Q4V8K3; -.
DR SMR; Q4V8K3; -.
DR STRING; 10116.ENSRNOP00000002776; -.
DR iPTMnet; Q4V8K3; -.
DR PhosphoSitePlus; Q4V8K3; -.
DR jPOST; Q4V8K3; -.
DR PaxDb; Q4V8K3; -.
DR PRIDE; Q4V8K3; -.
DR Ensembl; ENSRNOT00000002776; ENSRNOP00000002776; ENSRNOG00000002031.
DR GeneID; 289482; -.
DR KEGG; rno:289482; -.
DR UCSC; RGD:1564723; rat.
DR CTD; 84779; -.
DR RGD; 1564723; Naa11.
DR eggNOG; KOG3235; Eukaryota.
DR GeneTree; ENSGT00940000164242; -.
DR HOGENOM; CLU_013985_7_0_1; -.
DR InParanoid; Q4V8K3; -.
DR OMA; KGSEACQ; -.
DR OrthoDB; 1489230at2759; -.
DR PhylomeDB; Q4V8K3; -.
DR TreeFam; TF300078; -.
DR PRO; PR:Q4V8K3; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002031; Expressed in testis and 2 other tissues.
DR GO; GO:0031415; C:NatA complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; ISO:RGD.
DR GO; GO:1990190; F:peptide-glutamate-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISO:RGD.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR045047; Ard1-like.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR23091; PTHR23091; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..246
FT /note="N-alpha-acetyltransferase 11"
FT /id="PRO_0000305011"
FT DOMAIN 1..152
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..58
FT /note="Interaction with NAA15"
FT /evidence="ECO:0000250"
FT REGION 175..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 246 AA; 27623 MW; 7A2D6376A95F1483 CRC64;
MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDEDG KIVGYVLAKM
EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFSAKYVSLH VRKSNRAALH
LYSNTLNFQV SEVEPKYYAD GEDAYAMKRD LAQMADELRR QLVLKKSRYV VLGSEENQEA
QDSTLPDAEE ACQPENPAGK GSEACQPENP AGKGSEACQP ENPAGKDTGS HSTDVQDSSE
YLDSTS
