NTAQ1_RAT
ID NTAQ1_RAT Reviewed; 207 AA.
AC Q5BJV9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Protein N-terminal glutamine amidohydrolase {ECO:0000305};
DE EC=3.5.1.122 {ECO:0000250|UniProtKB:Q80WB5};
DE AltName: Full=Protein NH2-terminal glutamine deamidase;
DE Short=N-terminal Gln amidase;
DE Short=Nt(Q)-amidase;
DE AltName: Full=WDYHV motif-containing protein 1;
GN Name=Ntaq1; Synonyms=Wdyhv1;
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=Ovary;
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).
CC -!- FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine
CC residues to glutamate, an important step in N-end rule pathway of
CC protein degradation. Conversion of the resulting N-terminal glutamine
CC to glutamate renders the protein susceptible to arginylation,
CC polyubiquitination and degradation as specified by the N-end rule. Does
CC not act on substrates with internal or C-terminal glutamine and does
CC not act on non-glutamine residues in any position. Does not deaminate
CC acetylated N-terminal glutamine. With the exception of proline, all
CC tested second-position residues on substrate peptides do not greatly
CC influence the activity. In contrast, a proline at position 2, virtually
CC abolishes deamidation of N-terminal glutamine.
CC {ECO:0000250|UniProtKB:Q80WB5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-terminal L-glutaminyl-[protein] = N-terminal L-
CC glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:50680, Rhea:RHEA-
CC COMP:12668, Rhea:RHEA-COMP:12777, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:64721, ChEBI:CHEBI:64722;
CC EC=3.5.1.122; Evidence={ECO:0000250|UniProtKB:Q80WB5};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96HA8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q80WB5}. Nucleus {ECO:0000250|UniProtKB:Q80WB5}.
CC -!- SIMILARITY: Belongs to the NTAQ1 family. {ECO:0000305}.
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DR EMBL; BC091306; AAH91306.1; -; mRNA.
DR RefSeq; NP_001020195.1; NM_001025024.1.
DR AlphaFoldDB; Q5BJV9; -.
DR SMR; Q5BJV9; -.
DR STRING; 10116.ENSRNOP00000008785; -.
DR PaxDb; Q5BJV9; -.
DR Ensembl; ENSRNOT00000008785; ENSRNOP00000008785; ENSRNOG00000006700.
DR GeneID; 362914; -.
DR KEGG; rno:362914; -.
DR UCSC; RGD:1311362; rat.
DR CTD; 55093; -.
DR RGD; 1311362; Wdyhv1.
DR eggNOG; KOG3261; Eukaryota.
DR GeneTree; ENSGT00390000014398; -.
DR InParanoid; Q5BJV9; -.
DR OMA; GWGTVYS; -.
DR OrthoDB; 1337506at2759; -.
DR PhylomeDB; Q5BJV9; -.
DR PRO; PR:Q5BJV9; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000006700; Expressed in pancreas and 19 other tissues.
DR ExpressionAtlas; Q5BJV9; baseline and differential.
DR Genevisible; Q5BJV9; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IEA:InterPro.
DR GO; GO:0070773; F:protein-N-terminal glutamine amidohydrolase activity; ISS:UniProtKB.
DR GO; GO:0036211; P:protein modification process; ISS:UniProtKB.
DR Gene3D; 3.10.620.10; -; 1.
DR InterPro; IPR037132; N_Gln_amidohydro_ab_roll_sf.
DR InterPro; IPR039733; NTAQ1.
DR InterPro; IPR023128; Prot_N_Gln_amidohydro_ab_roll.
DR PANTHER; PTHR13035; PTHR13035; 1.
DR Pfam; PF09764; Nt_Gln_amidase; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..207
FT /note="Protein N-terminal glutamine amidohydrolase"
FT /id="PRO_0000279411"
FT ACT_SITE 30
FT /evidence="ECO:0000250"
FT ACT_SITE 83
FT /evidence="ECO:0000250"
FT ACT_SITE 99
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 24125 MW; 79BAD8A0C0A9DC7D CRC64;
MEGDSRAATA SQYQPACPTR DACVYSSCYC EENIWKLCEY IKTHNQYLLE ECYAVFISNE
KKMVPIWKQQ ARPENGPVIW DYHVVLLHVS REGQSFIYDL DTILPFPCPF DIYIEDALKS
DDDIHPQFRR KFRVVRADSY LKNFASDRSH MKDSSGNWRE PPPEYPCIET GDSKMNLNDF
ISMDPAVGWG AVYTLSEFVH RFSSKNY