ID   NTAQ1_XENLA             Reviewed;         204 AA.
AC   Q5PPU8;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 60.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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; BC087490; AAH87490.1; -; mRNA.
DR   RefSeq; NP_001088806.1; NM_001095337.1.
DR   AlphaFoldDB; Q5PPU8; -.
DR   SMR; Q5PPU8; -.
DR   MaxQB; Q5PPU8; -.
DR   DNASU; 496074; -.
DR   GeneID; 496074; -.
DR   KEGG; xla:496074; -.
DR   CTD; 496074; -.
DR   Xenbase; XB-GENE-5746206; ntaq1.S.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 496074; Expressed in muscle tissue and 19 other tissues.
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..204
FT                   /note="Protein N-terminal glutamine amidohydrolase"
FT                   /id="PRO_0000279413"
FT   ACT_SITE        24
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   204 AA;  23386 MW;  1AD6215767B1AE83 CRC64;
     MEQAAGEPSP FLVRSDCLYT SCYCEENVWK LCEYIRDHRP CLLEQFSAVF ISNENKMIPI
     WKQKSAKGDG PVIWDYHVIL LHESARDGNF VYDLDTILPF PSPCNTYIRE ALKCDSNIHC
     DFRRKLRVVG AHEFLQTFAS DRSHMRDSSS NWTKPPPPYP CIQSAESTMN LDDFISMNPE
     VGWGTVYSLA AFTERFGDTT LASH