ID   NTAQ1_DANRE             Reviewed;         202 AA.
AC   Q1LWX3; B7ZV64; Q0P423;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
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; ORFNames=si:rp71-45k5.3;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2006) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI22322.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BX511004; CAK03630.1; -; Genomic_DNA.
DR   EMBL; BC171472; AAI71472.1; -; mRNA.
DR   EMBL; BC171474; AAI71474.1; -; mRNA.
DR   EMBL; BC122321; AAI22322.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001038412.1; NM_001044947.1.
DR   AlphaFoldDB; Q1LWX3; -.
DR   SMR; Q1LWX3; -.
DR   STRING; 7955.ENSDARP00000094043; -.
DR   PaxDb; Q1LWX3; -.
DR   Ensembl; ENSDART00000103266; ENSDARP00000094043; ENSDARG00000070403.
DR   GeneID; 560935; -.
DR   KEGG; dre:560935; -.
DR   CTD; 76773; -.
DR   ZFIN; ZDB-GENE-060503-848; wdyhv1.
DR   eggNOG; KOG3261; Eukaryota.
DR   GeneTree; ENSGT00390000014398; -.
DR   HOGENOM; CLU_091083_1_0_1; -.
DR   InParanoid; Q1LWX3; -.
DR   OMA; GWGTVYS; -.
DR   OrthoDB; 1337506at2759; -.
DR   PhylomeDB; Q1LWX3; -.
DR   TreeFam; TF105807; -.
DR   PRO; PR:Q1LWX3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 19.
DR   Bgee; ENSDARG00000070403; Expressed in brain and 22 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..202
FT                   /note="Protein N-terminal glutamine amidohydrolase"
FT                   /id="PRO_0000279412"
FT   ACT_SITE        27
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        96
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   202 AA;  23546 MW;  D2B7F19DBDB13EC7 CRC64;
     MNEESASSEY KVITPSGNQC VYTSCYCEEN VWKLCEYIKN QRHCPLEEVY AVFISNERKK
     IPIWKQKSSR GDEPVIWDYH VILLHASKQG PSFIYDLDTI LPFPCSLDVY SMEAFQSDKH
     LKPAYWRKLR VIPGDTYLKE FASDRSHMKD SDGNWRMPPP AYPCLETPES KMNLDDFICM
     DPRVGYGEVY SLSDFVKHFG VK