ID   NTAQ1_BOVIN             Reviewed;         207 AA.
AC   Q3T0D3;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 88.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=19560421; DOI=10.1016/j.molcel.2009.04.032;
RA   Wang H., Piatkov K.I., Brower C.S., Varshavsky A.;
RT   "Glutamine-specific N-terminal amidase, a component of the N-end rule
RT   pathway.";
RL   Mol. Cell 34:686-695(2009).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3T0D3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3T0D3-2; Sequence=VSP_023422;
CC   -!- SIMILARITY: Belongs to the NTAQ1 family. {ECO:0000305}.
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DR   EMBL; BC102447; AAI02448.1; -; mRNA.
DR   EMBL; DV842245; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001030263.1; NM_001035091.1. [Q3T0D3-2]
DR   RefSeq; XP_005215414.1; XM_005215357.3. [Q3T0D3-1]
DR   AlphaFoldDB; Q3T0D3; -.
DR   SMR; Q3T0D3; -.
DR   STRING; 9913.ENSBTAP00000013086; -.
DR   PaxDb; Q3T0D3; -.
DR   PRIDE; Q3T0D3; -.
DR   Ensembl; ENSBTAT00000013086; ENSBTAP00000013086; ENSBTAG00000009916. [Q3T0D3-1]
DR   Ensembl; ENSBTAT00000047857; ENSBTAP00000045021; ENSBTAG00000009916. [Q3T0D3-2]
DR   GeneID; 510463; -.
DR   KEGG; bta:510463; -.
DR   CTD; 55093; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009916; -.
DR   eggNOG; KOG3261; Eukaryota.
DR   GeneTree; ENSGT00390000014398; -.
DR   HOGENOM; CLU_091083_1_0_1; -.
DR   InParanoid; Q3T0D3; -.
DR   OMA; GWGTVYS; -.
DR   OrthoDB; 1337506at2759; -.
DR   TreeFam; TF105807; -.
DR   BRENDA; 3.5.1.122; 908.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000009916; Expressed in granulosa cell and 104 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   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT   CHAIN           1..207
FT                   /note="Protein N-terminal glutamine amidohydrolase"
FT                   /id="PRO_0000279408"
FT   ACT_SITE        30
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        83
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        99
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         64..80
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_023422"
SQ   SEQUENCE   207 AA;  23910 MW;  0A7E3FA8EA87A9C0 CRC64;
     MEGDAPVAAA AHYQPASPPR DACVYNSCYC EENIWKLCEY IKNHDQYPLE ECYAVFISNE
     RKMIPIWKQQ ARPGDGPVIW DYHVVLLHVS SGGQSFIYDL DTVLPFPCPF DTYVEDAFKS
     DEDIHPQFRR KFRVIRADSY LKNFASDRSH MKDSSGNWRE PPPSYPCIET GDSKMNLNDF
     ISMDPEVGWG AVYSLPEFVH RFSSQNY