NTAQ1_MOUSE
ID NTAQ1_MOUSE Reviewed; 209 AA.
AC Q80WB5;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein N-terminal glutamine amidohydrolase {ECO:0000305};
DE EC=3.5.1.122 {ECO:0000269|PubMed:19560421};
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF CYS-23; CYS-28; CYS-30; CYS-38; GLU-39; ASP-81; HIS-83 AND
RP ASP-147.
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000269|PubMed:19560421}.
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:0000269|PubMed:19560421};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96HA8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19560421}.
CC Nucleus {ECO:0000269|PubMed:19560421}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19560421}.
CC -!- SIMILARITY: Belongs to the NTAQ1 family. {ECO:0000305}.
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DR EMBL; AK150578; BAE29673.1; -; mRNA.
DR EMBL; BC051524; AAH51524.1; -; mRNA.
DR CCDS; CCDS27490.1; -.
DR RefSeq; NP_084010.1; NM_029734.2.
DR AlphaFoldDB; Q80WB5; -.
DR SMR; Q80WB5; -.
DR BioGRID; 218305; 18.
DR STRING; 10090.ENSMUSP00000064622; -.
DR PhosphoSitePlus; Q80WB5; -.
DR EPD; Q80WB5; -.
DR MaxQB; Q80WB5; -.
DR PaxDb; Q80WB5; -.
DR PeptideAtlas; Q80WB5; -.
DR PRIDE; Q80WB5; -.
DR ProteomicsDB; 293754; -.
DR Antibodypedia; 13855; 68 antibodies from 18 providers.
DR DNASU; 76773; -.
DR Ensembl; ENSMUST00000067563; ENSMUSP00000064622; ENSMUSG00000022359.
DR GeneID; 76773; -.
DR KEGG; mmu:76773; -.
DR UCSC; uc007vti.1; mouse.
DR CTD; 76773; -.
DR MGI; MGI:1924023; Wdyhv1.
DR VEuPathDB; HostDB:ENSMUSG00000022359; -.
DR eggNOG; KOG3261; Eukaryota.
DR GeneTree; ENSGT00390000014398; -.
DR HOGENOM; CLU_091083_1_0_1; -.
DR InParanoid; Q80WB5; -.
DR OMA; GWGTVYS; -.
DR OrthoDB; 1337506at2759; -.
DR PhylomeDB; Q80WB5; -.
DR TreeFam; TF105807; -.
DR BRENDA; 3.5.1.122; 3474.
DR BioGRID-ORCS; 76773; 1 hit in 62 CRISPR screens.
DR ChiTaRS; Wdyhv1; mouse.
DR PRO; PR:Q80WB5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q80WB5; protein.
DR Bgee; ENSMUSG00000022359; Expressed in bone marrow and 61 other tissues.
DR ExpressionAtlas; Q80WB5; baseline and differential.
DR Genevisible; Q80WB5; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA: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; IDA:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; NAS:UniProtKB.
DR GO; GO:0036211; P:protein modification process; IDA: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 Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..209
FT /note="Protein N-terminal glutamine amidohydrolase"
FT /id="PRO_0000279410"
FT ACT_SITE 30
FT /evidence="ECO:0000305"
FT ACT_SITE 83
FT /evidence="ECO:0000305"
FT ACT_SITE 99
FT /evidence="ECO:0000305"
FT MUTAGEN 23
FT /note="C->A: Does not strongly affect N-terminal glutamine
FT amidohydrolase activity."
FT /evidence="ECO:0000269|PubMed:19560421"
FT MUTAGEN 28
FT /note="C->A: Does not strongly affect N-terminal glutamine
FT amidohydrolase activity."
FT /evidence="ECO:0000269|PubMed:19560421"
FT MUTAGEN 30
FT /note="C->A: Loss of N-terminal glutamine amidohydrolase
FT activity."
FT /evidence="ECO:0000269|PubMed:19560421"
FT MUTAGEN 38
FT /note="C->A: Does not strongly affect N-terminal glutamine
FT amidohydrolase activity."
FT /evidence="ECO:0000269|PubMed:19560421"
FT MUTAGEN 39
FT /note="E->Q: Does not strongly affect N-terminal glutamine
FT amidohydrolase activity."
FT /evidence="ECO:0000269|PubMed:19560421"
FT MUTAGEN 81
FT /note="D->N: Impaired N-terminal glutamine amidohydrolase
FT activity."
FT /evidence="ECO:0000269|PubMed:19560421"
FT MUTAGEN 83
FT /note="H->A: Loss of N-terminal glutamine amidohydrolase
FT activity."
FT /evidence="ECO:0000269|PubMed:19560421"
FT MUTAGEN 147
FT /note="D->N: Does not strongly affect N-terminal glutamine
FT amidohydrolase activity."
FT /evidence="ECO:0000269|PubMed:19560421"
SQ SEQUENCE 209 AA; 24337 MW; 789A08A3B94619CB CRC64;
MEGDGPAATA PQYQPVCPTR DACVYNSCYC EENIWKLCEY IKTHNQYLLE ECYAVFISNE
KKMVPIWKQQ ARPENGPVIW DYHVVLLHVS REGQSFIYDL DTILPFPCPF DIYIEDALKS
DDDIHLQFRR KFRVVRADSY LKHFASDRSH MKDSSGNWRE PPPEYPCIET GDSKMNLNDF
ISMDPAVGWG AVYTLPEFVH RFSSKTYQA
