NAGS_MOUSE
ID NAGS_MOUSE Reviewed; 527 AA.
AC Q8R4H7; B1AQG2; Q8C6G6; Q8CI77; Q8K1R8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=N-acetylglutamate synthase, mitochondrial;
DE EC=2.3.1.1 {ECO:0000269|PubMed:12049647};
DE AltName: Full=Amino-acid acetyltransferase;
DE Contains:
DE RecName: Full=N-acetylglutamate synthase long form;
DE Contains:
DE RecName: Full=N-acetylglutamate synthase short form;
DE Contains:
DE RecName: Full=N-acetylglutamate synthase conserved domain form;
DE Flags: Precursor;
GN Name=Nags;
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 [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=12049647; DOI=10.1042/bj20020161;
RA Caldovic L., Morizono H., Yu X., Thompson M., Shi D., Gallegos R.,
RA Allewell N.M., Malamy M.H., Tuchman M.;
RT "Identification, cloning and expression of the mouse N-acetylglutamate
RT synthase gene.";
RL Biochem. J. 364:825-831(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=129/Ola; TISSUE=Liver;
RA Eckhardt M., Yaghootfam A., Gieselmann V.;
RT "Molecular characterization of the murine N-acetylglutamate synthase.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 [7]
RP PROTEIN SEQUENCE OF 51-527 AND 84-527, AND PROTEOLYTIC PROCESSING.
RX PubMed=15050968; DOI=10.1016/j.ymgme.2003.10.017;
RA Morizono H., Caldovic L., Shi D., Tuchman M.;
RT "Mammalian N-acetylglutamate synthase.";
RL Mol. Genet. Metab. 81:S4-11(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
RN [9]
RP SUBUNIT.
RX PubMed=23894642; DOI=10.1371/journal.pone.0070369;
RA Zhao G., Jin Z., Allewell N.M., Tuchman M., Shi D.;
RT "Crystal structure of the N-acetyltransferase domain of human N-acetyl-L-
RT glutamate synthase in complex with N-acetyl-L-glutamate provides insights
RT into its catalytic and regulatory mechanisms.";
RL PLoS ONE 8:E70369-E70369(2013).
CC -!- FUNCTION: Plays a role in the regulation of ureagenesis by producing
CC the essential cofactor N-acetylglutamate (NAG), thus modulating
CC carbamoylphosphate synthase I (CPS1) activity.
CC {ECO:0000269|PubMed:12049647}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC Evidence={ECO:0000269|PubMed:12049647};
CC -!- ACTIVITY REGULATION: Increased by L-arginine.
CC {ECO:0000269|PubMed:12049647}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4. {ECO:0000305|PubMed:12049647}.
CC -!- SUBUNIT: Homodimer (By similarity). Homotetramer (PubMed:23894642).
CC {ECO:0000250|UniProtKB:Q8N159, ECO:0000269|PubMed:23894642}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q8N159}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R4H7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R4H7-2; Sequence=VSP_015620;
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver and small intestine.
CC Weakly expressed in the kidney, spleen and testis.
CC {ECO:0000269|PubMed:12049647}.
CC -!- DOMAIN: The amino-acid kinase (AAK) domain mediates binding of the
CC allosteric activator L-arginine. {ECO:0000250|UniProtKB:Q8N159}.
CC -!- PTM: Probably processed by mitochondrial processing peptidase (MPP).
CC The long form has not yet been isolated. {ECO:0000269|PubMed:15050968}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; AF462069; AAL86770.1; -; mRNA.
DR EMBL; AJ489814; CAD34015.1; -; mRNA.
DR EMBL; AK075765; BAC35941.1; -; mRNA.
DR EMBL; AL591145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34091.1; -; Genomic_DNA.
DR EMBL; BC057990; AAH57990.1; -; mRNA.
DR CCDS; CCDS25488.1; -. [Q8R4H7-1]
DR RefSeq; NP_665828.1; NM_145829.2. [Q8R4H7-1]
DR AlphaFoldDB; Q8R4H7; -.
DR SMR; Q8R4H7; -.
DR STRING; 10090.ENSMUSP00000050258; -.
DR iPTMnet; Q8R4H7; -.
DR PhosphoSitePlus; Q8R4H7; -.
DR SwissPalm; Q8R4H7; -.
DR jPOST; Q8R4H7; -.
DR MaxQB; Q8R4H7; -.
DR PaxDb; Q8R4H7; -.
DR PeptideAtlas; Q8R4H7; -.
DR PRIDE; Q8R4H7; -.
DR ProteomicsDB; 252762; -. [Q8R4H7-1]
DR ProteomicsDB; 252763; -. [Q8R4H7-2]
DR Antibodypedia; 29652; 87 antibodies from 23 providers.
DR DNASU; 217214; -.
DR Ensembl; ENSMUST00000055409; ENSMUSP00000050258; ENSMUSG00000048217. [Q8R4H7-1]
DR GeneID; 217214; -.
DR KEGG; mmu:217214; -.
DR UCSC; uc007lqp.2; mouse. [Q8R4H7-1]
DR CTD; 162417; -.
DR MGI; MGI:2387600; Nags.
DR VEuPathDB; HostDB:ENSMUSG00000048217; -.
DR eggNOG; KOG2436; Eukaryota.
DR GeneTree; ENSGT00390000005602; -.
DR HOGENOM; CLU_034853_0_0_1; -.
DR InParanoid; Q8R4H7; -.
DR OMA; FQTCYHS; -.
DR OrthoDB; 769117at2759; -.
DR PhylomeDB; Q8R4H7; -.
DR TreeFam; TF332628; -.
DR BRENDA; 2.3.1.1; 3474.
DR Reactome; R-MMU-70635; Urea cycle.
DR UniPathway; UPA00068; UER00106.
DR BioGRID-ORCS; 217214; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Nags; mouse.
DR PRO; PR:Q8R4H7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R4H7; protein.
DR Bgee; ENSMUSG00000048217; Expressed in left lobe of liver and 33 other tissues.
DR Genevisible; Q8R4H7; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IDA:MGI.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006536; P:glutamate metabolic process; IDA:MGI.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011243; GlcNAc_Synth_met.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR Pfam; PF04768; NAT; 1.
DR PIRSF; PIRSF036442; NAGS_animal; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51731; GNAT_NAGS; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Direct protein sequencing;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide;
KW Urea cycle.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..527
FT /note="N-acetylglutamate synthase long form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041933"
FT CHAIN 51..527
FT /note="N-acetylglutamate synthase short form"
FT /id="PRO_0000041934"
FT CHAIN 84..527
FT /note="N-acetylglutamate synthase conserved domain form"
FT /id="PRO_0000041935"
FT DOMAIN 368..519
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 14..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 19..369
FT /note="Amino-acid kinase domain (AAK)"
FT /evidence="ECO:0000250|UniProtKB:Q8N159"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N159"
FT BINDING 437
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N159"
FT BINDING 467..472
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N159"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015620"
FT CONFLICT 72..75
FT /note="EEPS -> DPRVR (in Ref. 1; AAL86770)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 57489 MW; 3A39E92955B11231 CRC64;
MATAWVATAL RSAAAARRLR SPGGPGGSRR LSGSARRRGA KSASPGRRLS TARAHAEDAE
GAKGRVQSPA VEEPSWTPLP TPLESPAPPA GRSLVQRDIQ AFLNQCGASP GEARHWLTQF
QTCYHSVDKP FAVMEVDEEV IRCPQAVSRL AFALAFLQRM DMKPLVVLGL PTPTAPSGCL
SFWEAKAQLA QSCKVLVDEL RHNAATAVPF FGGGSVLSAA EPAPHASYGG IVAVETDLLQ
WCLESNSIPI LCPIGETAAR RSVLLDSLEV TASLAKALQP TKIIFLNNSG GLRNNSQKIL
SNVNLPADLD LVTNAEWLSI KERQQIRLIV DVLSRLPHYS SAVITAASTL LTELFSNKGC
GTLFKNAERM LRVRNLDSLD QGRLVNLVNA SFGKKLREDY LESLRPRLHS IYVSEGYNAA
AILTVEPVLG GTPYLDKFVV SSSRQGQGSG QMLWECLRRD LQTLFWRSRV TNPINPWYFK
HSDGSFSNKQ WIFFWFGLAD IRDSYELVNH AKGLPDSFCK PASDPGS
