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N-acetylglutamate synthase, mitochondrial (EC 2.3.1.1) (Amino-acid acetyltransferase) [Cleaved into: N-acetylglutamate synthase long form; N-acetylglutamate synthase short form; N-acetylglutamate synthase conserved domain form]

 NAGS_MOUSE              Reviewed;         527 AA.
Q8R4H7; B1AQG2; Q8C6G6; Q8CI77; Q8K1R8;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
13-SEP-2005, sequence version 2.
12-SEP-2018, entry version 124.
RecName: Full=N-acetylglutamate synthase, mitochondrial;
EC=2.3.1.1 {ECO:0000269|PubMed:12049647};
AltName: Full=Amino-acid acetyltransferase;
Contains:
RecName: Full=N-acetylglutamate synthase long form;
Contains:
RecName: Full=N-acetylglutamate synthase short form;
Contains:
RecName: Full=N-acetylglutamate synthase conserved domain form;
Flags: Precursor;
Name=Nags;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=12049647; DOI=10.1042/BJ20020161;
Caldovic L., Morizono H., Yu X., Thompson M., Shi D., Gallegos R.,
Allewell N.M., Malamy M.H., Tuchman M.;
"Identification, cloning and expression of the mouse N-acetylglutamate
synthase gene.";
Biochem. J. 364:825-831(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=129/Ola; TISSUE=Liver;
Eckhardt M., Yaghootfam A., Gieselmann V.;
"Molecular characterization of the murine N-acetylglutamate
synthase.";
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 51-527 AND 84-527, AND PROTEOLYTIC PROCESSING.
PubMed=15050968; DOI=10.1016/j.ymgme.2003.10.017;
Morizono H., Caldovic L., Shi D., Tuchman M.;
"Mammalian N-acetylglutamate synthase.";
Mol. Genet. Metab. 81:S4-11(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
SUBUNIT.
PubMed=23894642; DOI=10.1371/journal.pone.0070369;
Zhao G., Jin Z., Allewell N.M., Tuchman M., Shi D.;
"Crystal structure of the N-acetyltransferase domain of human N-
acetyl-L-glutamate synthase in complex with N-acetyl-L-glutamate
provides insights into its catalytic and regulatory mechanisms.";
PLoS ONE 8:E70369-E70369(2013).
-!- FUNCTION: Plays a role in the regulation of ureagenesis by
producing the essential cofactor N-acetylglutamate (NAG), thus
modulating carbamoylphosphate synthase I (CPS1) activity.
{ECO:0000269|PubMed:12049647}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-
glutamate. {ECO:0000269|PubMed:12049647}.
-!- ACTIVITY REGULATION: Increased by L-arginine.
{ECO:0000269|PubMed:12049647}.
-!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
acetyl-L-ornithine from L-glutamate: step 1/4.
{ECO:0000305|PubMed:12049647}.
-!- SUBUNIT: Homodimer (By similarity). Homotetramer
(PubMed:23894642). {ECO:0000250|UniProtKB:Q8N159,
ECO:0000269|PubMed:23894642}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000250|UniProtKB:Q8N159}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8R4H7-1; Sequence=Displayed;
Name=2;
IsoId=Q8R4H7-2; Sequence=VSP_015620;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in the liver and small
intestine. Weakly expressed in the kidney, spleen and testis.
{ECO:0000269|PubMed:12049647}.
-!- DOMAIN: The amino-acid kinase (AAK) domain mediates binding of the
allosteric activator L-arginine. {ECO:0000250|UniProtKB:Q8N159}.
-!- PTM: Probably processed by mitochondrial processing peptidase
(MPP). The long form has not yet been isolated.
{ECO:0000269|PubMed:15050968}.
-!- SIMILARITY: Belongs to the acetyltransferase family.
{ECO:0000305}.
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EMBL; AF462069; AAL86770.1; -; mRNA.
EMBL; AJ489814; CAD34015.1; -; mRNA.
EMBL; AK075765; BAC35941.1; -; mRNA.
EMBL; AL591145; CAM23258.1; -; Genomic_DNA.
EMBL; CH466558; EDL34091.1; -; Genomic_DNA.
EMBL; BC057990; AAH57990.1; -; mRNA.
CCDS; CCDS25488.1; -. [Q8R4H7-1]
RefSeq; NP_665828.1; NM_145829.2. [Q8R4H7-1]
UniGene; Mm.31686; -.
ProteinModelPortal; Q8R4H7; -.
STRING; 10090.ENSMUSP00000050258; -.
iPTMnet; Q8R4H7; -.
PhosphoSitePlus; Q8R4H7; -.
SwissPalm; Q8R4H7; -.
PaxDb; Q8R4H7; -.
PeptideAtlas; Q8R4H7; -.
PRIDE; Q8R4H7; -.
Ensembl; ENSMUST00000055409; ENSMUSP00000050258; ENSMUSG00000048217. [Q8R4H7-1]
GeneID; 217214; -.
KEGG; mmu:217214; -.
UCSC; uc007lqp.2; mouse. [Q8R4H7-1]
CTD; 162417; -.
MGI; MGI:2387600; Nags.
eggNOG; KOG2436; Eukaryota.
eggNOG; COG0548; LUCA.
GeneTree; ENSGT00390000005602; -.
HOGENOM; HOG000007983; -.
HOVERGEN; HBG080036; -.
InParanoid; Q8R4H7; -.
KO; K11067; -.
OMA; GSIPILC; -.
OrthoDB; EOG091G0FPD; -.
PhylomeDB; Q8R4H7; -.
TreeFam; TF332628; -.
BRENDA; 2.3.1.1; 3474.
Reactome; R-MMU-70635; Urea cycle.
UniPathway; UPA00068; UER00106.
PRO; PR:Q8R4H7; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000048217; Expressed in 42 organ(s), highest expression level in liver.
CleanEx; MM_NAGS; -.
Genevisible; Q8R4H7; MM.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IDA:MGI.
GO; GO:0034618; F:arginine binding; IBA:GO_Central.
GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
GO; GO:0006536; P:glutamate metabolic process; IDA:MGI.
GO; GO:0016310; P:phosphorylation; IEA:GOC.
GO; GO:0000050; P:urea cycle; IEA:UniProtKB-KW.
Gene3D; 3.40.1160.10; -; 1.
InterPro; IPR036393; AceGlu_kinase-like_sf.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR011243; GlcNAc_Synth_met.
InterPro; IPR006855; Vertebrate-like_GNAT_dom.
Pfam; PF04768; NAT; 1.
PIRSF; PIRSF036442; NAGS_animal; 1.
SUPFAM; SSF53633; SSF53633; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51731; GNAT_NAGS; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Complete proteome;
Direct protein sequencing; Mitochondrion; Reference proteome;
Transferase; Transit peptide; Urea cycle.
TRANSIT 1 18 Mitochondrion. {ECO:0000255}.
CHAIN 19 527 N-acetylglutamate synthase long form.
{ECO:0000255}.
/FTId=PRO_0000041933.
CHAIN 51 527 N-acetylglutamate synthase short form.
/FTId=PRO_0000041934.
CHAIN 84 527 N-acetylglutamate synthase conserved
domain form.
/FTId=PRO_0000041935.
DOMAIN 368 519 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
REGION 19 369 Amino-acid kinase domain (AAK).
{ECO:0000250|UniProtKB:Q8N159}.
REGION 467 472 Substrate binding.
{ECO:0000250|UniProtKB:Q8N159}.
BINDING 394 394 Substrate.
{ECO:0000250|UniProtKB:Q8N159}.
BINDING 437 437 Substrate.
{ECO:0000250|UniProtKB:Q8N159}.
VAR_SEQ 1 159 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_015620.
CONFLICT 72 75 EEPS -> DPRVR (in Ref. 1; AAL86770).
{ECO:0000305}.
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


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