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Protein

N-acetylglutamate synthase, mitochondrial

Gene

Nags

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the regulation of ureagenesis by producing the essential cofactor N-acetylglutamate (NAG), thus modulating carbamoylphosphate synthase I (CPSI) activity.

Catalytic activityi

Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.

Enzyme regulationi

Increased by L-arginine.1 Publication

Pathwayi: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. N-acetylglutamate synthase, mitochondrial (Nags)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei394 – 3941SubstrateBy similarity
Binding sitei437 – 4371SubstrateBy similarity

GO - Molecular functioni

  • acetyl-CoA:L-glutamate N-acetyltransferase activity Source: MGI
  • arginine binding Source: GO_Central

GO - Biological processi

  • arginine biosynthetic process Source: GO_Central
  • glutamate metabolic process Source: MGI
  • urea cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Urea cycle

Enzyme and pathway databases

BRENDAi2.3.1.1. 3474.
ReactomeiR-MMU-70635. Urea cycle.
UniPathwayiUPA00068; UER00106.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylglutamate synthase, mitochondrial (EC:2.3.1.1)
Alternative name(s):
Amino-acid acetyltransferase
Cleaved into the following 3 chains:
Gene namesi
Name:Nags
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2387600. Nags.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1818MitochondrionSequence analysisAdd
BLAST
Chaini19 – 527509N-acetylglutamate synthase long formSequence analysisPRO_0000041933Add
BLAST
Chaini51 – 527477N-acetylglutamate synthase short formPRO_0000041934Add
BLAST
Chaini84 – 527444N-acetylglutamate synthase conserved domain formPRO_0000041935Add
BLAST

Post-translational modificationi

Probably processed by mitochondrial processing peptidase (MPP). The long form has not yet been isolated.1 Publication

Proteomic databases

MaxQBiQ8R4H7.
PaxDbiQ8R4H7.
PeptideAtlasiQ8R4H7.
PRIDEiQ8R4H7.

PTM databases

iPTMnetiQ8R4H7.
PhosphoSiteiQ8R4H7.

Expressioni

Tissue specificityi

Highly expressed in the liver and small intestine. Weakly expressed in the kidney, spleen and testis.1 Publication

Gene expression databases

BgeeiQ8R4H7.
CleanExiMM_NAGS.
GenevisibleiQ8R4H7. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000050258.

Structurei

3D structure databases

ProteinModelPortaliQ8R4H7.
SMRiQ8R4H7. Positions 91-521.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini368 – 519152N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 370352Amino-acid kinase domain (AAK)By similarityAdd
BLAST
Regioni467 – 4726Substrate bindingBy similarity

Domaini

The Amino-acid kinase domain (AAK) mediates binding of the allosteric activator L-arginine.By similarity

Sequence similaritiesi

Belongs to the acetyltransferase family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2436. Eukaryota.
COG0548. LUCA.
GeneTreeiENSGT00390000005602.
HOGENOMiHOG000007983.
HOVERGENiHBG080036.
InParanoidiQ8R4H7.
KOiK11067.
OMAiLTMEPVL.
OrthoDBiEOG77WWDH.
PhylomeDBiQ8R4H7.
TreeFamiTF332628.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR011243. GlcNAc_Synth_met.
IPR006855. Vertebrate-like_GNAT_dom.
[Graphical view]
PfamiPF04768. NAT. 1 hit.
[Graphical view]
PIRSFiPIRSF036442. NAGS_animal. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51731. GNAT_NAGS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8R4H7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATAWVATAL RSAAAARRLR SPGGPGGSRR LSGSARRRGA KSASPGRRLS
60 70 80 90 100
TARAHAEDAE GAKGRVQSPA VEEPSWTPLP TPLESPAPPA GRSLVQRDIQ
110 120 130 140 150
AFLNQCGASP GEARHWLTQF QTCYHSVDKP FAVMEVDEEV IRCPQAVSRL
160 170 180 190 200
AFALAFLQRM DMKPLVVLGL PTPTAPSGCL SFWEAKAQLA QSCKVLVDEL
210 220 230 240 250
RHNAATAVPF FGGGSVLSAA EPAPHASYGG IVAVETDLLQ WCLESNSIPI
260 270 280 290 300
LCPIGETAAR RSVLLDSLEV TASLAKALQP TKIIFLNNSG GLRNNSQKIL
310 320 330 340 350
SNVNLPADLD LVTNAEWLSI KERQQIRLIV DVLSRLPHYS SAVITAASTL
360 370 380 390 400
LTELFSNKGC GTLFKNAERM LRVRNLDSLD QGRLVNLVNA SFGKKLREDY
410 420 430 440 450
LESLRPRLHS IYVSEGYNAA AILTVEPVLG GTPYLDKFVV SSSRQGQGSG
460 470 480 490 500
QMLWECLRRD LQTLFWRSRV TNPINPWYFK HSDGSFSNKQ WIFFWFGLAD
510 520
IRDSYELVNH AKGLPDSFCK PASDPGS
Length:527
Mass (Da):57,489
Last modified:September 13, 2005 - v2
Checksum:i3A39E92955B11231
GO
Isoform 2 (identifier: Q8R4H7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.

Note: No experimental confirmation available.
Show »
Length:368
Mass (Da):40,480
Checksum:i43CD6AD1649191D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 754EEPS → DPRVR in AAL86770 (PubMed:12049647).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 159159Missing in isoform 2. 1 PublicationVSP_015620Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF462069 mRNA. Translation: AAL86770.1.
AJ489814 mRNA. Translation: CAD34015.1.
AK075765 mRNA. Translation: BAC35941.1.
AL591145 Genomic DNA. Translation: CAM23258.1.
CH466558 Genomic DNA. Translation: EDL34091.1.
BC057990 mRNA. Translation: AAH57990.1.
CCDSiCCDS25488.1. [Q8R4H7-1]
RefSeqiNP_665828.1. NM_145829.2. [Q8R4H7-1]
UniGeneiMm.31686.

Genome annotation databases

EnsembliENSMUST00000055409; ENSMUSP00000050258; ENSMUSG00000048217. [Q8R4H7-1]
GeneIDi217214.
KEGGimmu:217214.
UCSCiuc007lqp.2. mouse. [Q8R4H7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF462069 mRNA. Translation: AAL86770.1.
AJ489814 mRNA. Translation: CAD34015.1.
AK075765 mRNA. Translation: BAC35941.1.
AL591145 Genomic DNA. Translation: CAM23258.1.
CH466558 Genomic DNA. Translation: EDL34091.1.
BC057990 mRNA. Translation: AAH57990.1.
CCDSiCCDS25488.1. [Q8R4H7-1]
RefSeqiNP_665828.1. NM_145829.2. [Q8R4H7-1]
UniGeneiMm.31686.

3D structure databases

ProteinModelPortaliQ8R4H7.
SMRiQ8R4H7. Positions 91-521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000050258.

PTM databases

iPTMnetiQ8R4H7.
PhosphoSiteiQ8R4H7.

Proteomic databases

MaxQBiQ8R4H7.
PaxDbiQ8R4H7.
PeptideAtlasiQ8R4H7.
PRIDEiQ8R4H7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055409; ENSMUSP00000050258; ENSMUSG00000048217. [Q8R4H7-1]
GeneIDi217214.
KEGGimmu:217214.
UCSCiuc007lqp.2. mouse. [Q8R4H7-1]

Organism-specific databases

CTDi162417.
MGIiMGI:2387600. Nags.

Phylogenomic databases

eggNOGiKOG2436. Eukaryota.
COG0548. LUCA.
GeneTreeiENSGT00390000005602.
HOGENOMiHOG000007983.
HOVERGENiHBG080036.
InParanoidiQ8R4H7.
KOiK11067.
OMAiLTMEPVL.
OrthoDBiEOG77WWDH.
PhylomeDBiQ8R4H7.
TreeFamiTF332628.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00106.
BRENDAi2.3.1.1. 3474.
ReactomeiR-MMU-70635. Urea cycle.

Miscellaneous databases

PROiQ8R4H7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R4H7.
CleanExiMM_NAGS.
GenevisibleiQ8R4H7. MM.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR011243. GlcNAc_Synth_met.
IPR006855. Vertebrate-like_GNAT_dom.
[Graphical view]
PfamiPF04768. NAT. 1 hit.
[Graphical view]
PIRSFiPIRSF036442. NAGS_animal. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51731. GNAT_NAGS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, cloning and expression of the mouse N-acetylglutamate synthase gene."
    Caldovic L., Morizono H., Yu X., Thompson M., Shi D., Gallegos R., Allewell N.M., Malamy M.H., Tuchman M.
    Biochem. J. 364:825-831(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Liver.
  2. "Molecular characterization of the murine N-acetylglutamate synthase."
    Eckhardt M., Yaghootfam A., Gieselmann V.
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: 129/Ola.
    Tissue: Liver.
  3. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Liver.
  7. Cited for: PROTEIN SEQUENCE OF 51-527 AND 84-527, PROTEOLYTIC PROCESSING.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiNAGS_MOUSE
AccessioniPrimary (citable) accession number: Q8R4H7
Secondary accession number(s): B1AQG2
, Q8C6G6, Q8CI77, Q8K1R8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: July 6, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.