Carbamoyl-phosphate synthase [ammonia], mitochondrial precursor - Mus musculus (Mouse)

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Q8C196 (CPSM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Carbamoyl-phosphate synthase [ammonia], mitochondrial
EC=6.3.4.16

Alternative name(s):
Carbamoyl-phosphate synthetase I
Short name=CPSase I

Gene names

Name:

Cps1

Organism

Mus musculus (Mouse)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1500 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.
Catalytic activity	2 ATP + NH₃ + CO₂ + H₂O = 2 ADP + phosphate + carbamoyl phosphate.
Enzyme regulation	Requires N-acetyl-L-glutamate (NAG) as an allosteric activator By similarity.
Subcellular location	Mitochondrion By similarity.
Domain	The type-1 glutamine amidotransferase domain is defective By similarity.
Post-translational modification	Acetylation of Lys-287, Lys-603, Lys-841 and Lys-1291 is observed in liver mitochondria from fasted mice but not from fed mice.
Sequence similarities	Contains 2 ATP-grasp domains. Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	Urea cycle
Cellular component	Mitochondrion
Domain	Repeat Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	glutamine metabolic process Inferred from electronic annotation. Source: InterPro urea cycle Inferred by curator. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW carbamoyl-phosphate synthase (ammonia) activity Inferred from mutant phenotype. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Sirt5	Q8K2C6	2	EBI-2348828,EBI-2348809

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

38

Mitochondrion By similarity

Chain

1462

Carbamoyl-phosphate synthase [ammonia], mitochondrial By similarity

PRO_0000029898

Regions

Domain

186

Glutamine amidotransferase type-1

Domain

193

ATP-grasp 1

Domain

192

ATP-grasp 2

Region

180

Anthranilate phosphoribosyltransferase homolog

Sites

Binding site

1

Allosteric activator By similarity

Binding site

1

Allosteric activator By similarity

Binding site

1

Allosteric activator By similarity

Binding site

1

Allosteric activator By similarity

Binding site

1

Allosteric activator By similarity

Binding site

1

Allosteric activator By similarity

Amino acid modifications

Modified residue

1

N6-acetyllysine Ref.5

Modified residue

1

N6-acetyllysine Ref.5

Modified residue

1

N6-acetyllysine Ref.5

Modified residue

1

N6-acetyllysine Ref.5

Modified residue

1

N6-acetyllysine Ref.5

Modified residue

1

N6-acetyllysine Ref.5

Modified residue

1

N6-acetyllysine Ref.5

Modified residue

1

N6-acetyllysine Ref.5

Modified residue

1

Phosphoserine Ref.6

Modified residue

1

N6-acetyllysine Ref.5

Experimental info

Sequence conflict

4

LRLK → HASE in AAH67211. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q8C196 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 84A7268C1D7E8101
Show »

1,500

164,618

        10         20         30         40         50         60 
MTRILTACKV VKTLKSGFGF ANVTTKRQWD FSRPGIRLLS VKAKTAHIVL EDGTKMKGYS 

        70         80         90        100        110        120 
FGHPSSVAGE VVFNTGLGGY PEALTDPAYK GQILTMANPI IGNGGAPDTT ARDELGLNKY 

       130        140        150        160        170        180 
MESDGIKVAG LLVLNYSNDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML 

       190        200        210        220        230        240 
GKIEFEGQSV DFVDPNKQNL IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA 

       250        260        270        280        290        300 
EVHLVPWNHD FTQMEYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT 

       310        320        330        340        350        360 
GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT 

       370        380        390        400        410        420 
NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK GKGTTITSVL PKPALVASRV 

       430        440        450        460        470        480 
EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD 

       490        500        510        520        530        540 
AVYFLPITPQ FVTEVIKAER PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES 

       550        560        570        580        590        600 
IMATEDRQLF SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC 

       610        620        630        640        650        660 
PNKETLIDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT 

       670        680        690        700        710        720 
GDSVVVAPAQ TLSNAEFQML RRTSVNVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS 

       730        740        750        760        770        780 
RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR 

       790        800        810        820        830        840 
FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLK 

       850        860        870        880        890        900 
KELSEPSSTR IYAIAKALEN NMSLDEIVRL TSIDKWFLYK MRDILNMDKT LKGLNSDSVT 

       910        920        930        940        950        960 
EETLRKAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV 

       970        980        990       1000       1010       1020 
TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV 

      1030       1040       1050       1060       1070       1080 
STDFDECDKL YFEELSLERI LDIYHQEACN GCIISVGGQI PNNLAVPLYK NGVKIMGTSP 

      1090       1100       1110       1120       1130       1140 
LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN 

      1150       1160       1170       1180       1190       1200 
VVFSEDEMKR FLEEATRVSQ EHPVVLTKFV EGAREVEMDA VGKEGRVISH AISEHVEDAG 

      1210       1220       1230       1240       1250       1260 
VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA 

      1270       1280       1290       1300       1310       1320 
SRSFPFVSKT LGVDFIDVAT KVMIGESIDE KRLPTLEQPI IPSDYVAIKA PMFSWPRLRD 

      1330       1340       1350       1360       1370       1380 
ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ 

      1390       1400       1410       1420       1430       1440 
LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN 

      1450       1460       1470       1480       1490       1500 
NNTKFVHDNY VIRRTAVDSG IALLTNFQVT KLFAEAVQKS RTVDSKSLFH YRQYSAGKAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Liver.
[3]	Bienvenut W.V. Submitted (JUL-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 113-167; 183-207; 287-307; 317-328; 403-419; 459-522; 533-624; 631-638; 683-689; 729-740; 794-811; 815-826; 842-850; 857-880; 883-889; 893-905; 1030-1039; 1075-1085; 1090-1100; 1158-1168; 1175-1183; 1233-1259; 1270-1317; 1320-1326; 1349-1356; 1361-1387; 1429-1444 AND 1455-1479, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Liver.
[4]	"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. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 753-1500. Strain: C57BL/6J. Tissue: Skin.
[5]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-119; LYS-287; LYS-527; LYS-603; LYS-840; LYS-841; LYS-892 AND LYS-1291, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-898, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC101854 Genomic DNA. No translation available. AC133187 Genomic DNA. No translation available. BC067211 mRNA. Translation: AAH67211.1. BC126969 mRNA. Translation: AAI26970.1. AK028683 mRNA. Translation: BAC26064.1.
IPI	IPI00111908.
RefSeq	NP_001074278.1. NM_001080809.1.
UniGene	Mm.343942.
3D structure databases
ProteinModelPortal	Q8C196.
SMR	Q8C196. Positions 44-404, 416-819, 970-1478.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8C196. 2 interactions.
STRING	Q8C196.
PTM databases
PhosphoSite	Q8C196.
Proteomic databases
PRIDE	Q8C196.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027144; ENSMUSP00000027144; ENSMUSG00000025991.
GeneID	227231.
KEGG	mmu:227231.
UCSC	uc007biy.1. mouse.
Organism-specific databases
CTD	1373.
MGI	MGI:891996. Cps1.
Phylogenomic databases
HOGENOM	HBG405439.
HOVERGEN	HBG000279.
InParanoid	Q8C196.
OMA	DDKNAIR.
OrthoDB	EOG45MN4G.
PhylomeDB	Q8C196.
Gene expression databases
ArrayExpress	Q8C196.
Bgee	Q8C196.
CleanEx	MM_CPS1.
Genevestigator	Q8C196.
GermOnline	ENSMUSG00000025991. Mus musculus.
Family and domain databases
InterPro	IPR011761. ATP-grasp. IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR006275. CarbamoylP_synth_lsu. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR005483. CarbamoylP_synth_lsu_CPS-dom. IPR005481. CarbamoylP_synth_lsu_N. IPR005480. CarbamoylP_synth_lsu_oligo. IPR006274. CarbamoylP_synth_ssu. IPR002474. CarbamoylP_synth_ssu_N. IPR017926. GATASE_1. IPR011607. MGS-like_dom. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. [Graphical view]
Gene3D	G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 2 hits. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits. G3DSA:1.10.1030.10. CarbamoylP_synth_lsu_oligo. 1 hit. G3DSA:3.50.30.20. G3DSA:3.50.30.20. 1 hit. G3DSA:3.40.50.1380. MGS-like_dom. 1 hit. G3DSA:3.40.50.20. Pre-ATP_grasp. 2 hits.
KO	K01948.
Pfam	PF00289. CPSase_L_chain. 2 hits. PF02786. CPSase_L_D2. 2 hits. PF02787. CPSase_L_D3. 1 hit. PF00988. CPSase_sm_chain. 1 hit. PF00117. GATase. 1 hit. PF02142. MGS. 1 hit. [Graphical view]
PRINTS	PR00098. CPSASE.
SMART	SM01096. CPSase_L_D3. 1 hit. SM01097. CPSase_sm_chain. 1 hit. SM00851. MGS. 1 hit. [Graphical view]
SUPFAM	SSF48108. CarbamoylP_synth_lsu_oligo. 1 hit. SSF52021. CP_synthsmall. 1 hit. SSF52335. MGS-like_dom. 1 hit. SSF52440. PreATP-grasp-like. 2 hits.
TIGRFAMs	TIGR01369. CPSaseII_lrg. 1 hit. TIGR01368. CPSaseIIsmall. 1 hit.
PROSITE	PS50975. ATP_GRASP. 2 hits. PS00866. CPSASE_1. 2 hits. PS00867. CPSASE_2. 2 hits. PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	378522.
SOURCE	Search...

Entry information

Entry name

CPSM_MOUSE

Accession

Primary (citable) accession number: Q8C196
Secondary accession number(s): A0JNU4, Q6NX75

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	August 30, 2005
Last modified:	January 25, 2012
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents