Reviewed,
UniProtKB/Swiss-Prot P07756 (CPSM_RAT)
Last modified
October 13, 2009.
Version 90.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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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 |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
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 transcript 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-acetylglutamate as an allosteric activator. |
| Subcellular location | |
| Tissue specificity | Primarily in the liver and small intestine. |
| Domain | The type-1 glutamine amidotransferase domain is defective. |
| Post-translational modification | 50% of the mature protein that was isolated had Leu-39 as its N-terminal residue and 50% had Ser-40 suggesting two adjacent processing sites. However, the possibility of proteolytic removal of Leu-39 during the isolation of the enzyme cannot be excluded. |
| Sequence similarities | Contains 2 ATP-grasp domains. Contains 1 glutamine amidotransferase type-1 domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 38 | 38 | Mitochondrion | ||||||
| Chain | 39 – 1500 | 1462 | Carbamoyl-phosphate synthase [ammonia], mitochondrial | PRO_0000029899 | |||||
Regions | |||||||||
| Domain | 219 – 404 | 186 | Glutamine amidotransferase type-1 | ||||||
| Domain | 551 – 743 | 193 | ATP-grasp 1 | ||||||
| Domain | 1093 – 1284 | 192 | ATP-grasp 2 | ||||||
| Region | 39 – 218 | 180 | Anthranilate phosphoribosyltransferase homolog | ||||||
Amino acid modifications | |||||||||
| Modified residue | 55 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 119 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 287 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 527 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 603 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 841 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 892 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 898 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1291 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "Characterization and derivation of the gene coding for mitochondrial carbamyl phosphate synthetase I of rat." Nyunoya H., Broglie K.E., Widgren E.E., Lusty C.J. J. Biol. Chem. 260:9346-9356(1985) [PubMed: 2991241] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. |
| [2] | "Rat carbamyl-phosphate synthetase I gene. Promoter sequence and tissue-specific transcriptional regulation in vitro." Lagace M., Howell B.W., Burak R., Lusty C.J., Shore G.C. J. Biol. Chem. 262:10415-10418(1987) [PubMed: 3038878] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
M12335 M12328 Genomic DNA. Translation: AAB59717.1. J02805 Genomic DNA. Translation: AAA40959.1. | |
| IPI | IPI00210644. |
| PIR | SYRTCA. A28481. |
| RefSeq | NP_058768.1. |
| UniGene | Rn.53968 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1M6V based on UniProtKB P00968. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P07756. |
Protein family/group databases | |
| MEROPS | C26.951. |
PTM databases | |
| PhosphoSite | P07756. |
Proteomic databases | |
| PRIDE | P07756. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000019023; ENSRNOP00000019021; ENSRNOG00000013704; Rattus norvegicus. [Genome view] |
| GeneID | 497840. |
| KEGG | rno:497840. |
Organism-specific databases | |
| CTD | 497840. |
| RGD | 2395. Cps1. |
Phylogenomic databases | |
| HOVERGEN | P07756. |
Enzyme and pathway databases | |
| BRENDA | 6.3.4.16. 248. |
Gene expression databases | |
| ArrayExpress | P07756. |
| Genevestigator | P07756. |
| GermOnline | ENSRNOG00000013704. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR001317. CarbamoylP_synth_GATase. IPR005483. CarbamoylP_synth_lsu. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR006275. CarbamoylP_synth_lsu_Gln-dep. IPR005481. CarbamoylP_synth_lsu_N. IPR005480. CarbamoylP_synth_lsu_oligo. IPR006274. CarbamoylP_synth_ssu. IPR002474. CarbamoylP_synth_ssu_N. IPR017926. GATASE_1. IPR000991. GATase_class1_C. IPR011607. MGS. IPR013817. Pre-ATP_grasp. [Graphical view] |
| Gene3D | G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit. |
| 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. PR00099. CPSGATASE. |
| 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 Resources | |
| NextBio | 697797. |
Entry information
| Entry name | CPSM_RAT | ||||||||
| Accession | Primary (citable) accession number: P07756 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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