P11725 · OTC_MOUSE
- ProteinOrnithine transcarbamylase, mitochondrial
- GeneOtc
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids354 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline. The urea cycle ensures the detoxification of ammonia by converting it to urea for excretion.
Catalytic activity
- carbamoyl phosphate + L-ornithine = H+ + L-citrulline + phosphateThis reaction proceeds in the backward direction.
Activity regulation
Negatively regulated by lysine acetylation.
Pathway
Nitrogen metabolism; urea cycle; L-citrulline from L-ornithine and carbamoyl phosphate: step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 90-94 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: STRTR | ||||||
Binding site | 141 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 141 | L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 168 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 199 | L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 263-267 | L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: DTWIS | ||||||
Binding site | 302-305 | L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: HCLP | ||||||
Active site | 303 | |||||
Sequence: C | ||||||
Binding site | 330 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 330 | L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Molecular Function | amino acid binding | |
Molecular Function | identical protein binding | |
Molecular Function | ornithine carbamoyltransferase activity | |
Molecular Function | phosphate ion binding | |
Molecular Function | phospholipid binding | |
Biological Process | ammonium homeostasis | |
Biological Process | arginine biosynthetic process via ornithine | |
Biological Process | citrulline biosynthetic process | |
Biological Process | liver development | |
Biological Process | midgut development | |
Biological Process | monoatomic anion homeostasis | |
Biological Process | ornithine catabolic process | |
Biological Process | ornithine metabolic process | |
Biological Process | response to biotin | |
Biological Process | response to insulin | |
Biological Process | response to xenobiotic stimulus | |
Biological Process | response to zinc ion | |
Biological Process | urea cycle |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameOrnithine transcarbamylase, mitochondrial
- EC number
- Short namesOTCase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP11725
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Involvement in disease
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 117 | in spf | ||||
Sequence: H → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 14 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-32 | Mitochondrion | ||||
Sequence: MLSNLRILLNNAALRKGHTSVVRHFWCGKPVQ | ||||||
Chain | PRO_0000020335 | 33-354 | Ornithine transcarbamylase, mitochondrial | |||
Sequence: SQVQLKGRDLLTLKNFTGEEIQYMLWLSADLKFRIKQKGEYLPLLQGKSLGMIFEKRSTRTRLSTETGFALLGGHPSFLTTQDIHLGVNESLTDTARVLSSMTDAVLARVYKQSDLDTLAKEASIPIVNGLSDLYHPIQILADYLTLQEHYGSLKGLTLSWIGDGNNILHSIMMSAAKFGMHLQAATPKGYEPDPNIVKLAEQYAKENGTKLSMTNDPLEAARGGNVLITDTWISMGQEDEKKKRLQAFQGYQVTMKTAKVAASDWTFLHCLPRKPEEVDDEVFYSPRSLVFPEAENRKWTIMAVMVSLLTDYSPVLQKPKF | ||||||
Modified residue | 70 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 70 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 80 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 88 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 88 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 133 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 144 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 144 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 221 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 221 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 231 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 231 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 238 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 238 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 243 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 274 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 289 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 292 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 292 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 307 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 307 | N6-succinyllysine; alternate | ||||
Sequence: K |
Post-translational modification
Acetylation at Lys-88 negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length354
- Mass (Da)39,765
- Last updated1989-10-01 v1
- Checksum33BBE5D1E88AA196
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q8R1A8 | Q8R1A8_MOUSE | Otc | 351 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 195 | in Ref. 2; CAA30121 | ||||
Sequence: G → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M17030 EMBL· GenBank· DDBJ | AAA39865.1 EMBL· GenBank· DDBJ | mRNA | ||
M12716 EMBL· GenBank· DDBJ | AAA39864.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
X07092 EMBL· GenBank· DDBJ | CAA30121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X07093 EMBL· GenBank· DDBJ | CAA30121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X07094 EMBL· GenBank· DDBJ | CAA30121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X07095 EMBL· GenBank· DDBJ | CAA30121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X07096 EMBL· GenBank· DDBJ | CAA30121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X07097 EMBL· GenBank· DDBJ | CAA30121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X07098 EMBL· GenBank· DDBJ | CAA30121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X07099 EMBL· GenBank· DDBJ | CAA30121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X07100 EMBL· GenBank· DDBJ | CAA30121.1 EMBL· GenBank· DDBJ | Genomic DNA |