Ornithine carbamoyltransferase, mitochondrial precursor

Contribute

Send feedback

Read comments (?) or add your own

P11725 (OTC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 125. History...

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

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

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

Names and origin

Protein names

Recommended name:
Ornithine carbamoyltransferase, mitochondrial
EC=2.1.3.3

Alternative name(s):
Ornithine transcarbamylase
Short name=OTCase

Gene names

Name:

Otc

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	354 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)

Catalytic activity	Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline.
Enzyme regulation	Negatively regulated by lysine acetylation By similarity.
Pathway	Nitrogen metabolism; urea cycle; L-citrulline from L-ornithine and carbamoyl phosphate: step 1/1.
Subunit structure	Homotrimer.
Subcellular location	Mitochondrion matrix.
Post-translational modification	Acetylation at Lys-88 negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals By similarity.
Involvement in disease	Defects in Otc are the cause of the Sparse fur (spf) phenotype. Spf mouse have an OTCase with an overall decrease in activity, and altered substrate affinity.
Sequence similarities	Belongs to the ATCase/OTCase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Urea cycle
Cellular component	Mitochondrion
Disease	Disease mutation
Domain	Transit peptide
Molecular function	Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anion homeostasis Inferred from electronic annotation. Source: Compara arginine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW citrulline biosynthetic process Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara midgut development Inferred from electronic annotation. Source: Compara protein homotrimerization Inferred from electronic annotation. Source: Compara response to biotin Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to insulin stimulus Inferred from electronic annotation. Source: Compara response to zinc ion Inferred from electronic annotation. Source: Compara urea cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrial inner membrane Inferred from direct assay PubMed 12865426. Source: MGI mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	amino acid binding Inferred from electronic annotation. Source: Compara ornithine carbamoyltransferase activity Inferred from electronic annotation. Source: EC phosphate ion binding Inferred from electronic annotation. Source: Compara phospholipid binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 32

Mitochondrion

Chain

33 – 354

322

Ornithine carbamoyltransferase, mitochondrial

PRO_0000020335

Regions

Region

90 – 94

Carbamoyl phosphate binding By similarity

Region

263 – 267

Ornithine binding By similarity

Region

302 – 305

Ornithine binding By similarity

Sites

Active site

303

By similarity

Binding site

141

Carbamoyl phosphate By similarity

Binding site

141

Ornithine By similarity

Binding site

168

Carbamoyl phosphate By similarity

Binding site

199

Ornithine By similarity

Binding site

330

Carbamoyl phosphate By similarity

Binding site

330

Ornithine By similarity

Amino acid modifications

Modified residue

N6-acetyllysine Ref.4

Modified residue

231

N6-acetyllysine Ref.4

Modified residue

238

N6-acetyllysine Ref.4

Natural variations

Natural variant

117

H → N in spf. Ref.1

Experimental info

Sequence conflict

195

G → R in CAA30121. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P11725 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 33BBE5D1E88AA196
Show »

FASTA

354

39,765

        10         20         30         40         50         60 
MLSNLRILLN NAALRKGHTS VVRHFWCGKP VQSQVQLKGR DLLTLKNFTG EEIQYMLWLS 

        70         80         90        100        110        120 
ADLKFRIKQK GEYLPLLQGK SLGMIFEKRS TRTRLSTETG FALLGGHPSF LTTQDIHLGV 

       130        140        150        160        170        180 
NESLTDTARV LSSMTDAVLA RVYKQSDLDT LAKEASIPIV NGLSDLYHPI QILADYLTLQ 

       190        200        210        220        230        240 
EHYGSLKGLT LSWIGDGNNI LHSIMMSAAK FGMHLQAATP KGYEPDPNIV KLAEQYAKEN 

       250        260        270        280        290        300 
GTKLSMTNDP LEAARGGNVL ITDTWISMGQ EDEKKKRLQA FQGYQVTMKT AKVAASDWTF 

       310        320        330        340        350 
LHCLPRKPEE VDDEVFYSPR SLVFPEAENR KWTIMAVMVS LLTDYSPVLQ KPKF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The molecular basis of the sparse fur mouse mutation." Veres G., Gibbs R.A., Scherer S.E., Caskey C.T. Science 237:415-417(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-117. Strain: C57BL/6J.
[2]	"The genetic structure of mouse ornithine transcarbamylase." Scherer S.E., Veres G., Caskey C.T. Nucleic Acids Res. 16:1593-1601(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The 5' flanking region of the ornithine transcarbamylase gene contains DNA sequences regulating tissue-specific expression." Veres G., Craigen W.J., Caskey C.T. J. Biol. Chem. 261:7588-7591(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26. Strain: C57BL/6J.
[4]	"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] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-88; LYS-231 AND LYS-238, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M17030 mRNA. Translation: AAA39865.1. M12716 Genomic DNA. Translation: AAA39864.1. Sequence problems. X07092 X07100 Genomic DNA. Translation: CAA30121.1.
IPI	IPI00116603.
PIR	OWMS. A43609.
RefSeq	NP_032795.1. NM_008769.3.
UniGene	Mm.2611.
3D structure databases
ProteinModelPortal	P11725.
SMR	P11725. Positions 34-354.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000056152.
PTM databases
PhosphoSite	P11725.
2D gel databases
SWISS-2DPAGE	P11725.
Proteomic databases
PaxDb	P11725.
PRIDE	P11725.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000049910; ENSMUSP00000056152; ENSMUSG00000031173.
GeneID	18416.
KEGG	mmu:18416.
Organism-specific databases
CTD	5009.
MGI	MGI:97448. Otc.
Phylogenomic databases
eggNOG	COG0078.
HOGENOM	HOG000022686.
HOVERGEN	HBG007881.
InParanoid	P11725.
KO	K00611.
OrthoDB	EOG4GB76C.
Enzyme and pathway databases
UniPathway	UPA00158; UER00271.
Gene expression databases
ArrayExpress	P11725.
Bgee	P11725.
CleanEx	MM_OTC.
Genevestigator	P11725.
GermOnline	ENSMUSG00000031173. Mus musculus.
Family and domain databases
InterPro	IPR006132. Asp/Orn_carbamoyltranf_P-bd. IPR006130. Asp/Orn_carbamoylTrfase. IPR006131. Asp_carbamoyltransf_Asp/Orn-bd. IPR002292. Orn/put_carbamltrans. [Graphical view]
Pfam	PF00185. OTCace. 1 hit. PF02729. OTCace_N. 1 hit. [Graphical view]
PRINTS	PR00100. AOTCASE. PR00102. OTCASE.
SUPFAM	SSF53671. Asp/Orn_carbamoyltranf. 1 hit.
TIGRFAMs	TIGR00658. orni_carb_tr. 1 hit.
PROSITE	PS00097. CARBAMOYLTRANSFERASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	294052.
SOURCE	Search...

Entry information

Entry name

OTC_MOUSE

Accession

Primary (citable) accession number: P11725

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	April 3, 2013
This is version 125 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents