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P11725 (OTC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ornithine carbamoyltransferase, mitochondrial

EC=2.1.3.3
Alternative name(s):
Ornithine transcarbamylase
Short name=OTCase
Gene names
Name:Otc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processAmino-acid biosynthesis
Arginine biosynthesis
Urea cycle
   Cellular componentMitochondrion
   DiseaseDisease mutation
   DomainTransit peptide
   Molecular functionTransferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanion homeostasis

Inferred from electronic annotation. Source: Ensembl

arginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

citrulline biosynthetic process

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

midgut development

Inferred from electronic annotation. Source: Ensembl

protein homotrimerization

Inferred from electronic annotation. Source: Ensembl

response to biotin

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

urea cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

   Molecular_functionamino acid binding

Inferred from electronic annotation. Source: Ensembl

ornithine carbamoyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphate ion binding

Inferred from electronic annotation. Source: Ensembl

phospholipid binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion
Chain33 – 354322Ornithine carbamoyltransferase, mitochondrial
PRO_0000020335

Regions

Region90 – 945Carbamoyl phosphate binding By similarity
Region263 – 2675Ornithine binding By similarity
Region302 – 3054Ornithine binding By similarity

Sites

Active site3031 By similarity
Binding site1411Carbamoyl phosphate By similarity
Binding site1411Ornithine By similarity
Binding site1681Carbamoyl phosphate By similarity
Binding site1991Ornithine By similarity
Binding site3301Carbamoyl phosphate By similarity
Binding site3301Ornithine By similarity

Amino acid modifications

Modified residue701N6-acetyllysine; alternate Ref.5
Modified residue701N6-succinyllysine; alternate Ref.4
Modified residue801N6-succinyllysine Ref.4
Modified residue881N6-acetyllysine; alternate Ref.5
Modified residue881N6-succinyllysine; alternate Ref.4
Modified residue1441N6-acetyllysine; alternate Ref.5
Modified residue1441N6-succinyllysine; alternate Ref.4
Modified residue2211N6-acetyllysine; alternate Ref.5
Modified residue2211N6-succinyllysine; alternate Ref.4
Modified residue2311N6-acetyllysine; alternate Ref.5
Modified residue2311N6-succinyllysine; alternate Ref.4
Modified residue2381N6-acetyllysine; alternate Ref.5
Modified residue2381N6-succinyllysine; alternate Ref.4
Modified residue2431N6-acetyllysine Ref.5
Modified residue2741N6-succinyllysine Ref.4
Modified residue2891N6-succinyllysine Ref.4
Modified residue2921N6-acetyllysine; alternate Ref.5
Modified residue2921N6-succinyllysine; alternate Ref.4
Modified residue3071N6-acetyllysine; alternate Ref.5
Modified residue3071N6-succinyllysine; alternate Ref.4

Natural variations

Natural variant1171H → N in spf. Ref.1

Experimental info

Sequence conflict1951G → R in CAA30121. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P11725 [UniParc].

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

FASTA35439,765
        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' 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]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-80; LYS-88; LYS-144; LYS-221; LYS-231; LYS-238; LYS-274; LYS-289; LYS-292 AND LYS-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-88; LYS-144; LYS-221; LYS-231; LYS-238; LYS-243; LYS-292 AND LYS-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 expand/collapse EMBL AC list , X07093, X07094, X07095, X07096, X07097, X07098, X07099, X07100 Genomic DNA. Translation: CAA30121.1.
CCDSCCDS30015.1.
PIROWMS. A43609.
RefSeqNP_032795.1. NM_008769.3.
UniGeneMm.2611.

3D structure databases

ProteinModelPortalP11725.
SMRP11725. Positions 34-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP11725. 2 interactions.
MINTMINT-1838977.
STRING10090.ENSMUSP00000056152.

PTM databases

PhosphoSiteP11725.

2D gel databases

SWISS-2DPAGEP11725.

Proteomic databases

MaxQBP11725.
PaxDbP11725.
PRIDEP11725.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049910; ENSMUSP00000056152; ENSMUSG00000031173.
GeneID18416.
KEGGmmu:18416.
UCSCuc009sqk.1. mouse.

Organism-specific databases

CTD5009.
MGIMGI:97448. Otc.

Phylogenomic databases

eggNOGCOG0078.
HOGENOMHOG000022686.
HOVERGENHBG007881.
InParanoidP11725.
KOK00611.
OMAKWAEQNA.
OrthoDBEOG7D85XC.
PhylomeDBP11725.
TreeFamTF352580.

Enzyme and pathway databases

UniPathwayUPA00158; UER00271.

Gene expression databases

ArrayExpressP11725.
BgeeP11725.
CleanExMM_OTC.
GenevestigatorP11725.

Family and domain databases

Gene3D3.40.50.1370. 2 hits.
InterProIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR002292. Orn/put_carbamltrans.
[Graphical view]
PfamPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSPR00100. AOTCASE.
PR00102. OTCASE.
SUPFAMSSF53671. SSF53671. 1 hit.
TIGRFAMsTIGR00658. orni_carb_tr. 1 hit.
PROSITEPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294052.
PROP11725.
SOURCESearch...

Entry information

Entry nameOTC_MOUSE
AccessionPrimary (citable) accession number: P11725
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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