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Protein

Ornithine carbamoyltransferase, mitochondrial

Gene

Otc

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline.

Enzyme regulationi

Negatively regulated by lysine acetylation.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411Carbamoyl phosphateBy similarity
Binding sitei141 – 1411OrnithineBy similarity
Binding sitei168 – 1681Carbamoyl phosphateBy similarity
Binding sitei199 – 1991OrnithineBy similarity
Active sitei303 – 3031By similarity
Binding sitei330 – 3301Carbamoyl phosphateBy similarity
Binding sitei330 – 3301OrnithineBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Urea cycle

Enzyme and pathway databases

ReactomeiREACT_315699. Urea cycle.
UniPathwayiUPA00158; UER00271.

Names & Taxonomyi

Protein namesi
Recommended name:
Ornithine carbamoyltransferase, mitochondrial (EC:2.1.3.3)
Alternative name(s):
Ornithine transcarbamylase
Short name:
OTCase
Gene namesi
Name:Otc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:97448. Otc.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: MGI
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

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.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232MitochondrionAdd
BLAST
Chaini33 – 354322Ornithine carbamoyltransferase, mitochondrialPRO_0000020335Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysine; alternate1 Publication
Modified residuei70 – 701N6-succinyllysine; alternate1 Publication
Modified residuei80 – 801N6-succinyllysine1 Publication
Modified residuei88 – 881N6-acetyllysine; alternate1 Publication
Modified residuei88 – 881N6-succinyllysine; alternate1 Publication
Modified residuei133 – 1331PhosphoserineBy similarity
Modified residuei144 – 1441N6-acetyllysine; alternate1 Publication
Modified residuei144 – 1441N6-succinyllysine; alternate1 Publication
Modified residuei221 – 2211N6-acetyllysine; alternate1 Publication
Modified residuei221 – 2211N6-succinyllysine; alternate1 Publication
Modified residuei231 – 2311N6-acetyllysine; alternate1 Publication
Modified residuei231 – 2311N6-succinyllysine; alternate1 Publication
Modified residuei238 – 2381N6-acetyllysine; alternate1 Publication
Modified residuei238 – 2381N6-succinyllysine; alternate1 Publication
Modified residuei243 – 2431N6-acetyllysine1 Publication
Modified residuei274 – 2741N6-succinyllysine1 Publication
Modified residuei289 – 2891N6-succinyllysine1 Publication
Modified residuei292 – 2921N6-acetyllysine; alternate1 Publication
Modified residuei292 – 2921N6-succinyllysine; alternate1 Publication
Modified residuei307 – 3071N6-acetyllysine; alternate1 Publication
Modified residuei307 – 3071N6-succinyllysine; alternate1 Publication

Post-translational modificationi

Acetylation at Lys-88 negatively regulates ornithine carbamoyltransferase activity in response to nutrient signals.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP11725.
PaxDbiP11725.
PRIDEiP11725.

2D gel databases

SWISS-2DPAGEP11725.

PTM databases

PhosphoSiteiP11725.

Expressioni

Gene expression databases

BgeeiP11725.
CleanExiMM_OTC.
ExpressionAtlasiP11725. baseline and differential.
GenevestigatoriP11725.

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

IntActiP11725. 2 interactions.
MINTiMINT-1838977.
STRINGi10090.ENSMUSP00000056152.

Structurei

3D structure databases

ProteinModelPortaliP11725.
SMRiP11725. Positions 34-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni90 – 945Carbamoyl phosphate bindingBy similarity
Regioni263 – 2675Ornithine bindingBy similarity
Regioni302 – 3054Ornithine bindingBy similarity

Sequence similaritiesi

Belongs to the ATCase/OTCase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0078.
HOGENOMiHOG000022686.
HOVERGENiHBG007881.
InParanoidiP11725.
KOiK00611.
OMAiGNNVCNS.
OrthoDBiEOG7D85XC.
PhylomeDBiP11725.
TreeFamiTF352580.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR002292. Orn/put_carbamltrans.
[Graphical view]
PfamiPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSiPR00100. AOTCASE.
PR00102. OTCASE.
SUPFAMiSSF53671. SSF53671. 1 hit.
TIGRFAMsiTIGR00658. orni_carb_tr. 1 hit.
PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11725-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSNLRILLN NAALRKGHTS VVRHFWCGKP VQSQVQLKGR DLLTLKNFTG
60 70 80 90 100
EEIQYMLWLS ADLKFRIKQK GEYLPLLQGK SLGMIFEKRS TRTRLSTETG
110 120 130 140 150
FALLGGHPSF LTTQDIHLGV NESLTDTARV LSSMTDAVLA RVYKQSDLDT
160 170 180 190 200
LAKEASIPIV NGLSDLYHPI QILADYLTLQ EHYGSLKGLT LSWIGDGNNI
210 220 230 240 250
LHSIMMSAAK FGMHLQAATP KGYEPDPNIV KLAEQYAKEN GTKLSMTNDP
260 270 280 290 300
LEAARGGNVL ITDTWISMGQ EDEKKKRLQA FQGYQVTMKT AKVAASDWTF
310 320 330 340 350
LHCLPRKPEE VDDEVFYSPR SLVFPEAENR KWTIMAVMVS LLTDYSPVLQ

KPKF
Length:354
Mass (Da):39,765
Last modified:October 1, 1989 - v1
Checksum:i33BBE5D1E88AA196
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951G → R in CAA30121 (PubMed:2831503).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti117 – 1171H → N in spf. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17030 mRNA. Translation: AAA39865.1.
M12716 Genomic DNA. Translation: AAA39864.1. Sequence problems.
X07092
, X07093, X07094, X07095, X07096, X07097, X07098, X07099, X07100 Genomic DNA. Translation: CAA30121.1.
CCDSiCCDS30015.1.
PIRiA43609. OWMS.
RefSeqiNP_032795.1. NM_008769.3.
UniGeneiMm.2611.

Genome annotation databases

EnsembliENSMUST00000049910; ENSMUSP00000056152; ENSMUSG00000031173.
GeneIDi18416.
KEGGimmu:18416.
UCSCiuc009sqk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17030 mRNA. Translation: AAA39865.1.
M12716 Genomic DNA. Translation: AAA39864.1. Sequence problems.
X07092
, X07093, X07094, X07095, X07096, X07097, X07098, X07099, X07100 Genomic DNA. Translation: CAA30121.1.
CCDSiCCDS30015.1.
PIRiA43609. OWMS.
RefSeqiNP_032795.1. NM_008769.3.
UniGeneiMm.2611.

3D structure databases

ProteinModelPortaliP11725.
SMRiP11725. Positions 34-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11725. 2 interactions.
MINTiMINT-1838977.
STRINGi10090.ENSMUSP00000056152.

PTM databases

PhosphoSiteiP11725.

2D gel databases

SWISS-2DPAGEP11725.

Proteomic databases

MaxQBiP11725.
PaxDbiP11725.
PRIDEiP11725.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049910; ENSMUSP00000056152; ENSMUSG00000031173.
GeneIDi18416.
KEGGimmu:18416.
UCSCiuc009sqk.1. mouse.

Organism-specific databases

CTDi5009.
MGIiMGI:97448. Otc.

Phylogenomic databases

eggNOGiCOG0078.
HOGENOMiHOG000022686.
HOVERGENiHBG007881.
InParanoidiP11725.
KOiK00611.
OMAiGNNVCNS.
OrthoDBiEOG7D85XC.
PhylomeDBiP11725.
TreeFamiTF352580.

Enzyme and pathway databases

UniPathwayiUPA00158; UER00271.
ReactomeiREACT_315699. Urea cycle.

Miscellaneous databases

NextBioi294052.
PROiP11725.
SOURCEiSearch...

Gene expression databases

BgeeiP11725.
CleanExiMM_OTC.
ExpressionAtlasiP11725. baseline and differential.
GenevestigatoriP11725.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR002292. Orn/put_carbamltrans.
[Graphical view]
PfamiPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSiPR00100. AOTCASE.
PR00102. OTCASE.
SUPFAMiSSF53671. SSF53671. 1 hit.
TIGRFAMsiTIGR00658. orni_carb_tr. 1 hit.
PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiOTC_MOUSE
AccessioniPrimary (citable) accession number: P11725
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: April 1, 2015
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.