ID OTC_MOUSE Reviewed; 354 AA.
AC P11725;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 22-FEB-2012, entry version 116.
DE RecName: Full=Ornithine carbamoyltransferase, mitochondrial;
DE EC=2.1.3.3;
DE AltName: Full=Ornithine transcarbamylase;
DE Short=OTCase;
DE Flags: Precursor;
GN Name=Otc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-117.
RC STRAIN=C57BL/6J;
RX MEDLINE=87263407; PubMed=3603027; DOI=10.1126/science.3603027;
RA Veres G., Gibbs R.A., Scherer S.E., Caskey C.T.;
RT "The molecular basis of the sparse fur mouse mutation.";
RL Science 237:415-417(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=88157717; PubMed=2831503; DOI=10.1093/nar/16.4.1593;
RA Scherer S.E., Veres G., Caskey C.T.;
RT "The genetic structure of mouse ornithine transcarbamylase.";
RL Nucleic Acids Res. 16:1593-1601(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RC STRAIN=C57BL/6J;
RX MEDLINE=86224037; PubMed=3011788;
RA Veres G., Craigen W.J., Caskey C.T.;
RT "The 5' flanking region of the ornithine transcarbamylase gene
RT contains DNA sequences regulating tissue-specific expression.";
RL J. Biol. Chem. 261:7588-7591(1986).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-88; LYS-231 AND LYS-238, AND
RP MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT "Substrate and functional diversity of lysine acetylation revealed by
RT a proteomics survey.";
RL Mol. Cell 23:607-618(2006).
CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate
CC + L-citrulline.
CC -!- ENZYME REGULATION: Negatively regulated by lysine acetylation (By
CC similarity).
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-citrulline from L-
CC ornithine and carbamoyl phosphate: step 1/1.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- PTM: Acetylation at Lys-88 negatively regulates ornithine
CC carbamoyltransferase activity in response to nutrient signals (By
CC similarity).
CC -!- DISEASE: Note=Defects in Otc are the cause of the Sparse fur (spf)
CC phenotype. Spf mouse have an OTCase with an overall decrease in
CC activity, and altered substrate affinity.
CC -!- SIMILARITY: Belongs to the ATCase/OTCase family.
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DR EMBL; M17030; AAA39865.1; -; mRNA.
DR EMBL; M12716; AAA39864.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X07092; CAA30121.1; -; Genomic_DNA.
DR EMBL; X07093; CAA30121.1; JOINED; Genomic_DNA.
DR EMBL; X07094; CAA30121.1; JOINED; Genomic_DNA.
DR EMBL; X07095; CAA30121.1; JOINED; Genomic_DNA.
DR EMBL; X07096; CAA30121.1; JOINED; Genomic_DNA.
DR EMBL; X07097; CAA30121.1; JOINED; Genomic_DNA.
DR EMBL; X07098; CAA30121.1; JOINED; Genomic_DNA.
DR EMBL; X07099; CAA30121.1; JOINED; Genomic_DNA.
DR EMBL; X07100; CAA30121.1; JOINED; Genomic_DNA.
DR IPI; IPI00116603; -.
DR PIR; A43609; OWMS.
DR RefSeq; NP_032795.1; NM_008769.3.
DR UniGene; Mm.2611; -.
DR ProteinModelPortal; P11725; -.
DR SMR; P11725; 34-354.
DR STRING; P11725; -.
DR PhosphoSite; P11725; -.
DR SWISS-2DPAGE; P11725; -.
DR PRIDE; P11725; -.
DR Ensembl; ENSMUST00000049910; ENSMUSP00000056152; ENSMUSG00000031173.
DR GeneID; 18416; -.
DR KEGG; mmu:18416; -.
DR CTD; 5009; -.
DR MGI; MGI:97448; Otc.
DR eggNOG; COG0078; -.
DR GeneTree; ENSGT00510000047417; -.
DR HOGENOM; HBG579429; -.
DR HOVERGEN; HBG007881; -.
DR InParanoid; P11725; -.
DR KO; K00611; -.
DR OMA; KHLLSIK; -.
DR OrthoDB; EOG4GB76C; -.
DR PhylomeDB; P11725; -.
DR NextBio; 294052; -.
DR ArrayExpress; P11725; -.
DR Bgee; P11725; -.
DR CleanEx; MM_OTC; -.
DR Genevestigator; P11725; -.
DR GermOnline; ENSMUSG00000031173; Mus musculus.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-KW.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR InterPro; IPR002292; Orn/put_carbamltrans.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00102; OTCASE.
DR SUPFAM; SSF53671; Asp/Orn_carbamoyltranf; 1.
DR TIGRFAMs; TIGR00658; Orni_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Arginine biosynthesis;
KW Complete proteome; Disease mutation; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide; Urea cycle.
FT TRANSIT 1 32 Mitochondrion.
FT CHAIN 33 354 Ornithine carbamoyltransferase,
FT mitochondrial.
FT /FTId=PRO_0000020335.
FT REGION 90 94 Carbamoyl phosphate binding (By
FT similarity).
FT REGION 263 267 Ornithine binding (By similarity).
FT REGION 302 305 Ornithine binding (By similarity).
FT ACT_SITE 303 303 By similarity.
FT BINDING 141 141 Carbamoyl phosphate (By similarity).
FT BINDING 141 141 Ornithine (By similarity).
FT BINDING 168 168 Carbamoyl phosphate (By similarity).
FT BINDING 199 199 Ornithine (By similarity).
FT BINDING 330 330 Carbamoyl phosphate (By similarity).
FT BINDING 330 330 Ornithine (By similarity).
FT MOD_RES 88 88 N6-acetyllysine.
FT MOD_RES 231 231 N6-acetyllysine.
FT MOD_RES 238 238 N6-acetyllysine.
FT VARIANT 117 117 H -> N (in spf).
FT CONFLICT 195 195 G -> R (in Ref. 2; CAA30121).
SQ SEQUENCE 354 AA; 39765 MW; 33BBE5D1E88AA196 CRC64;
MLSNLRILLN NAALRKGHTS VVRHFWCGKP VQSQVQLKGR DLLTLKNFTG EEIQYMLWLS
ADLKFRIKQK GEYLPLLQGK SLGMIFEKRS TRTRLSTETG FALLGGHPSF LTTQDIHLGV
NESLTDTARV LSSMTDAVLA RVYKQSDLDT LAKEASIPIV NGLSDLYHPI QILADYLTLQ
EHYGSLKGLT LSWIGDGNNI LHSIMMSAAK FGMHLQAATP KGYEPDPNIV KLAEQYAKEN
GTKLSMTNDP LEAARGGNVL ITDTWISMGQ EDEKKKRLQA FQGYQVTMKT AKVAASDWTF
LHCLPRKPEE VDDEVFYSPR SLVFPEAENR KWTIMAVMVS LLTDYSPVLQ KPKF
//