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 06-JUL-2016, entry version 154. 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], VARIANT SPF ASN-117, AND DISEASE. RC STRAIN=C57BL/6J; RX 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 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 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [5] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-80; LYS-88; RP LYS-144; LYS-221; LYS-231; LYS-238; LYS-274; LYS-289; LYS-292 AND RP LYS-307, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-88; LYS-144; RP LYS-221; LYS-231; LYS-238; LYS-243; LYS-292 AND LYS-307, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23576753; DOI=10.1073/pnas.1302961110; RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., RA Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.; RT "Label-free quantitative proteomics of the lysine acetylome in RT mitochondria identifies substrates of SIRT3 in metabolic pathways."; RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013). CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate CC + L-citrulline. CC -!- ENZYME REGULATION: Negatively regulated by lysine acetylation. CC {ECO:0000250}. 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. CC {ECO:0000250}. 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 {ECO:0000269|PubMed:3603027}. CC -!- SIMILARITY: Belongs to the ATCase/OTCase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CCDS; CCDS30015.1; -. DR PIR; A43609; OWMS. DR RefSeq; NP_032795.1; NM_008769.4. DR UniGene; Mm.2611; -. DR ProteinModelPortal; P11725; -. DR SMR; P11725; 34-354. DR IntAct; P11725; 2. DR MINT; MINT-1838977; -. DR STRING; 10090.ENSMUSP00000056152; -. DR iPTMnet; P11725; -. DR PhosphoSite; P11725; -. DR SwissPalm; P11725; -. DR SWISS-2DPAGE; P11725; -. DR EPD; P11725; -. DR PaxDb; P11725; -. DR PeptideAtlas; P11725; -. DR PRIDE; P11725; -. DR Ensembl; ENSMUST00000049910; ENSMUSP00000056152; ENSMUSG00000031173. DR GeneID; 18416; -. DR KEGG; mmu:18416; -. DR UCSC; uc009sqk.1; mouse. DR CTD; 5009; -. DR MGI; MGI:97448; Otc. DR eggNOG; KOG1504; Eukaryota. DR eggNOG; COG0078; LUCA. DR HOGENOM; HOG000022686; -. DR HOVERGEN; HBG007881; -. DR InParanoid; P11725; -. DR KO; K00611; -. DR OMA; GNNMAHS; -. DR OrthoDB; EOG7D85XC; -. DR PhylomeDB; P11725; -. DR TreeFam; TF352580; -. DR Reactome; R-MMU-70635; Urea cycle. DR UniPathway; UPA00158; UER00271. DR PRO; PR:P11725; -. DR Proteomes; UP000000589; Chromosome X. DR Bgee; P11725; -. DR CleanEx; MM_OTC; -. DR ExpressionAtlas; P11725; baseline and differential. DR Genevisible; P11725; MM. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0016597; F:amino acid binding; IEA:Ensembl. DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; ISO:MGI. DR GO; GO:0042301; F:phosphate ion binding; IEA:Ensembl. DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl. DR GO; GO:0097272; P:ammonia homeostasis; ISO:MGI. DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central. DR GO; GO:0019240; P:citrulline biosynthetic process; ISO:MGI. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0007494; P:midgut development; IEA:Ensembl. DR GO; GO:0006593; P:ornithine catabolic process; ISO:MGI. DR GO; GO:0070207; P:protein homotrimerization; IEA:Ensembl. DR GO; GO:0070781; P:response to biotin; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl. DR GO; GO:0000050; P:urea cycle; ISO:MGI. DR Gene3D; 3.40.50.1370; -; 2. 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; SSF53671; 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; Phosphoprotein; 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. FT {ECO:0000250}. FT REGION 263 267 Ornithine binding. {ECO:0000250}. FT REGION 302 305 Ornithine binding. {ECO:0000250}. FT ACT_SITE 303 303 {ECO:0000250}. FT BINDING 141 141 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 141 141 Ornithine. {ECO:0000250}. FT BINDING 168 168 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 199 199 Ornithine. {ECO:0000250}. FT BINDING 330 330 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 330 330 Ornithine. {ECO:0000250}. FT MOD_RES 70 70 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23576753}. FT MOD_RES 70 70 N6-succinyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 80 80 N6-succinyllysine. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 88 88 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23576753}. FT MOD_RES 88 88 N6-succinyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 133 133 Phosphoserine. FT {ECO:0000250|UniProtKB:P00480}. FT MOD_RES 144 144 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23576753}. FT MOD_RES 144 144 N6-succinyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 221 221 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23576753}. FT MOD_RES 221 221 N6-succinyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 231 231 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23576753}. FT MOD_RES 231 231 N6-succinyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 238 238 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23576753}. FT MOD_RES 238 238 N6-succinyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 243 243 N6-acetyllysine. FT {ECO:0000244|PubMed:23576753}. FT MOD_RES 274 274 N6-succinyllysine. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 289 289 N6-succinyllysine. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 292 292 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23576753}. FT MOD_RES 292 292 N6-succinyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT MOD_RES 307 307 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:23576753}. FT MOD_RES 307 307 N6-succinyllysine; alternate. FT {ECO:0000244|PubMed:23806337}. FT VARIANT 117 117 H -> N (in spf). FT {ECO:0000269|PubMed:3603027}. FT CONFLICT 195 195 G -> R (in Ref. 2; CAA30121). FT {ECO:0000305}. 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 //