OTC_BOVIN
ID OTC_BOVIN Reviewed; 354 AA.
AC Q9N1U7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Ornithine transcarbamylase, mitochondrial {ECO:0000250|UniProtKB:P00480};
DE Short=OTCase {ECO:0000250|UniProtKB:P00480};
DE EC=2.1.3.3 {ECO:0000250|UniProtKB:P00480};
DE AltName: Full=Ornithine carbamoyltransferase, mitochondrial {ECO:0000250|UniProtKB:P00480};
DE Flags: Precursor;
GN Name=OTC {ECO:0000250|UniProtKB:P00480};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shimogiri T., Koyanagi K., Mannen H., Tsuji S.;
RT "Ornithine transcarbamylase is expressed in uricotelic animals.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the second step of the urea cycle, the condensation
CC of carbamoyl phosphate with L-ornithine to form L-citrulline. The urea
CC cycle ensures the detoxification of ammonia by converting it to urea
CC for excretion. {ECO:0000250|UniProtKB:P00480}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:58228; EC=2.1.3.3;
CC Evidence={ECO:0000250|UniProtKB:P00480};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19515;
CC Evidence={ECO:0000250|UniProtKB:P00480};
CC -!- ACTIVITY REGULATION: Negatively regulated by lysine acetylation.
CC {ECO:0000250|UniProtKB:P00480}.
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-citrulline from L-ornithine
CC and carbamoyl phosphate: step 1/1. {ECO:0000250|UniProtKB:P00480}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P00480}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P00480}.
CC -!- PTM: Acetylation at Lys-88 negatively regulates ornithine
CC carbamoyltransferase activity in response to nutrient signals.
CC {ECO:0000250|UniProtKB:P00480}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; AF134841; AAF61405.1; -; mRNA.
DR RefSeq; NP_803453.1; NM_177487.2.
DR AlphaFoldDB; Q9N1U7; -.
DR SMR; Q9N1U7; -.
DR STRING; 9913.ENSBTAP00000001947; -.
DR PaxDb; Q9N1U7; -.
DR PeptideAtlas; Q9N1U7; -.
DR PRIDE; Q9N1U7; -.
DR GeneID; 280887; -.
DR KEGG; bta:280887; -.
DR CTD; 5009; -.
DR eggNOG; KOG1504; Eukaryota.
DR InParanoid; Q9N1U7; -.
DR OrthoDB; 1404554at2759; -.
DR SABIO-RK; Q9N1U7; -.
DR UniPathway; UPA00158; UER00271.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1370; -; 2.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
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 2: Evidence at transcript level;
KW Acetylation; Amino-acid biosynthesis; Arginine biosynthesis; Mitochondrion;
KW Phosphoprotein; Reference proteome; Transferase; Transit peptide;
KW Urea cycle.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT CHAIN 33..354
FT /note="Ornithine transcarbamylase, mitochondrial"
FT /id="PRO_0000245026"
FT ACT_SITE 263
FT /evidence="ECO:0000250"
FT ACT_SITE 303
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 70
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 80
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 88
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT MOD_RES 88
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT MOD_RES 144
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 144
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 221
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 221
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 231
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 231
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 238
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 238
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 274
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 289
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 292
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 292
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 307
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 307
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
SQ SEQUENCE 354 AA; 39842 MW; 30EAC2EF4AC1D71B CRC64;
MLFHLRTLLN NAALRNGHNF VVRNFRCGQP LQDKVQLKGR DLLTLKNFTG EEIKYMLWLS
ADLKFRIKQK GEYLPLLQGK SLGMIFEKRS TRTRLSTETG FALLGGHPCF LTTDDIHLGV
NESLTDTARV LSSMTDAVLA RVYKQSDLDL LAKEASIPIV NGLSDLYHPI QILADYLTLQ
EHYGSLKGLT LSWIGDGNNI LHSIMMSAAK FGMHLQVATP KGYEPDPSIT KMAEQYAKEN
GTKLSLTNDP LEAACGGNVL ITDTWISMGQ EEEKKKRLQA FQGYQVTMKT AKVAAPDWTF
LHCLPRKPEE VDDEVFYSPR SLVSPEAENR KWTIMAVMVS LLTDYSPQLQ KPKF
