OTC_SHEEP
ID OTC_SHEEP Reviewed; 355 AA.
AC P84010; W5NRA6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Ornithine transcarbamylase, mitochondrial {ECO:0000305|PubMed:20809919};
DE Short=OTCase {ECO:0000303|PubMed:14527149};
DE EC=2.1.3.3 {ECO:0000250|UniProtKB:P00480};
DE AltName: Full=Ornithine carbamoyltransferase, mitochondrial;
DE Flags: Precursor;
GN Name=OTC {ECO:0000250|UniProtKB:P00480};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1] {ECO:0000312|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000312|Ensembl:ENSOARP00000000696};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 36-355, PROTEIN SEQUENCE OF 36-89,
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND TRANSIT PEPTIDE.
RC TISSUE=Liver {ECO:0000269|PubMed:14527149};
RX PubMed=14527149; DOI=10.1039/b304901a;
RA De Gregorio A., Battistutta R., Arena N., Panzalorto M., Francescato P.,
RA Valentini G., Bruno G., Zanotti G.;
RT "Functional and structural characterization of ovine ornithine
RT transcarbamoylase.";
RL Org. Biomol. Chem. 1:3178-3185(2003).
CC -!- FUNCTION: Catalyzes the second step of the urea cycle, the condensation
CC of carbamoyl phosphate with L-ornithine to form L-citrulline
CC (PubMed:14527149). The urea cycle ensures the detoxification of ammonia
CC by converting it to urea for excretion (Probable).
CC {ECO:0000269|PubMed:14527149, ECO:0000305}.
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:0000269|PubMed:14527149};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19515;
CC Evidence={ECO:0000305|PubMed:14527149};
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:0000305|PubMed:14527149}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:14527149}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P00480}.
CC -!- DOMAIN: Residues 88-96, 111-125 and 247-283 form flexible loops whose
CC positions are affected on substrate binding.
CC {ECO:0000303|PubMed:14527149}.
CC -!- PTM: Acetylation at Lys-89 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:0000269|PubMed:14527149}.
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DR EMBL; AMGL01114734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01114735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004022051.1; XM_004022002.3.
DR PDB; 1FB5; X-ray; 3.50 A; A=36-355.
DR PDBsum; 1FB5; -.
DR AlphaFoldDB; P84010; -.
DR SMR; P84010; -.
DR STRING; 9940.ENSOARP00000000696; -.
DR Ensembl; ENSOART00000000728; ENSOARP00000000696; ENSOARG00000000678.
DR Ensembl; ENSOART00020032796; ENSOARP00020027102; ENSOARG00020021238.
DR GeneID; 101102207; -.
DR KEGG; oas:101102207; -.
DR CTD; 5009; -.
DR eggNOG; KOG1504; Eukaryota.
DR HOGENOM; CLU_043846_3_0_1; -.
DR OMA; DGNNVCN; -.
DR OrthoDB; 1404554at2759; -.
DR UniPathway; UPA00158; UER00271.
DR EvolutionaryTrace; P84010; -.
DR Proteomes; UP000002356; Chromosome X.
DR Bgee; ENSOARG00000000678; Expressed in jejunum and 41 other tissues.
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:0097272; P:ammonium homeostasis; IEA:Ensembl.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019240; P:citrulline biosynthetic process; IEA:Ensembl.
DR GO; GO:0006593; P:ornithine catabolic process; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amino-acid biosynthesis; Arginine biosynthesis;
KW Direct protein sequencing; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transferase; Transit peptide; Urea cycle.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:14527149"
FT CHAIN 36..355
FT /note="Ornithine transcarbamylase, mitochondrial"
FT /id="PRO_0000113081"
FT ACT_SITE 304
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 91..95
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 264..268
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 303..306
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250"
FT MOD_RES 71
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 71
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 81
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 89
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT MOD_RES 89
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT MOD_RES 145
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 145
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 222
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 222
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 232
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 232
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 239
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 239
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 244
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 275
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 290
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 293
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 293
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 308
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT MOD_RES 308
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11725"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 51..69
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1FB5"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1FB5"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:1FB5"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 125..134
FT /evidence="ECO:0007829|PDB:1FB5"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:1FB5"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 170..184
FT /evidence="ECO:0007829|PDB:1FB5"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1FB5"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 228..241
FT /evidence="ECO:0007829|PDB:1FB5"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1FB5"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1FB5"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:1FB5"
FT TURN 273..277
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:1FB5"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:1FB5"
FT HELIX 324..343
FT /evidence="ECO:0007829|PDB:1FB5"
SQ SEQUENCE 355 AA; 39960 MW; 30A195B3D8B197F5 CRC64;
MLFINLRTLL NNAALRNGHN FVVRNFRCGQ PVQDKVQLKG RDLLTLKNFT GEEIKYMLWL
SADLKFRIKQ KGEYLPLLQG KSLGMIFEKR STRTRLSTET GFALLGGHPC FLTTDDIHLG
VNESLTDTAR VLSSMTDAVL ARVYKQSDLD ILAKEASIPI VNGLSDLYHP IQILADYLTL
QEHYGSLKGL TLSWIGDGNN ILHSIMMSAA KFGMHLQVAT PKGYEPDPSI TKLAEQYAKE
NGTKLSLTND PLEAACGGNV LITDTWISMG QEEEKKKRLQ AFQGYQVTMK TAKVAAPDWT
FLHCLPRKPE EVDDEVFYSP RSLVFPEAEN RKWTIMAVMV SLLTDYSPQL QKPKF
