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Database: UniProt
Entry: P08955
LinkDB: P08955
Original site: P08955 
ID   PYR1_MESAU              Reviewed;        2225 AA.
AC   P08955; P70108;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 4.
DT   05-DEC-2018, entry version 161.
DE   RecName: Full=CAD protein;
DE   Includes:
DE     RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase;
DE              EC=6.3.5.5 {ECO:0000269|PubMed:9218000};
DE   Includes:
DE     RecName: Full=Aspartate carbamoyltransferase;
DE              EC=2.1.3.2 {ECO:0000269|PubMed:9218000};
DE   Includes:
DE     RecName: Full=Dihydroorotase;
DE              EC=3.5.2.3 {ECO:0000269|PubMed:9218000};
GN   Name=CAD;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-169.
RX   PubMed=1671675;
RA   Bein K., Simmer J.P., Evans D.R.;
RT   "Molecular cloning of a cDNA encoding the amino end of the mammalian
RT   multifunctional protein CAD and analysis of the 5'-flanking region of
RT   the CAD gene.";
RL   J. Biol. Chem. 266:3791-3799(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-73.
RX   PubMed=1982061;
RA   Farnham P.J., Kollmar R.;
RT   "Characterization of the 5' end of the growth-regulated Syrian hamster
RT   CAD gene.";
RL   Cell Growth Differ. 1:179-189(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 156-1455.
RX   PubMed=1972379;
RA   Simmer J.P., Kelly R.E., Rinker A.G. Jr., Scully J.L., Evans D.R.;
RT   "Mammalian carbamyl phosphate synthetase (CPS). DNA sequence and
RT   evolution of the CPS domain of the Syrian hamster multifunctional
RT   protein CAD.";
RL   J. Biol. Chem. 265:10395-10402(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 246-513.
RX   PubMed=2900634; DOI=10.1016/0006-291X(88)90246-X;
RA   Maley J.A., Davidson J.N.;
RT   "Identification of the junction between the glutamine amidotransferase
RT   and carbamyl phosphate synthetase domains of the mammalian CAD
RT   protein.";
RL   Biochem. Biophys. Res. Commun. 154:1047-1053(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1391-1870.
RX   PubMed=1967494; DOI=10.1073/pnas.87.1.174;
RA   Simmer J.P., Kelly R.E., Rinker A.G. Jr., Zimmermann B.H.,
RA   Scully J.L., Kim H., Evans D.R.;
RT   "Mammalian dihydroorotase: nucleotide sequence, peptide sequences, and
RT   evolution of the dihydroorotase domain of the multifunctional protein
RT   CAD.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:174-178(1990).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1403-2110.
RX   PubMed=1979549; DOI=10.1016/0378-1119(90)90399-C;
RA   Williams N.K., Simpson R.J., Moritz R.L., Peide Y., Crofts L.,
RA   Minasian E., Leach S.J., Wake R.G., Christopherson R.I.;
RT   "Location of the dihydroorotase domain within trifunctional hamster
RT   dihydroorotate synthetase.";
RL   Gene 94:283-288(1990).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1774-2225.
RX   PubMed=2543974; DOI=10.1073/pnas.86.12.4382;
RA   Simmer J.P., Kelly R.E., Scully J.L., Grayson D.R., Rinker A.G. Jr.,
RA   Bergh S.T., Evans D.R.;
RT   "Mammalian aspartate transcarbamylase (ATCase): sequence of the ATCase
RT   domain and interdomain linker in the CAD multifunctional polypeptide
RT   and properties of the isolated domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:4382-4386(1989).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2074-2225.
RX   PubMed=2862577; DOI=10.1128/MCB.5.7.1735;
RA   Shigesada K., Stark G.R., Maley J.A., Niswander L.A., Davidson J.N.;
RT   "Construction of a cDNA to the hamster CAD gene and its application
RT   toward defining the domain for aspartate transcarbamylase.";
RL   Mol. Cell. Biol. 5:1735-1742(1985).
RN   [9]
RP   SUBUNIT.
RX   PubMed=2995985; DOI=10.1073/pnas.82.20.6802;
RA   Lee L., Kelly R.E., Pastra-Landis S.C., Evans D.R.;
RT   "Oligomeric structure of the multifunctional protein CAD that
RT   initiates pyrimidine biosynthesis in mammalian cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:6802-6806(1985).
RN   [10]
RP   DOMAINS, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1348059;
RA   Kim H., Kelly R.E., Evans D.R.;
RT   "The structural organization of the hamster multifunctional protein
RT   CAD. Controlled proteolysis, domains, and linkers.";
RL   J. Biol. Chem. 267:7177-7184(1992).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-1406, AND
RP   MUTAGENESIS OF SER-1406.
RX   PubMed=9218000; DOI=10.1007/BF02679954;
RA   Banerjei L.C., Davidson J.N.;
RT   "Site-directed substitution of Ser1406 of hamster CAD with glutamic
RT   acid alters allosteric regulation of carbamyl phosphate synthetase
RT   II.";
RL   Somat. Cell Mol. Genet. 23:37-49(1997).
RN   [12]
RP   3D-STRUCTURE MODELING OF ATCASE DOMAIN.
RX   PubMed=2006137; DOI=10.1002/prot.340090305;
RA   Scully J.L., Evans D.R.;
RT   "Comparative modeling of mammalian aspartate transcarbamylase.";
RL   Proteins 9:191-206(1991).
CC   -!- FUNCTION: This protein is a "fusion" protein encoding four
CC       enzymatic activities of the pyrimidine pathway (GATase, CPSase,
CC       ATCase and DHOase). {ECO:0000269|PubMed:9218000}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5;
CC         Evidence={ECO:0000269|PubMed:9218000};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC         aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58228; EC=2.1.3.2;
CC         Evidence={ECO:0000269|PubMed:9218000};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-
CC         aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814;
CC         EC=3.5.2.3; Evidence={ECO:0000269|PubMed:9218000};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P27708};
CC       Note=Binds 3 Zn(2+) ions per subunit (for dihydroorotase
CC       activity). {ECO:0000250|UniProtKB:P27708};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC       Note=Binds 4 magnesium or manganese ions per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU00409};
CC   -!- ACTIVITY REGULATION: Allosterically regulated and controlled by
CC       phosphorylation. 5-phosphoribose 1-diphosphate (PRPP) is an
CC       activator while UMP and UTP are inhibitors of the CPSase reaction.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC   -!- SUBUNIT: Homohexamer (PubMed:2995985). Interacts with CIPC (By
CC       similarity). {ECO:0000250|UniProtKB:P27708,
CC       ECO:0000269|PubMed:2995985}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC       Note=Cytosolic and unphosphorylated in resting cells, translocates
CC       to the nucleus in response to EGF stimulation, nuclear import
CC       promotes optimal cell growth. {ECO:0000250}.
CC   -!- PTM: Activated by MAP kinase (Erk1/2) phosphorylation just prior
CC       to the S phase of the cell cycle, when the demand for pyrimidine
CC       nucleotides is greatest, and down-regulated as the cells emerge
CC       from S phase by protein kinase A (PKA) phosphorylation.
CC       Phosphorylation at Ser-1859 by RPS6KB1 downstream of MTOR promotes
CC       oligomerization and stimulates dihydroorotase activity (By
CC       similarity). Phosphorylation at Ser-1406 reduces sensitivy to
CC       feedback inhibition by UTP. {ECO:0000250,
CC       ECO:0000269|PubMed:9218000}.
CC   -!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
CC       (carbamoyl phosphate synthase) form together the glutamine-
CC       dependent CPSase (GD-CPSase) (EC 6.3.5.5).
CC   -!- SIMILARITY: In the central section; belongs to the metallo-
CC       dependent hydrolases superfamily. DHOase family. CAD subfamily.
CC       {ECO:0000305}.
DR   EMBL; J05503; AAA37062.1; -; mRNA.
DR   EMBL; M28866; AAA37073.1; -; mRNA.
DR   EMBL; M60078; AAA63617.1; -; mRNA.
DR   EMBL; M11242; AAA37061.1; -; mRNA.
DR   EMBL; M23652; AAA37064.1; -; mRNA.
DR   EMBL; M21927; AAA37063.1; -; mRNA.
DR   PIR; A38653; A23443.
DR   ProteinModelPortal; P08955; -.
DR   SMR; P08955; -.
DR   MEROPS; M38.972; -.
DR   iPTMnet; P08955; -.
DR   PRIDE; P08955; -.
DR   HOVERGEN; HBG000279; -.
DR   BRENDA; 3.5.2.3; 3239.
DR   SABIO-RK; P08955; -.
DR   UniPathway; UPA00070; UER00115.
DR   UniPathway; UPA00070; UER00116.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000189706; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR   GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR   GO; GO:0016363; C:nuclear matrix; IDA:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0070335; F:aspartate binding; IDA:BHF-UCL.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IDA:BHF-UCL.
DR   GO; GO:0004151; F:dihydroorotase activity; IDA:BHF-UCL.
DR   GO; GO:0004672; F:protein kinase activity; IDA:BHF-UCL.
DR   GO; GO:0002134; F:UTP binding; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006541; P:glutamine metabolic process; IDA:BHF-UCL.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:BHF-UCL.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; -; 1.
DR   HAMAP; MF_00001; Asp_carb_tr; 1.
DR   HAMAP; MF_01209; CPSase_S_chain; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR002082; Asp_carbamoyltransf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR035686; CPSase_GATase1.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF02142; MGS; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   SUPFAM; SSF52021; SSF52021; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; ATP-binding; Complete proteome;
KW   Cytoplasm; Direct protein sequencing; Glutamine amidotransferase;
KW   Hydrolase; Ligase; Magnesium; Manganese; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Pyrimidine biosynthesis; Reference proteome; Repeat; Transferase;
KW   Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P27708}.
FT   CHAIN         2   2225       CAD protein.
FT                                /FTId=PRO_0000199507.
FT   DOMAIN      177    363       Glutamine amidotransferase type-1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT   DOMAIN      519    711       ATP-grasp 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN     1052   1243       ATP-grasp 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN     1308   1462       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     545    600       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND    1078   1135       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   REGION        2    365       GATase (Glutamine amidotransferase).
FT                                {ECO:0000303|PubMed:1348059}.
FT   REGION      366    394       Linker. {ECO:0000303|PubMed:1348059}.
FT   REGION      395   1455       CPSase (Carbamoyl-phosphate synthase).
FT                                {ECO:0000303|PubMed:1348059}.
FT   REGION      395    933       CPSase A. {ECO:0000303|PubMed:1348059}.
FT   REGION      934   1455       CPSase B. {ECO:0000303|PubMed:1348059}.
FT   REGION     1456   1788       DHOase (dihydroorotase).
FT                                {ECO:0000303|PubMed:1348059}.
FT   REGION     1789   1917       Linker. {ECO:0000303|PubMed:1348059}.
FT   REGION     1918   2225       ATCase (Aspartate transcarbamylase).
FT                                {ECO:0000303|PubMed:1348059}.
FT   ACT_SITE    252    252       Nucleophile; for GATase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT   ACT_SITE    336    336       For GATase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT   ACT_SITE    338    338       For GATase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00605}.
FT   METAL       668    668       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       682    682       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       682    682       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       684    684       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1202   1202       Magnesium or manganese 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1214   1214       Magnesium or manganese 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1214   1214       Magnesium or manganese 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1216   1216       Magnesium or manganese 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL      1471   1471       Zinc 1; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1471   1471       Zinc 2; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1473   1473       Zinc 1; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1556   1556       Zinc 1; via carbamate group.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1556   1556       Zinc 3; via carbamate group.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1590   1590       Zinc 3; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1613   1613       Zinc 2. {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1614   1614       Zinc 3; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1637   1637       Zinc 2. {ECO:0000250|UniProtKB:P27708}.
FT   METAL      1686   1686       Zinc 1. {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1475   1475       N-carbamoyl-L-aspartate.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1505   1505       N-carbamoyl-L-aspartate.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1661   1661       N-carbamoyl-L-aspartate; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1686   1686       N-carbamoyl-L-aspartate.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   BINDING    1690   1690       N-carbamoyl-L-aspartate.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES     456    456       Phosphothreonine; by MAPK1.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES     747    747       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES    1038   1038       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES    1406   1406       Phosphoserine; by PKA.
FT                                {ECO:0000269|PubMed:9218000}.
FT   MOD_RES    1411   1411       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES    1556   1556       N6-carboxylysine.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES    1859   1859       Phosphoserine; by RPS6KB1 and PKA.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES    1873   1873       Phosphoserine; by PKC; in vitro.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES    1884   1884       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES    1900   1900       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MOD_RES    1938   1938       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P27708}.
FT   MUTAGEN    1406   1406       S->A: No effect on enzyme kinetics.
FT                                {ECO:0000269|PubMed:9218000}.
FT   MUTAGEN    1406   1406       S->D: Increases CPSase activity and
FT                                reduces sensitivy to feedback inhibition
FT                                by UTP. {ECO:0000269|PubMed:9218000}.
SQ   SEQUENCE   2225 AA;  243128 MW;  9F6EBA9BD4C6EC5A CRC64;
     MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY
     GIPSDEEDEF GLSKWFESSE NHVAGLVVGE CCPTPSHWSA TCTLHEWLQQ HGIPGLQGVD
     TRELTKKLRE QGSLLGKLVQ SGTEPSTLPF VDPNARPLAP EVSIKTPRVF NAGGAPRICA
     LDCGLKYNQI RCLCQLGAEV TVVPWNHELD SQKYDGLFLS NGPGDPASYP GVVATLNRVL
     SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD
     ADSLPAGWTP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF DVFLETVREA
     VAGNPGGQTV KERLVQRLCP PGLLIPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI
     KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITPHYV TQVIRNERPD GVLLTFGGQT
     ALNCGVELTK AGVLARYGVR VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ
     AQAAAERLGY PVLVRAAFAL GGLGSGFAST KEELSALVAP AFAHTSQVLI DKSLKGWKEI
     EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRR TAIKVTQHLG
     IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA LGIPLPELRN
     SVTGGTAAFE PSLDYCVVKI PRWDLSKFLR VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL
     RMVDENCVGF DHTVKPVSDV ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM
     KRIVTHAQLL EQHRGQPLSQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
     KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RTPHVLVLGS GVYRIGSSVE FDWCAVGCIQ
     QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM DIYELENPDG VILSMGGQLP
     NNMAMALHRQ QCRVLGTSPE AIDSAENRFK FSRLLDTIGI SQPQWRELSD LESARQFCQT
     VGYPCVVRPS YVLSGAAMNV AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV
     ACDGVVSAIA ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN
     LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPI GLMTGSGVVG
     VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL KAMLSTGFKI PKKNILLTIG
     SYKNKSELLP TVRLLESLGY SLYASLGTAD FYTEHGVKVT AVDWHFEEAV DGECPPQRSI
     LDQLAENHFE LVINLSMRGA GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL
     GQIGPAPPLK VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGVTMV
     CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGAVAG SAAGLKLYLN
     ETFSELRLDS VAQWMEHFET WPSHLPIVAH AERQSVAAVL MVAQLTQRPV HICHVARKEE
     ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL ERLGPGRGEV RPELGSREDM EALWENMAVI
     DCFASDHAPH TLEEKCGPKP PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF
     HLPLQEDTYV EVDLEHEWTI PSHMPFSKAR WTPFEGQKVK GTIRRVVLRG EVAYIDGQVL
     VPPGYGQDVR KWPQGAVPQP PPSAPATTEI TTTPERPRRV IPGLPDGRFH LPPRIHRASD
     PGLPAEEPKE KPSRKVVEPE LMGTPDGPCY PAPPVPRQAS PQNLGSSGLL HPQTSPLLHS
     LVGQHILSVK QFTKDQMSHL FNVAHTLRMM VQKERSLDIL KGKVMASMFY EVSTRTSSSF
     AAAMARLGGA VLSFSEATSS VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR
     PVINAGDGVG EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
     LRYVAPPSLR MPPSVWDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE RFGSTQEYEA
     CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR AAYFRQAENG MYIRMALLAT
     VLGRF
//
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