PYR1_MOUSE
ID PYR1_MOUSE Reviewed; 2225 AA.
AC B2RQC6; B7ZN27;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=CAD protein;
DE Includes:
DE RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase;
DE EC=6.3.5.5 {ECO:0000250|UniProtKB:P27708};
DE Includes:
DE RecName: Full=Aspartate carbamoyltransferase;
DE EC=2.1.3.2 {ECO:0000250|UniProtKB:P27708};
DE Includes:
DE RecName: Full=Dihydroorotase;
DE EC=3.5.2.3 {ECO:0000250|UniProtKB:P27708};
GN Name=Cad;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1859, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: This protein is a 'fusion' protein encoding four enzymatic
CC activities of the pyrimidine pathway (GATase, CPSase, ATCase and
CC DHOase). {ECO:0000250|UniProtKB:P27708}.
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:0000250|UniProtKB:P27708};
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:0000250|UniProtKB:P27708};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC Evidence={ECO:0000250|UniProtKB:P27708};
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 activity).
CC {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 activator
CC while UMP and UTP are inhibitors of the CPSase reaction (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3.
CC -!- SUBUNIT: Homohexamer. Interacts with CIPC.
CC {ECO:0000250|UniProtKB:P27708}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Cytosolic and unphosphorylated in resting cells, translocates to
CC the nucleus in response to EGF stimulation, nuclear import promotes
CC optimal cell growth. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B2RQC6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B2RQC6-2; Sequence=VSP_053912;
CC -!- PTM: Activated by MAP kinase (Erk1/2) phosphorylation just prior to the
CC S phase of the cell cycle, when the demand for pyrimidine nucleotides
CC is greatest, and down-regulated as the cells emerge from S phase by
CC protein kinase A (PKA) phosphorylation. Phosphorylation at Ser-1859 by
CC RPS6KB1 downstream of MTOR promotes oligomerization and stimulates
CC dihydroorotase activity. Phosphorylation at Ser-1406 reduces
CC sensitivity to feedback inhibition by UTP (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: GATase (glutamine amidotransferase) and CPSase
CC (carbamoyl phosphate synthase) form together the glutamine-dependent
CC CPSase (GD-CPSase) (EC 6.3.5.5).
CC -!- SIMILARITY: In the central section; belongs to the metallo-dependent
CC hydrolases superfamily. DHOase family. CAD subfamily. {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; AC109608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466524; EDL37329.1; -; Genomic_DNA.
DR EMBL; BC137856; AAI37857.1; -; mRNA.
DR EMBL; BC144972; AAI44973.1; -; mRNA.
DR CCDS; CCDS19171.1; -. [B2RQC6-1]
DR CCDS; CCDS80246.1; -. [B2RQC6-2]
DR RefSeq; NP_001276451.1; NM_001289522.1. [B2RQC6-2]
DR RefSeq; NP_076014.1; NM_023525.2. [B2RQC6-1]
DR AlphaFoldDB; B2RQC6; -.
DR SMR; B2RQC6; -.
DR BioGRID; 213636; 15.
DR DIP; DIP-61412N; -.
DR IntAct; B2RQC6; 14.
DR MINT; B2RQC6; -.
DR STRING; 10090.ENSMUSP00000013773; -.
DR BindingDB; B2RQC6; -.
DR ChEMBL; CHEMBL2774; -.
DR iPTMnet; B2RQC6; -.
DR PhosphoSitePlus; B2RQC6; -.
DR SwissPalm; B2RQC6; -.
DR EPD; B2RQC6; -.
DR jPOST; B2RQC6; -.
DR MaxQB; B2RQC6; -.
DR PaxDb; B2RQC6; -.
DR PeptideAtlas; B2RQC6; -.
DR PRIDE; B2RQC6; -.
DR ProteomicsDB; 301985; -. [B2RQC6-1]
DR ProteomicsDB; 301986; -. [B2RQC6-2]
DR Antibodypedia; 28293; 329 antibodies from 35 providers.
DR DNASU; 69719; -.
DR Ensembl; ENSMUST00000013773; ENSMUSP00000013773; ENSMUSG00000013629. [B2RQC6-1]
DR Ensembl; ENSMUST00000201182; ENSMUSP00000144684; ENSMUSG00000013629. [B2RQC6-2]
DR GeneID; 69719; -.
DR KEGG; mmu:69719; -.
DR UCSC; uc008wwz.2; mouse. [B2RQC6-1]
DR UCSC; uc012duk.2; mouse. [B2RQC6-2]
DR CTD; 790; -.
DR MGI; MGI:1916969; Cad.
DR VEuPathDB; HostDB:ENSMUSG00000013629; -.
DR eggNOG; KOG0370; Eukaryota.
DR GeneTree; ENSGT00940000157241; -.
DR HOGENOM; CLU_000513_2_0_1; -.
DR InParanoid; B2RQC6; -.
DR OMA; IPCTSML; -.
DR OrthoDB; 273358at2759; -.
DR PhylomeDB; B2RQC6; -.
DR TreeFam; TF105604; -.
DR Reactome; R-MMU-500753; Pyrimidine biosynthesis.
DR SABIO-RK; B2RQC6; -.
DR UniPathway; UPA00070; UER00115.
DR UniPathway; UPA00070; UER00116.
DR UniPathway; UPA00070; UER00117.
DR BioGRID-ORCS; 69719; 28 hits in 77 CRISPR screens.
DR ChiTaRS; Cad; mouse.
DR PRO; PR:B2RQC6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; B2RQC6; protein.
DR Bgee; ENSMUSG00000013629; Expressed in internal carotid artery and 255 other tissues.
DR ExpressionAtlas; B2RQC6; baseline and differential.
DR Genevisible; B2RQC6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IDA:MGI.
DR GO; GO:0004151; F:dihydroorotase activity; IMP:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0002134; F:UTP binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; ISS:UniProtKB.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IMP:MGI.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006225; P:UDP biosynthetic process; ISO:MGI.
DR GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
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; 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; Alternative splicing; ATP-binding;
KW Cytoplasm; Glutamine amidotransferase; Hydrolase; Ligase; Magnesium;
KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Pyrimidine biosynthesis; Reference proteome;
KW Repeat; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT CHAIN 2..2225
FT /note="CAD protein"
FT /id="PRO_0000425955"
FT DOMAIN 177..363
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT DOMAIN 519..711
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 1052..1243
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 1308..1462
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 2..365
FT /note="GATase (Glutamine amidotransferase)"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 366..394
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 395..1455
FT /note="CPSase (Carbamoyl-phosphate synthase)"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 395..933
FT /note="CPSase A"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 934..1455
FT /note="CPSase B"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 1456..1788
FT /note="DHOase (dihydroorotase)"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 1789..1917
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT REGION 1815..1885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1918..2225
FT /note="ATCase (Aspartate transcarbamylase)"
FT /evidence="ECO:0000250|UniProtKB:P08955"
FT COMPBIAS 1850..1877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 252
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 336
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 338
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 545..600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 668
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 682
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 682
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 684
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1078..1135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 1471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1473
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1475
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1505
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1556
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1556
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /note="via carbamate group"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1590
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1614
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1637
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1661
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1686
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1686
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT BINDING 1690
FT /ligand="N-carbamoyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:32814"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 456
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 747
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 1038
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 1406
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 1411
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 1556
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 1859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1884
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 1900
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT MOD_RES 1938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27708"
FT VAR_SEQ 1962..2032
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053912"
SQ SEQUENCE 2225 AA; 243238 MW; E7E606A0F650ABB4 CRC64;
MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY
GIPSDEEDEF GLSKWFESSE IHVAGLVVGE CCPTPSHWSA NCTLHEWLQQ RGIPGLQGVD
TRELTKKLRE QGSLLGKLVQ KGTEPSALPF VDPNARPLAP EVSIKTPRVF NAGGAPRICA
LDCGLKYNQI RCLCQLGAEV TVVPWDHELD SQKYDGLFLS NGPGDPASYP GVVSTLSRVL
SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD
ADSLPAGWAP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF DVFLETVREA
AAGNIGGQTV RERLAQRLCP PELPIPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI
KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITLHYV 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 DHTVKPVSDM ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM
KRIVTHAQLL EQHRGQALPQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RAPHVLVLGS GVYRIGSSVE FDWCAVGCIQ
QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM DIYELENPEG VILSMGGQLP
NNMAMALHRQ QCRVLGTSPE AIDSAENRFK FSRLLDTIGI SQPQWRELSD LESARQFCHT
VGYPCVVRPS YVLSGAAMNV AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV
ACDGIVSAIA ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPV GLMTGSGVVG
VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL KAMLSTGFKI PEKNILLTIG
SYKNKSELLP TVRLLESLGY SLYASLGTAD FYTEHGVKVT AVDWHFEEAV DGECPPQRSI
LDQLAENHFE LVINLSMRGA GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL
GQIGPAPPLK VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGVTMV
CAMPNTRPPI IDAPALALAQ KLAEAGARCD FTLFLGASSE NAGTLGAVAG SAAGLKLYLN
ETFSELRLDS VAQWMEHFET WPAHLPIVAH AERQSVAAVL MVAQLTQRPV HICHVARKEE
ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL ERLGPGKGEV RPELGSREDM EALWENMAVI
DCFASDHAPH TLEEKCGPKP PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF
HLPLQEDTYV EVDLEHEWTV PSHMPFSKAR WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL
VPPGYGQDVR KWPQGVVPQP PPSTPATTEI TTTPERPRRV IPGLPDGRFH LPPRIHRASD
PGLPAEEPKE KPPRKVVEPE LMGTPDGPCY PAPPVPRQAS PQNLGSSGLL HPQMSPLLHS
LVGQHILSVK QFTKDQMSHL FNVAHTLRMM VQKERSLDIL KGKVMASMFY EVSTRTSSSF
AAAMARLGGA VLSFSEATSS VQKGESLADS VQTMSCYADV IVLRHPQPGA VELAAKHCRR
PVINAGDGVG EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
LRYVAPPSLR MPPSVRDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE RFGSVQEYEA
CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR AAYFRQAENG MYIRMALLAT
VLGRF
