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UniProtKB/Swiss-Prot entry P08955


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PYR1_MESAU
Primary accession number P08955
Secondary accession number P70108
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on August 1, 1992 (Sequence version 4)
Annotations were last modified on    September 2, 2008 (Entry version 92)
Name and origin of the protein
Protein name CAD protein
Synonyms None
Includes Glutamine-dependent carbamoyl-phosphate synthase
     (EC 6.3.5.5)
Aspartate carbamoyltransferase
     (EC 2.1.3.2)
Dihydroorotase
     (EC 3.5.2.3)
Gene name
Name: CAD
From
Mesocricetus auratus (Golden hamster) [TaxID: 10036] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Cricetidae; Cricetinae; Mesocricetus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-169.
PubMed=1671675 [NCBI, ExPASy, EBI, Israel, Japan]
Bein K., Simmer J.P., Evans D.R.;
"Molecular cloning of a cDNA encoding the amino end of the mammalian multifunctional protein CAD and analysis of the 5'-flanking region of the CAD gene.";
J. Biol. Chem. 266:3791-3799(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-73.
PubMed=1982061 [NCBI, ExPASy, EBI, Israel, Japan]
Farnham P.J., Kollmar R.;
"Characterization of the 5' end of the growth-regulated Syrian hamster CAD gene.";
Cell Growth Differ. 1:179-189(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 156-1455.
PubMed=1972379 [NCBI, ExPASy, EBI, Israel, Japan]
Simmer J.P., Kelly R.E., Rinker A.G. Jr., Scully J.L., Evans D.R.;
"Mammalian carbamyl phosphate synthetase (CPS). DNA sequence and evolution of the CPS domain of the Syrian hamster multifunctional protein CAD.";
J. Biol. Chem. 265:10395-10402(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 246-513.
DOI=10.1016/0006-291X(88)90246-X; PubMed=2900634 [NCBI, ExPASy, EBI, Israel, Japan]
Maley J.A., Davidson J.N.;
"Identification of the junction between the glutamine amidotransferase and carbamyl phosphate synthetase domains of the mammalian CAD protein.";
Biochem. Biophys. Res. Commun. 154:1047-1053(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1391-1870.
PubMed=1967494 [NCBI, ExPASy, EBI, Israel, Japan]
Simmer J.P., Kelly R.E., Rinker A.G. Jr., Zimmermann B.H., Scully J.L., Kim H., Evans D.R.;
"Mammalian dihydroorotase: nucleotide sequence, peptide sequences, and evolution of the dihydroorotase domain of the multifunctional protein CAD.";
Proc. Natl. Acad. Sci. U.S.A. 87:174-178(1990).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1403-2110.
DOI=10.1016/0378-1119(90)90399-C; PubMed=1979549 [NCBI, ExPASy, EBI, Israel, Japan]
Williams N.K., Simpson R.J., Moritz R.L., Peide Y., Crofts L., Minasian E., Leach S.J., Wake R.G., Christopherson R.I.;
"Location of the dihydroorotase domain within trifunctional hamster dihydroorotate synthetase.";
Gene 94:283-288(1990).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1774-2225.
PubMed=2543974 [NCBI, ExPASy, EBI, Israel, Japan]
Simmer J.P., Kelly R.E., Scully J.L., Grayson D.R., Rinker A.G. Jr., Bergh S.T., Evans D.R.;
"Mammalian aspartate transcarbamylase (ATCase): sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain.";
Proc. Natl. Acad. Sci. U.S.A. 86:4382-4386(1989).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 2074-2225.
PubMed=2862577 [NCBI, ExPASy, EBI, Israel, Japan]
Shigesada K., Stark G.R., Maley J.A., Niswander L.A., Davidson J.N.;
"Construction of a cDNA to the hamster CAD gene and its application toward defining the domain for aspartate transcarbamylase.";
Mol. Cell. Biol. 5:1735-1742(1985).
[9]
DOMAINS, AND PARTIAL PROTEIN SEQUENCE.
PubMed=1348059 [NCBI, ExPASy, EBI, Israel, Japan]
Kim H., Kelly R.E., Evans D.R.;
"The structural organization of the hamster multifunctional protein CAD. Controlled proteolysis, domains, and linkers.";
J. Biol. Chem. 267:7177-7184(1992).
[10]
3D-STRUCTURE MODELING OF ATCASE DOMAIN.
DOI=10.1002/prot.340090305; PubMed=2006137 [NCBI, ExPASy, EBI, Israel, Japan]
Scully J.L., Evans D.R.;
"Comparative modeling of mammalian aspartate transcarbamylase.";
Proteins 9:191-206(1991).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J05503; AAA37062.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M28866; AAA37073.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M60078; AAA63617.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11242; AAA37061.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M23652; AAA37064.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21927; AAA37063.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38653; A23443.
3D structure databases
HSSP P00479; 3CSU. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase P08955.
Protein family/group databases
MEROPS M38.972; -.
Ontologies
GO
GO:0004088; Molecular function: carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR006680; Amidohydro_1.
IPR006220; Anth_synthII.
IPR006130; Asp/Orn_carbamoyltranf.
IPR006132; Asp/Orn_carbamoyltranf_P_bd.
IPR006131; Asp_carbamoyltransf_Asp/Orn_bd.
IPR002082; Aspartate_carbamoyltransf_euk.
IPR011761; ATP-grasp.
IPR013816; ATP_grasp_subdomain_2.
IPR001317; CarbamoylP_synth_GATase.
IPR005483; CarbamoylP_synth_lsu.
IPR005479; CarbamoylP_synth_lsu_ATP-bd.
IPR006275; CarbamoylP_synth_lsu_Gln-dep.
IPR005481; CarbamoylP_synth_lsu_N.
IPR005480; CarbamoylP_synth_lsu_oligo.
IPR006274; CarbamoylP_synth_ssu.
IPR002474; CarbamoylP_synth_ssu_N.
IPR004722; DHOmult.
IPR002195; Dihydroorotase_CS.
IPR011702; GATASE.
IPR012998; GATase_1_AS.
IPR000991; GATase_class1_C.
IPR011607; MGS.
IPR013817; Pre-ATP_grasp.
Graphical view of domain structure.
Gene3D G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
G3DSA:3.40.50.20; Pre-ATP_grasp; 2.
Pfam PF01979; Amidohydro_1; 1.
PF00289; CPSase_L_chain; 2.
PF02786; CPSase_L_D2; 2.
PF02787; CPSase_L_D3; 1.
PF00988; CPSase_sm_chain; 1.
PF00117; GATase; 1.
PF02142; MGS; 1.
PF00185; OTCace; 1.
PF02729; OTCace_N; 1.
Pfam graphical view of domain structure.
PRINTS PR00097; ANTSNTHASEII.
PR00100; AOTCASE.
PR00101; ATCASE.
PR00098; CPSASE.
PR00099; CPSGATASE.
PR00096; GATASE.
TIGRFAMs TIGR00670; asp_carb_tr; 1.
TIGR01369; CPSaseII_lrg; 1.
TIGR01368; CPSaseIIsmall; 1.
TIGR00857; pyrC_multi; 1.
PROSITE PS50975; ATP_GRASP; 2.
PS00097; CARBAMOYLTRANSFERASE; 1.
PS00866; CPSASE_1; 2.
PS00867; CPSASE_2; 2.
PS00482; DIHYDROOROTASE_1; 1.
PS00483; DIHYDROOROTASE_2; 1.
PS51273; GATASE_TYPE_1; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P08955.
Phylogenomic databases
HOVERGEN P08955; -.
Other
ProtoNet P08955.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Allosteric enzyme; Cytoplasm; Direct protein sequencing; Hydrolase; Ligase; Metal-binding; Multifunctional enzyme; Phosphoprotein; Pyrimidine biosynthesis; Repeat; Transferase; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
INIT_MET   1      1        Removed (By similarity). 
CHAIN   2   2225  2224     CAD protein. PRO_0000199507
DOMAIN   177    363  187     Glutamine amidotransferase type-1. 
DOMAIN   519    711  193     ATP-grasp 1. 
DOMAIN   1052   1243  192     ATP-grasp 2. 
REGION   2    365  364     GATase (Glutamine amidotransferase). 
REGION   366    394  29     Linker. 
REGION   395   1455  1061     CPSase (Carbamoyl-phosphate synthase). 
REGION   395    933  539     CPSase A. 
REGION   934   1455  522     CPSase B. 
REGION   1456   1788  333     DHOase (dihydroorotase). 
REGION   1789   1917  129     Linker. 
REGION   1918   2225  308     ATCase (Aspartate transcarbamylase). 
ACT_SITE   252    252        For GATase activity (By similarity). 
ACT_SITE   336    336        For GATase activity (By similarity). 
ACT_SITE   338    338        For GATase activity (By similarity). 
METAL   1471   1471        Zinc (Potential). 
METAL   1473   1473        Zinc (Potential). 
MOD_RES   2      2        N-acetylalanine (By similarity). 
MOD_RES   1423   1423        Phosphoserine (By similarity). 
MOD_RES   1823   1823        Phosphoserine (By similarity). 
MOD_RES   1859   1859        Phosphoserine (By similarity). 
Sequence information
Length: 2225 AA [This is the length of the unprocessed precursor] Molecular weight: 243128 Da [This is the MW of the unprocessed precursor] CRC64: 9F6EBA9BD4C6EC5A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY 

        70         80         90        100        110        120 
GIPSDEEDEF GLSKWFESSE NHVAGLVVGE CCPTPSHWSA TCTLHEWLQQ HGIPGLQGVD 

       130        140        150        160        170        180 
TRELTKKLRE QGSLLGKLVQ SGTEPSTLPF VDPNARPLAP EVSIKTPRVF NAGGAPRICA 

       190        200        210        220        230        240 
LDCGLKYNQI RCLCQLGAEV TVVPWNHELD SQKYDGLFLS NGPGDPASYP GVVATLNRVL 

       250        260        270        280        290        300 
SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD 

       310        320        330        340        350        360 
ADSLPAGWTP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF DVFLETVREA 

       370        380        390        400        410        420 
VAGNPGGQTV KERLVQRLCP PGLLIPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI 

       430        440        450        460        470        480 
KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITPHYV TQVIRNERPD GVLLTFGGQT 

       490        500        510        520        530        540 
ALNCGVELTK AGVLARYGVR VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ 

       550        560        570        580        590        600 
AQAAAERLGY PVLVRAAFAL GGLGSGFAST KEELSALVAP AFAHTSQVLI DKSLKGWKEI 

       610        620        630        640        650        660 
EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRR TAIKVTQHLG 

       670        680        690        700        710        720 
IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA LGIPLPELRN 

       730        740        750        760        770        780 
SVTGGTAAFE PSLDYCVVKI PRWDLSKFLR VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL 

       790        800        810        820        830        840 
RMVDENCVGF DHTVKPVSDV ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM 

       850        860        870        880        890        900 
KRIVTHAQLL EQHRGQPLSQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV 

       910        920        930        940        950        960 
KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RTPHVLVLGS GVYRIGSSVE FDWCAVGCIQ 

       970        980        990       1000       1010       1020 
QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM DIYELENPDG VILSMGGQLP 

      1030       1040       1050       1060       1070       1080 
NNMAMALHRQ QCRVLGTSPE AIDSAENRFK FSRLLDTIGI SQPQWRELSD LESARQFCQT 

      1090       1100       1110       1120       1130       1140 
VGYPCVVRPS YVLSGAAMNV AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV 

      1150       1160       1170       1180       1190       1200 
ACDGVVSAIA ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN 

      1210       1220       1230       1240       1250       1260 
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPI GLMTGSGVVG 

      1270       1280       1290       1300       1310       1320 
VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL KAMLSTGFKI PKKNILLTIG 

      1330       1340       1350       1360       1370       1380 
SYKNKSELLP TVRLLESLGY SLYASLGTAD FYTEHGVKVT AVDWHFEEAV DGECPPQRSI 

      1390       1400       1410       1420       1430       1440 
LDQLAENHFE LVINLSMRGA GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL 

      1450       1460       1470       1480       1490       1500 
GQIGPAPPLK VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGVTMV 

      1510       1520       1530       1540       1550       1560 
CAMPNTRPPI IDAPALALAQ KLAEAGARCD FALFLGASSE NAGTLGAVAG SAAGLKLYLN 

      1570       1580       1590       1600       1610       1620 
ETFSELRLDS VAQWMEHFET WPSHLPIVAH AERQSVAAVL MVAQLTQRPV HICHVARKEE 

      1630       1640       1650       1660       1670       1680 
ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL ERLGPGRGEV RPELGSREDM EALWENMAVI 

      1690       1700       1710       1720       1730       1740 
DCFASDHAPH TLEEKCGPKP PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF 

      1750       1760       1770       1780       1790       1800 
HLPLQEDTYV EVDLEHEWTI PSHMPFSKAR WTPFEGQKVK GTIRRVVLRG EVAYIDGQVL 

      1810       1820       1830       1840       1850       1860 
VPPGYGQDVR KWPQGAVPQP PPSAPATTEI TTTPERPRRV IPGLPDGRFH LPPRIHRASD 

      1870       1880       1890       1900       1910       1920 
PGLPAEEPKE KPSRKVVEPE LMGTPDGPCY PAPPVPRQAS PQNLGSSGLL HPQTSPLLHS 

      1930       1940       1950       1960       1970       1980 
LVGQHILSVK QFTKDQMSHL FNVAHTLRMM VQKERSLDIL KGKVMASMFY EVSTRTSSSF 

      1990       2000       2010       2020       2030       2040 
AAAMARLGGA VLSFSEATSS VQKGESLADS VQTMSCYADV VVLRHPQPGA VELAAKHCRR 

      2050       2060       2070       2080       2090       2100 
PVINAGDGVG EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS 

      2110       2120       2130       2140       2150       2160 
LRYVAPPSLR MPPSVWDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE RFGSTQEYEA 

      2170       2180       2190       2200       2210       2220 
CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR AAYFRQAENG MYIRMALLAT 


VLGRF 

P08955 in FASTA format

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