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B2RQC6

- PYR1_MOUSE

UniProt

B2RQC6 - PYR1_MOUSE

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Protein

CAD protein

Gene

Cad

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).By similarity

Catalytic activityi

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.

Cofactori

Binds 3 zinc ions per subunit (for dihydroorotase activity).By similarity

Enzyme regulationi

Allosterically regulated and controlled by phosphorylation. 5-phosphoribose 1-diphosphate (PRPP) is an activator while UMP and UTP are inhibitors of the CPSase reaction (By similarity).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei252 – 2521For GATase activityBy similarity
Active sitei336 – 3361For GATase activityBy similarity
Active sitei338 – 3381For GATase activityBy similarity
Metal bindingi1471 – 14711Zinc 1; via tele nitrogenBy similarity
Metal bindingi1471 – 14711Zinc 2; via pros nitrogenBy similarity
Metal bindingi1473 – 14731Zinc 1; via tele nitrogenBy similarity
Binding sitei1475 – 14751N-carbamoyl-L-aspartateBy similarity
Binding sitei1505 – 15051N-carbamoyl-L-aspartateBy similarity
Metal bindingi1556 – 15561Zinc 1; via carbamate groupBy similarity
Metal bindingi1556 – 15561Zinc 3; via carbamate groupBy similarity
Metal bindingi1590 – 15901Zinc 3; via pros nitrogenBy similarity
Metal bindingi1613 – 16131Zinc 2By similarity
Metal bindingi1614 – 16141Zinc 3; via tele nitrogenBy similarity
Metal bindingi1637 – 16371Zinc 2By similarity
Binding sitei1661 – 16611N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi1686 – 16861Zinc 1By similarity
Binding sitei1686 – 16861N-carbamoyl-L-aspartateBy similarity
Binding sitei1690 – 16901N-carbamoyl-L-aspartateBy similarity

GO - Molecular functioni

  1. amino acid binding Source: InterPro
  2. aspartate carbamoyltransferase activity Source: UniProtKB-EC
  3. ATP binding Source: UniProtKB-KW
  4. carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
  5. dihydroorotase activity Source: UniProtKB
  6. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. 'de novo' pyrimidine nucleobase biosynthetic process Source: UniProtKB
  2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  3. carbamoyl phosphate biosynthetic process Source: InterPro
  4. cellular response to drug Source: Ensembl
  5. cellular response to epidermal growth factor stimulus Source: Ensembl
  6. drug metabolic process Source: Ensembl
  7. embryo development Source: Ensembl
  8. female pregnancy Source: Ensembl
  9. glutamine catabolic process Source: InterPro
  10. lactation Source: Ensembl
  11. organ regeneration Source: Ensembl
  12. response to amine Source: Ensembl
  13. response to caffeine Source: Ensembl
  14. response to cortisol Source: Ensembl
  15. response to testosterone Source: Ensembl
  16. UTP biosynthetic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Ligase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00070; UER00115.
UPA00070; UER00116.
UPA00070; UER00117.

Names & Taxonomyi

Protein namesi
Recommended name:
CAD protein
Including the following 3 domains:
Glutamine-dependent carbamoyl-phosphate synthase (EC:6.3.5.5)
Aspartate carbamoyltransferase (EC:2.1.3.2)
Dihydroorotase (EC:3.5.2.3)
Gene namesi
Name:Cad
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1916969. Cad.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: Cytosolic and unphosphorylated in resting cells, translocates to the nucleus in response to EGF stimulation, nuclear import promotes optimal cell growth.By similarity

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. neuronal cell body Source: Ensembl
  4. nuclear matrix Source: Ensembl
  5. protein complex Source: Ensembl
  6. terminal bouton Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 22252224CAD proteinPRO_0000425955Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei456 – 4561Phosphothreonine; by MAPK1By similarity
Modified residuei747 – 7471N6-acetyllysineBy similarity
Modified residuei1406 – 14061Phosphoserine; by PKABy similarity
Modified residuei1411 – 14111N6-acetyllysineBy similarity
Modified residuei1556 – 15561N6-carboxylysineBy similarity
Modified residuei1859 – 18591Phosphoserine; by RPS6KB1 and PKABy similarity
Modified residuei1884 – 18841PhosphothreonineBy similarity
Modified residuei1900 – 19001PhosphoserineBy similarity

Post-translational modificationi

Activated by MAP kinase (Erk1/2) phosphorylation just prior to the S phase of the cell cycle, when the demand for pyrimidine nucleotides is greatest, and down-regulated as the cells emerge from S phase by protein kinase A (PKA) phosphorylation. Phosphorylation at Ser-1859 by RPS6KB1 downstream of MTOR promotes oligomerization and stimulates dihydroorotase activity. Phosphorylation at Ser-1406 reduces sensitivy to feedback inhibition by UTP (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiB2RQC6.

Expressioni

Gene expression databases

ExpressionAtlasiB2RQC6. baseline and differential.
GenevestigatoriB2RQC6.

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

IntActiB2RQC6. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliB2RQC6.
SMRiB2RQC6. Positions 1460-1823.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini177 – 363187Glutamine amidotransferase type-1Add
BLAST
Domaini519 – 711193ATP-grasp 1Add
BLAST
Domaini1052 – 1243192ATP-grasp 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 365364GATase (Glutamine amidotransferase)Add
BLAST
Regioni366 – 39429LinkerAdd
BLAST
Regioni395 – 14551061CPSase (Carbamoyl-phosphate synthase)Add
BLAST
Regioni395 – 933539CPSase AAdd
BLAST
Regioni934 – 1455522CPSase BAdd
BLAST
Regioni1456 – 1788333DHOase (dihydroorotase)Add
BLAST
Regioni1789 – 1917129LinkerAdd
BLAST
Regioni1918 – 2225308ATCase (Aspartate transcarbamylase)Add
BLAST

Sequence similaritiesi

In the central section; belongs to the DHOase family.Curated
Contains 2 ATP-grasp domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0458.
GeneTreeiENSGT00390000015604.
HOGENOMiHOG000234584.
HOVERGENiHBG000279.
InParanoidiB2RQC6.
KOiK11540.
OMAiKRIVTHA.
OrthoDBiEOG7M6D6F.
PhylomeDBiB2RQC6.
TreeFamiTF105604.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1370. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_00001. Asp_carb_tr.
MF_01209. CPSase_S_chain.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR029062. Class_I_gatase-like.
IPR002195. Dihydroorotase_CS.
IPR017926. GATASE.
IPR011059. Metal-dep_hydrolase_composite.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
PF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
PF02142. MGS. 1 hit.
PF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSiPR00100. AOTCASE.
PR00101. ATCASE.
PR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF51338. SSF51338. 1 hit.
SSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
SSF53671. SSF53671. 1 hit.
TIGRFAMsiTIGR00670. asp_carb_tr. 1 hit.
TIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00097. CARBAMOYLTRANSFERASE. 1 hit.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: B2RQC6-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL
60 70 80 90 100
VLTYPLIGNY GIPSDEEDEF GLSKWFESSE IHVAGLVVGE CCPTPSHWSA
110 120 130 140 150
NCTLHEWLQQ RGIPGLQGVD TRELTKKLRE QGSLLGKLVQ KGTEPSALPF
160 170 180 190 200
VDPNARPLAP EVSIKTPRVF NAGGAPRICA LDCGLKYNQI RCLCQLGAEV
210 220 230 240 250
TVVPWDHELD SQKYDGLFLS NGPGDPASYP GVVSTLSRVL SEPNPRPVFG
260 270 280 290 300
ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD
310 320 330 340 350
ADSLPAGWAP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF
360 370 380 390 400
DVFLETVREA AAGNIGGQTV RERLAQRLCP PELPIPGSGL PPPRKVLILG
410 420 430 440 450
SGGLSIGQAG EFDYSGSQAI KALKEENIQT LLINPNIATV QTSQGLADKV
460 470 480 490 500
YFLPITLHYV TQVIRNERPD GVLLTFGGQT ALNCGVELTK AGVLARYGVR
510 520 530 540 550
VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ AQAAAERLGY
560 570 580 590 600
PVLVRAAFAL GGLGSGFAST KEELSALVAP AFAHTSQVLI DKSLKGWKEI
610 620 630 640 650
EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRR
660 670 680 690 700
TAIKVTQHLG IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY
710 720 730 740 750
PLAYVAAKLA LGIPLPELRN SVTGGTAAFE PSLDYCVVKI PRWDLSKFLR
760 770 780 790 800
VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL RMVDENCVGF DHTVKPVSDM
810 820 830 840 850
ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM KRIVTHAQLL
860 870 880 890 900
EQHRGQALPQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
910 920 930 940 950
KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RAPHVLVLGS GVYRIGSSVE
960 970 980 990 1000
FDWCAVGCIQ QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM
1010 1020 1030 1040 1050
DIYELENPEG VILSMGGQLP NNMAMALHRQ QCRVLGTSPE AIDSAENRFK
1060 1070 1080 1090 1100
FSRLLDTIGI SQPQWRELSD LESARQFCHT VGYPCVVRPS YVLSGAAMNV
1110 1120 1130 1140 1150
AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV ACDGIVSAIA
1160 1170 1180 1190 1200
ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN
1210 1220 1230 1240 1250
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPV
1260 1270 1280 1290 1300
GLMTGSGVVG VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL
1310 1320 1330 1340 1350
KAMLSTGFKI PEKNILLTIG SYKNKSELLP TVRLLESLGY SLYASLGTAD
1360 1370 1380 1390 1400
FYTEHGVKVT AVDWHFEEAV DGECPPQRSI LDQLAENHFE LVINLSMRGA
1410 1420 1430 1440 1450
GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL GQIGPAPPLK
1460 1470 1480 1490 1500
VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGVTMV
1510 1520 1530 1540 1550
CAMPNTRPPI IDAPALALAQ KLAEAGARCD FTLFLGASSE NAGTLGAVAG
1560 1570 1580 1590 1600
SAAGLKLYLN ETFSELRLDS VAQWMEHFET WPAHLPIVAH AERQSVAAVL
1610 1620 1630 1640 1650
MVAQLTQRPV HICHVARKEE ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL
1660 1670 1680 1690 1700
ERLGPGKGEV RPELGSREDM EALWENMAVI DCFASDHAPH TLEEKCGPKP
1710 1720 1730 1740 1750
PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF HLPLQEDTYV
1760 1770 1780 1790 1800
EVDLEHEWTV PSHMPFSKAR WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL
1810 1820 1830 1840 1850
VPPGYGQDVR KWPQGVVPQP PPSTPATTEI TTTPERPRRV IPGLPDGRFH
1860 1870 1880 1890 1900
LPPRIHRASD PGLPAEEPKE KPPRKVVEPE LMGTPDGPCY PAPPVPRQAS
1910 1920 1930 1940 1950
PQNLGSSGLL HPQMSPLLHS LVGQHILSVK QFTKDQMSHL FNVAHTLRMM
1960 1970 1980 1990 2000
VQKERSLDIL KGKVMASMFY EVSTRTSSSF AAAMARLGGA VLSFSEATSS
2010 2020 2030 2040 2050
VQKGESLADS VQTMSCYADV IVLRHPQPGA VELAAKHCRR PVINAGDGVG
2060 2070 2080 2090 2100
EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
2110 2120 2130 2140 2150
LRYVAPPSLR MPPSVRDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE
2160 2170 2180 2190 2200
RFGSVQEYEA CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR
2210 2220
AAYFRQAENG MYIRMALLAT VLGRF
Length:2,225
Mass (Da):243,238
Last modified:July 1, 2008 - v1
Checksum:iE7E606A0F650ABB4
GO
Isoform 2 (identifier: B2RQC6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1962-2032: Missing.

Show »
Length:2,154
Mass (Da):235,851
Checksum:iA83FA6E22929070C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1962 – 203271Missing in isoform 2. 1 PublicationVSP_053912Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC109608 Genomic DNA. No translation available.
CH466524 Genomic DNA. Translation: EDL37329.1.
BC137856 mRNA. Translation: AAI37857.1.
BC144972 mRNA. Translation: AAI44973.1.
CCDSiCCDS19171.1. [B2RQC6-1]
RefSeqiNP_001276451.1. NM_001289522.1. [B2RQC6-2]
NP_076014.1. NM_023525.2. [B2RQC6-1]
UniGeneiMm.305535.

Genome annotation databases

EnsembliENSMUST00000013773; ENSMUSP00000013773; ENSMUSG00000013629. [B2RQC6-1]
ENSMUST00000170329; ENSMUSP00000130789; ENSMUSG00000013629. [B2RQC6-2]
GeneIDi69719.
KEGGimmu:69719.
UCSCiuc008wwz.1. mouse. [B2RQC6-1]
uc012duk.1. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC109608 Genomic DNA. No translation available.
CH466524 Genomic DNA. Translation: EDL37329.1 .
BC137856 mRNA. Translation: AAI37857.1 .
BC144972 mRNA. Translation: AAI44973.1 .
CCDSi CCDS19171.1. [B2RQC6-1 ]
RefSeqi NP_001276451.1. NM_001289522.1. [B2RQC6-2 ]
NP_076014.1. NM_023525.2. [B2RQC6-1 ]
UniGenei Mm.305535.

3D structure databases

ProteinModelPortali B2RQC6.
SMRi B2RQC6. Positions 1460-1823.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi B2RQC6. 3 interactions.

Chemistry

ChEMBLi CHEMBL2774.

Proteomic databases

MaxQBi B2RQC6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000013773 ; ENSMUSP00000013773 ; ENSMUSG00000013629 . [B2RQC6-1 ]
ENSMUST00000170329 ; ENSMUSP00000130789 ; ENSMUSG00000013629 . [B2RQC6-2 ]
GeneIDi 69719.
KEGGi mmu:69719.
UCSCi uc008wwz.1. mouse. [B2RQC6-1 ]
uc012duk.1. mouse.

Organism-specific databases

CTDi 790.
MGIi MGI:1916969. Cad.

Phylogenomic databases

eggNOGi COG0458.
GeneTreei ENSGT00390000015604.
HOGENOMi HOG000234584.
HOVERGENi HBG000279.
InParanoidi B2RQC6.
KOi K11540.
OMAi KRIVTHA.
OrthoDBi EOG7M6D6F.
PhylomeDBi B2RQC6.
TreeFami TF105604.

Enzyme and pathway databases

UniPathwayi UPA00070 ; UER00115 .
UPA00070 ; UER00116 .
UPA00070 ; UER00117 .

Miscellaneous databases

ChiTaRSi cad. mouse.
NextBioi 330178.
SOURCEi Search...

Gene expression databases

ExpressionAtlasi B2RQC6. baseline and differential.
Genevestigatori B2RQC6.

Family and domain databases

Gene3Di 1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1370. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPi MF_00001. Asp_carb_tr.
MF_01209. CPSase_S_chain.
InterProi IPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR029062. Class_I_gatase-like.
IPR002195. Dihydroorotase_CS.
IPR017926. GATASE.
IPR011059. Metal-dep_hydrolase_composite.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view ]
Pfami PF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
PF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
PF02142. MGS. 1 hit.
PF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view ]
PRINTSi PR00100. AOTCASE.
PR00101. ATCASE.
PR00098. CPSASE.
SMARTi SM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48108. SSF48108. 1 hit.
SSF51338. SSF51338. 1 hit.
SSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
SSF53671. SSF53671. 1 hit.
TIGRFAMsi TIGR00670. asp_carb_tr. 1 hit.
TIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEi PS50975. ATP_GRASP. 2 hits.
PS00097. CARBAMOYLTRANSFERASE. 1 hit.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.

Entry informationi

Entry nameiPYR1_MOUSE
AccessioniPrimary (citable) accession number: B2RQC6
Secondary accession number(s): B7ZN27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: July 1, 2008
Last modified: October 29, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3