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P07756

- CPSM_RAT

UniProt

P07756 - CPSM_RAT

Protein

Carbamoyl-phosphate synthase [ammonia], mitochondrial

Gene

Cps1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    Functioni

    Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.

    Catalytic activityi

    2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate.1 Publication

    Enzyme regulationi

    Requires N-acetyl-L-glutamate (NAG) as an allosteric activator. N-acetyl-L-beta-phenylglutamate (Phe-NAG) can also activate CPSase I, but with an activation constant that is 2-fold higher than that for NAG.1 Publication

    Kineticsi

    The activation constant Ka of N-acetyl-L-glutamate for the reaction is 0.11 mM.

    1. KM=1.06 mM for ATP1 Publication
    2. KM=6.43 mM for HCO3-1 Publication
    3. KM=1.07 mM for NH4+1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1391 – 13911Allosteric activator
    Binding sitei1394 – 13941Allosteric activator
    Binding sitei1410 – 14101Allosteric activator
    Binding sitei1437 – 14371Allosteric activator
    Binding sitei1440 – 14401Allosteric activator
    Binding sitei1449 – 14491Allosteric activator

    GO - Molecular functioni

    1. ATP binding Source: RGD
    2. calcium ion binding Source: RGD
    3. carbamoyl-phosphate synthase (ammonia) activity Source: RGD
    4. endopeptidase activity Source: RGD
    5. glutamate binding Source: RGD
    6. modified amino acid binding Source: Ensembl
    7. phospholipid binding Source: RGD
    8. protein complex binding Source: RGD

    GO - Biological processi

    1. anion homeostasis Source: RGD
    2. carbamoyl phosphate biosynthetic process Source: Ensembl
    3. cellular response to cAMP Source: RGD
    4. cellular response to fibroblast growth factor stimulus Source: RGD
    5. cellular response to glucagon stimulus Source: RGD
    6. cellular response to oleic acid Source: RGD
    7. glutamine catabolic process Source: InterPro
    8. glycogen catabolic process Source: Ensembl
    9. hepatocyte differentiation Source: RGD
    10. homocysteine metabolic process Source: Ensembl
    11. liver development Source: RGD
    12. midgut development Source: RGD
    13. nitric oxide metabolic process Source: Ensembl
    14. positive regulation of vasodilation Source: Ensembl
    15. proteolysis Source: GOC
    16. response to acid chemical Source: RGD
    17. response to amine Source: RGD
    18. response to amino acid Source: RGD
    19. response to cAMP Source: RGD
    20. response to dexamethasone Source: RGD
    21. response to drug Source: RGD
    22. response to food Source: RGD
    23. response to glucagon Source: RGD
    24. response to glucocorticoid Source: RGD
    25. response to growth hormone Source: RGD
    26. response to lipopolysaccharide Source: RGD
    27. response to oleic acid Source: RGD
    28. response to starvation Source: RGD
    29. response to steroid hormone Source: RGD
    30. response to toxic substance Source: RGD
    31. response to zinc ion Source: RGD
    32. triglyceride catabolic process Source: Ensembl
    33. urea cycle Source: RGD

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Urea cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_216480. Urea cycle.
    SABIO-RKP07756.

    Protein family/group databases

    MEROPSiC26.951.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC:6.3.4.16)
    Alternative name(s):
    Carbamoyl-phosphate synthetase I
    Short name:
    CPSase I
    Gene namesi
    Name:Cps1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 9

    Organism-specific databases

    RGDi2395. Cps1.

    Subcellular locationi

    Mitochondrion. Nucleusnucleolus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. mitochondrial inner membrane Source: RGD
    3. mitochondrial nucleoid Source: Ensembl
    4. mitochondrion Source: HGNC
    5. nucleolus Source: UniProtKB-SubCell
    6. protein complex Source: RGD

    Keywords - Cellular componenti

    Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1391 – 13911T → V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG. 1 Publication
    Mutagenesisi1394 – 13941T → A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG. 1 Publication
    Mutagenesisi1410 – 14101W → K: 60-fold increase in the activation constant of NAG. 1 Publication
    Mutagenesisi1437 – 14371N → D: 70-fold increase in the activation constant of NAG. 1 Publication
    Mutagenesisi1440 – 14401N → D: 110-fold increase in the activation constant of NAG. Modifies the specificity for the activator: Binds Phe-NAG considerably better than NAG. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3838MitochondrionAdd
    BLAST
    Chaini39 – 15001462Carbamoyl-phosphate synthase [ammonia], mitochondrialPRO_0000029899Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551N6-acetyllysine; alternateBy similarity
    Modified residuei55 – 551N6-succinyllysine; alternateBy similarity
    Modified residuei57 – 571N6-acetyllysine; alternateBy similarity
    Modified residuei57 – 571N6-succinyllysine; alternateBy similarity
    Modified residuei119 – 1191N6-acetyllysine; alternateBy similarity
    Modified residuei119 – 1191N6-succinyllysine; alternateBy similarity
    Modified residuei157 – 1571N6-acetyllysine; alternateBy similarity
    Modified residuei157 – 1571N6-succinyllysine; alternateBy similarity
    Modified residuei171 – 1711N6-acetyllysineBy similarity
    Modified residuei182 – 1821N6-acetyllysineBy similarity
    Modified residuei197 – 1971N6-acetyllysineBy similarity
    Modified residuei207 – 2071N6-acetyllysine; alternateBy similarity
    Modified residuei207 – 2071N6-succinyllysine; alternateBy similarity
    Modified residuei210 – 2101N6-acetyllysineBy similarity
    Modified residuei214 – 2141N6-acetyllysine; alternateBy similarity
    Modified residuei214 – 2141N6-succinyllysine; alternateBy similarity
    Modified residuei219 – 2191N6-acetyllysineBy similarity
    Modified residuei228 – 2281N6-acetyllysineBy similarity
    Modified residuei279 – 2791N6-acetyllysineBy similarity
    Modified residuei280 – 2801N6-acetyllysineBy similarity
    Modified residuei287 – 2871N6-acetyllysine; alternateBy similarity
    Modified residuei287 – 2871N6-succinyllysine; alternateBy similarity
    Modified residuei307 – 3071N6-acetyllysine; alternateBy similarity
    Modified residuei307 – 3071N6-succinyllysine; alternateBy similarity
    Modified residuei310 – 3101N6-acetyllysineBy similarity
    Modified residuei400 – 4001N6-succinyllysineBy similarity
    Modified residuei402 – 4021N6-succinyllysineBy similarity
    Modified residuei412 – 4121N6-acetyllysine; alternateBy similarity
    Modified residuei412 – 4121N6-succinyllysine; alternateBy similarity
    Modified residuei453 – 4531N6-acetyllysineBy similarity
    Modified residuei458 – 4581N6-acetyllysine; alternateBy similarity
    Modified residuei458 – 4581N6-succinyllysine; alternateBy similarity
    Modified residuei522 – 5221N6-acetyllysine; alternateBy similarity
    Modified residuei522 – 5221N6-succinyllysine; alternateBy similarity
    Modified residuei527 – 5271N6-acetyllysine; alternateBy similarity
    Modified residuei527 – 5271N6-succinyllysine; alternateBy similarity
    Modified residuei532 – 5321N6-acetyllysineBy similarity
    Modified residuei537 – 5371PhosphoserineBy similarity
    Glycosylationi537 – 5371O-linked (GlcNAc)1 Publication
    Modified residuei553 – 5531N6-acetyllysine; alternateBy similarity
    Modified residuei553 – 5531N6-succinyllysine; alternateBy similarity
    Modified residuei560 – 5601N6-acetyllysine; alternateBy similarity
    Modified residuei560 – 5601N6-succinyllysine; alternateBy similarity
    Modified residuei575 – 5751N6-acetyllysine; alternateBy similarity
    Modified residuei575 – 5751N6-succinyllysine; alternateBy similarity
    Modified residuei603 – 6031N6-acetyllysine; alternateBy similarity
    Modified residuei603 – 6031N6-succinyllysine; alternateBy similarity
    Modified residuei612 – 6121N6-acetyllysine; alternateBy similarity
    Modified residuei612 – 6121N6-succinyllysine; alternateBy similarity
    Modified residuei630 – 6301N6-acetyllysineBy similarity
    Modified residuei751 – 7511N6-acetyllysine; alternateBy similarity
    Modified residuei751 – 7511N6-succinyllysine; alternateBy similarity
    Modified residuei757 – 7571N6-acetyllysine; alternateBy similarity
    Modified residuei757 – 7571N6-succinyllysine; alternateBy similarity
    Modified residuei772 – 7721N6-acetyllysineBy similarity
    Modified residuei793 – 7931N6-acetyllysine; alternateBy similarity
    Modified residuei793 – 7931N6-succinyllysine; alternateBy similarity
    Modified residuei811 – 8111N6-acetyllysineBy similarity
    Modified residuei831 – 8311N6-acetyllysine; alternateBy similarity
    Modified residuei831 – 8311N6-succinyllysine; alternateBy similarity
    Modified residuei841 – 8411N6-acetyllysineBy similarity
    Modified residuei856 – 8561N6-acetyllysineBy similarity
    Modified residuei875 – 8751N6-acetyllysine; alternateBy similarity
    Modified residuei875 – 8751N6-succinyllysine; alternateBy similarity
    Modified residuei889 – 8891N6-acetyllysine; alternateBy similarity
    Modified residuei889 – 8891N6-succinyllysine; alternateBy similarity
    Modified residuei892 – 8921N6-acetyllysine; alternateBy similarity
    Modified residuei892 – 8921N6-succinyllysine; alternateBy similarity
    Modified residuei908 – 9081N6-acetyllysineBy similarity
    Modified residuei915 – 9151N6-acetyllysine; alternateBy similarity
    Modified residuei915 – 9151N6-succinyllysine; alternateBy similarity
    Modified residuei919 – 9191N6-acetyllysine; alternateBy similarity
    Modified residuei919 – 9191N6-succinyllysine; alternateBy similarity
    Modified residuei935 – 9351N6-acetyllysineBy similarity
    Modified residuei1074 – 10741N6-acetyllysine; alternateBy similarity
    Modified residuei1074 – 10741N6-succinyllysine; alternateBy similarity
    Modified residuei1079 – 10791PhosphoserineBy similarity
    Modified residuei1100 – 11001N6-acetyllysine; alternateBy similarity
    Modified residuei1100 – 11001N6-succinyllysine; alternateBy similarity
    Modified residuei1149 – 11491N6-succinyllysineBy similarity
    Modified residuei1168 – 11681N6-acetyllysine; alternateBy similarity
    Modified residuei1168 – 11681N6-succinyllysine; alternateBy similarity
    Modified residuei1183 – 11831N6-acetyllysine; alternateBy similarity
    Modified residuei1183 – 11831N6-succinyllysine; alternateBy similarity
    Modified residuei1222 – 12221N6-acetyllysineBy similarity
    Modified residuei1232 – 12321N6-acetyllysine; alternateBy similarity
    Modified residuei1232 – 12321N6-succinyllysine; alternateBy similarity
    Modified residuei1269 – 12691N6-acetyllysine; alternateBy similarity
    Modified residuei1269 – 12691N6-succinyllysine; alternateBy similarity
    Modified residuei1291 – 12911N6-acetyllysine; alternateBy similarity
    Modified residuei1291 – 12911N6-succinyllysine; alternateBy similarity
    Glycosylationi1331 – 13311O-linked (GlcNAc)1 Publication
    Glycosylationi1332 – 13321O-linked (GlcNAc)1 Publication
    Modified residuei1356 – 13561N6-acetyllysine; alternateBy similarity
    Modified residuei1356 – 13561N6-succinyllysine; alternateBy similarity
    Modified residuei1360 – 13601N6-succinyllysineBy similarity
    Modified residuei1444 – 14441N6-acetyllysine; alternateBy similarity
    Modified residuei1444 – 14441N6-succinyllysine; alternateBy similarity
    Modified residuei1471 – 14711N6-acetyllysine; alternateBy similarity
    Modified residuei1471 – 14711N6-succinyllysine; alternateBy similarity
    Modified residuei1479 – 14791N6-acetyllysine; alternateBy similarity
    Modified residuei1479 – 14791N6-succinyllysine; alternateBy similarity
    Modified residuei1486 – 14861N6-acetyllysine; alternateBy similarity
    Modified residuei1486 – 14861N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    50% of the mature protein that was isolated had Leu-39 as its N-terminal residue and 50% had Ser-40 suggesting two adjacent processing sites. However, the possibility of proteolytic removal of Leu-39 during the isolation of the enzyme cannot be excluded.
    Succinylated at Lys-287 and Lys-1291. Desuccinylated at Lys-1291 by SIRT5, leading to activation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP07756.
    PRIDEiP07756.

    PTM databases

    PhosphoSiteiP07756.

    Expressioni

    Tissue specificityi

    Primarily in the liver and small intestine.

    Gene expression databases

    GenevestigatoriP07756.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000019021.

    Structurei

    3D structure databases

    ProteinModelPortaliP07756.
    SMRiP07756. Positions 1343-1478.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini219 – 404186Glutamine amidotransferase type-1Add
    BLAST
    Domaini551 – 743193ATP-grasp 1Add
    BLAST
    Domaini1093 – 1284192ATP-grasp 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni39 – 218180Anthranilate phosphoribosyltransferase homologAdd
    BLAST

    Domaini

    The type-1 glutamine amidotransferase domain is defective.

    Sequence similaritiesi

    Contains 2 ATP-grasp domains.Curated

    Keywords - Domaini

    Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0458.
    GeneTreeiENSGT00390000015604.
    HOGENOMiHOG000234583.
    HOVERGENiHBG000279.
    InParanoidiP07756.
    KOiK01948.
    OMAiMDLGTKA.
    OrthoDBiEOG7M6D6F.
    PhylomeDBiP07756.

    Family and domain databases

    Gene3Di1.10.1030.10. 1 hit.
    3.30.1490.20. 2 hits.
    3.30.470.20. 2 hits.
    3.40.50.1380. 1 hit.
    3.40.50.20. 2 hits.
    3.40.50.880. 1 hit.
    3.50.30.20. 1 hit.
    HAMAPiMF_01209. CPSase_S_chain.
    InterProiIPR011761. 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.
    IPR017926. GATASE.
    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.
    [Graphical view]
    PRINTSiPR00098. CPSASE.
    SMARTiSM01096. CPSase_L_D3. 1 hit.
    SM01097. CPSase_sm_chain. 1 hit.
    SM00851. MGS. 1 hit.
    [Graphical view]
    SUPFAMiSSF48108. SSF48108. 1 hit.
    SSF52021. SSF52021. 1 hit.
    SSF52317. SSF52317. 1 hit.
    SSF52335. SSF52335. 1 hit.
    SSF52440. SSF52440. 2 hits.
    TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
    TIGR01368. CPSaseIIsmall. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 2 hits.
    PS00866. CPSASE_1. 2 hits.
    PS00867. CPSASE_2. 2 hits.
    PS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07756-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRILTACKV VKTLKSGFGL ANVTSKRQWD FSRPGIRLLS VKAQTAHIVL     50
    EDGTKMKGYS FGHPSSVAGE VVFNTGLGGY SEALTDPAYK GQILTMANPI 100
    IGNGGAPDTT ARDELGLNKY MESDGIKVAG LLVLNYSHDY NHWLATKSLG 150
    QWLQEEKVPA IYGVDTRMLT KIIRDKGTML GKIEFEGQSV DFVDPNKQNL 200
    IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA EVHLVPWNHD 250
    FTQMDYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT 300
    GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK 350
    PLFVNVNDQT NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK 400
    GKGTTITSVL PKPALVASRV EVSKVLILGS GGLSIGQAGE FDYSGSQAVK 450
    AMKEENVKTV LMNPNIASVQ TNEVGLKQAD AVYFLPITPQ FVTEVIKAER 500
    PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES IMATEDRQLF 550
    SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC 600
    PNKETLMDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM 650
    ENVDAMGVHT GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ 700
    FALHPTSMEY CIIEVNARLS RSSALASKAT GYPLAFIAAK IALGIPLPEI 750
    KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR FHGTSSRIGS SMKSVGEVMA 800
    IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLR KELSEPSSTR 850
    IYAIAKALEN NMSLDEIVKL TSIDKWFLYK MRDILNMDKT LKGLNSESVT 900
    EETLRQAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE 950
    YPSVTNYLYV TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI 1000
    RTLRQLGKKT VVVNCNPETV STDFDECDKL YFEELSLERI LDIYHQEACN 1050
    GCIISVGGQI PNNLAVPLYK NGVKIMGTSP LQIDRAEDRS IFSAVLDELK 1100
    VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN VVFSEDEMKR 1150
    FLEEATRVSQ EHPVVLTKFI EGAREVEMDA VGKEGRVISH AISEHVEDAG 1200
    VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND 1250
    VLVIECNLRA SRSFPFVSKT LGVDFIDVAT KVMIGESVDE KHLPTLEQPI 1300
    IPSDYVAIKA PMFSWPRLRD ADPILRCEMA STGEVACFGE GIHTAFLKAM 1350
    LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ LHNEGFKLFA TEATSDWLNA 1400
    NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN NNTKFVHDNY 1450
    VIRRTAVDSG IALLTNFQVT KLFAEAVQKA RTVDSKSLFH YRQYSAGKAA 1500
    Length:1,500
    Mass (Da):164,580
    Last modified:August 1, 1988 - v1
    Checksum:i038E8F893DE1C34D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12335
    , M11710, M12318, M12319, M12320, M12321, M12322, M12323, M12324, M12325, M12326, M12327, M12328 Genomic DNA. Translation: AAB59717.1.
    J02805 Genomic DNA. Translation: AAA40959.1.
    PIRiA28481. SYRTCA.
    RefSeqiNP_058768.1. NM_017072.1.
    UniGeneiRn.53968.

    Genome annotation databases

    EnsembliENSRNOT00000019023; ENSRNOP00000019021; ENSRNOG00000013704.
    GeneIDi497840.
    KEGGirno:497840.
    UCSCiRGD:2395. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12335
    , M11710 , M12318 , M12319 , M12320 , M12321 , M12322 , M12323 , M12324 , M12325 , M12326 , M12327 , M12328 Genomic DNA. Translation: AAB59717.1 .
    J02805 Genomic DNA. Translation: AAA40959.1 .
    PIRi A28481. SYRTCA.
    RefSeqi NP_058768.1. NM_017072.1.
    UniGenei Rn.53968.

    3D structure databases

    ProteinModelPortali P07756.
    SMRi P07756. Positions 1343-1478.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000019021.

    Protein family/group databases

    MEROPSi C26.951.

    PTM databases

    PhosphoSitei P07756.

    Proteomic databases

    PaxDbi P07756.
    PRIDEi P07756.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000019023 ; ENSRNOP00000019021 ; ENSRNOG00000013704 .
    GeneIDi 497840.
    KEGGi rno:497840.
    UCSCi RGD:2395. rat.

    Organism-specific databases

    CTDi 1373.
    RGDi 2395. Cps1.

    Phylogenomic databases

    eggNOGi COG0458.
    GeneTreei ENSGT00390000015604.
    HOGENOMi HOG000234583.
    HOVERGENi HBG000279.
    InParanoidi P07756.
    KOi K01948.
    OMAi MDLGTKA.
    OrthoDBi EOG7M6D6F.
    PhylomeDBi P07756.

    Enzyme and pathway databases

    Reactomei REACT_216480. Urea cycle.
    SABIO-RK P07756.

    Miscellaneous databases

    NextBioi 697797.
    PROi P07756.

    Gene expression databases

    Genevestigatori P07756.

    Family and domain databases

    Gene3Di 1.10.1030.10. 1 hit.
    3.30.1490.20. 2 hits.
    3.30.470.20. 2 hits.
    3.40.50.1380. 1 hit.
    3.40.50.20. 2 hits.
    3.40.50.880. 1 hit.
    3.50.30.20. 1 hit.
    HAMAPi MF_01209. CPSase_S_chain.
    InterProi 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.
    IPR017926. GATASE.
    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.
    [Graphical view ]
    PRINTSi 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.
    SSF52021. SSF52021. 1 hit.
    SSF52317. SSF52317. 1 hit.
    SSF52335. SSF52335. 1 hit.
    SSF52440. SSF52440. 2 hits.
    TIGRFAMsi TIGR01369. CPSaseII_lrg. 1 hit.
    TIGR01368. CPSaseIIsmall. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 2 hits.
    PS00866. CPSASE_1. 2 hits.
    PS00867. CPSASE_2. 2 hits.
    PS51273. GATASE_TYPE_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and derivation of the gene coding for mitochondrial carbamyl phosphate synthetase I of rat."
      Nyunoya H., Broglie K.E., Widgren E.E., Lusty C.J.
      J. Biol. Chem. 260:9346-9356(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "Rat carbamyl-phosphate synthetase I gene. Promoter sequence and tissue-specific transcriptional regulation in vitro."
      Lagace M., Howell B.W., Burak R., Lusty C.J., Shore G.C.
      J. Biol. Chem. 262:10415-10418(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
    3. "Structural insight on the control of urea synthesis: identification of the binding site for N-acetyl-L-glutamate, the essential allosteric activator of mitochondrial carbamoyl phosphate synthetase."
      Pekkala S., Martinez A.I., Barcelona B., Gallego J., Bendala E., Yefimenko I., Rubio V., Cervera J.
      Biochem. J. 424:211-220(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, ALLOSTERIC ACTIVATOR NAG BINDING SITE, KINETIC PARAMETERS, MUTAGENESIS OF THR-1391; THR-1394; TRP-1410; ASN-1437 AND ASN-1440.
    4. "Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods."
      Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.
      PLoS ONE 8:E76399-E76399(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-537; SER-1331 AND THR-1332.

    Entry informationi

    Entry nameiCPSM_RAT
    AccessioniPrimary (citable) accession number: P07756
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3