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Protein

Carbamoyl-phosphate synthase [ammonia], mitochondrial

Gene

Cps1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

    • ATP binding Source: RGD
    • calcium ion binding Source: RGD
    • carbamoyl-phosphate synthase (ammonia) activity Source: RGD
    • carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: GO_Central
    • endopeptidase activity Source: RGD
    • glutamate binding Source: RGD
    • modified amino acid binding Source: Ensembl
    • phospholipid binding Source: RGD
    • protein complex binding Source: RGD

    GO - Biological processi

    • 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
    • anion homeostasis Source: RGD
    • arginine biosynthetic process Source: GO_Central
    • carbamoyl phosphate biosynthetic process Source: Ensembl
    • cellular response to cAMP Source: RGD
    • cellular response to fibroblast growth factor stimulus Source: RGD
    • cellular response to glucagon stimulus Source: RGD
    • cellular response to oleic acid Source: RGD
    • glutamine metabolic process Source: InterPro
    • glycogen catabolic process Source: Ensembl
    • hepatocyte differentiation Source: RGD
    • homocysteine metabolic process Source: Ensembl
    • liver development Source: RGD
    • midgut development Source: RGD
    • nitric oxide metabolic process Source: Ensembl
    • positive regulation of vasodilation Source: Ensembl
    • proteolysis Source: GOC
    • response to amine Source: RGD
    • response to amino acid Source: RGD
    • response to cAMP Source: RGD
    • response to dexamethasone Source: RGD
    • response to drug Source: RGD
    • response to food Source: RGD
    • response to glucagon Source: RGD
    • response to glucocorticoid Source: RGD
    • response to growth hormone Source: RGD
    • response to lipopolysaccharide Source: RGD
    • response to oleic acid Source: RGD
    • response to starvation Source: RGD
    • response to steroid hormone Source: RGD
    • response to toxic substance Source: RGD
    • response to zinc ion Source: RGD
    • triglyceride catabolic process Source: Ensembl
    • urea cycle Source: RGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Urea cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_328693. 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 Componenti: Chromosome 9

    Organism-specific databases

    RGDi2395. Cps1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: RGD
    • mitochondrial inner membrane Source: RGD
    • mitochondrial nucleoid Source: Ensembl
    • mitochondrion Source: HGNC
    • nucleolus Source: UniProtKB-SubCell
    • protein complex Source: RGD
    Complete GO annotation...

    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-glutaryllysineBy 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 residuei148 – 1481PhosphoserineBy similarity
    Modified residuei157 – 1571N6-acetyllysine; alternateBy similarity
    Modified residuei157 – 1571N6-succinyllysine; alternateBy similarity
    Modified residuei171 – 1711N6-acetyllysineBy similarity
    Modified residuei171 – 1711N6-glutaryllysineBy similarity
    Modified residuei176 – 1761N6-glutaryllysineBy similarity
    Modified residuei182 – 1821N6-acetyllysineBy similarity
    Modified residuei197 – 1971N6-acetyllysineBy similarity
    Modified residuei207 – 2071N6-acetyllysine; alternateBy similarity
    Modified residuei207 – 2071N6-glutaryllysineBy similarity
    Modified residuei207 – 2071N6-succinyllysine; alternateBy similarity
    Modified residuei210 – 2101N6-acetyllysineBy similarity
    Modified residuei210 – 2101N6-glutaryllysineBy similarity
    Modified residuei214 – 2141N6-acetyllysine; alternateBy similarity
    Modified residuei214 – 2141N6-glutaryllysineBy similarity
    Modified residuei214 – 2141N6-succinyllysine; alternateBy similarity
    Modified residuei219 – 2191N6-acetyllysineBy similarity
    Modified residuei219 – 2191N6-glutaryllysineBy similarity
    Modified residuei228 – 2281N6-acetyllysineBy similarity
    Modified residuei228 – 2281N6-glutaryllysineBy similarity
    Modified residuei237 – 2371N6-glutaryllysineBy similarity
    Modified residuei279 – 2791N6-acetyllysineBy similarity
    Modified residuei280 – 2801N6-acetyllysineBy similarity
    Modified residuei280 – 2801N6-glutaryllysineBy similarity
    Modified residuei287 – 2871N6-acetyllysine; alternateBy similarity
    Modified residuei287 – 2871N6-succinyllysine; alternateBy similarity
    Modified residuei307 – 3071N6-acetyllysine; alternateBy similarity
    Modified residuei307 – 3071N6-glutaryllysineBy similarity
    Modified residuei307 – 3071N6-succinyllysine; alternateBy similarity
    Modified residuei310 – 3101N6-acetyllysineBy similarity
    Modified residuei310 – 3101N6-glutaryllysineBy similarity
    Modified residuei400 – 4001N6-succinyllysineBy similarity
    Modified residuei402 – 4021N6-glutaryllysineBy similarity
    Modified residuei402 – 4021N6-succinyllysineBy similarity
    Modified residuei412 – 4121N6-acetyllysine; alternateBy similarity
    Modified residuei412 – 4121N6-glutaryllysineBy similarity
    Modified residuei412 – 4121N6-succinyllysine; alternateBy similarity
    Modified residuei453 – 4531N6-acetyllysineBy similarity
    Modified residuei453 – 4531N6-glutaryllysineBy similarity
    Modified residuei458 – 4581N6-acetyllysine; alternateBy similarity
    Modified residuei458 – 4581N6-glutaryllysineBy 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-glutaryllysineBy similarity
    Modified residuei527 – 5271N6-succinyllysine; alternateBy similarity
    Modified residuei532 – 5321N6-acetyllysineBy similarity
    Modified residuei532 – 5321N6-glutaryllysineBy similarity
    Modified residuei537 – 5371Phosphoserine; alternateBy similarity
    Glycosylationi537 – 5371O-linked (GlcNAc); alternate1 Publication
    Modified residuei553 – 5531N6-acetyllysine; alternateBy similarity
    Modified residuei553 – 5531N6-glutaryllysineBy similarity
    Modified residuei553 – 5531N6-succinyllysine; alternateBy similarity
    Modified residuei560 – 5601N6-acetyllysine; alternateBy similarity
    Modified residuei560 – 5601N6-succinyllysine; alternateBy similarity
    Modified residuei569 – 5691PhosphoserineBy 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 residuei728 – 7281N6-glutaryllysineBy similarity
    Modified residuei751 – 7511N6-acetyllysine; alternateBy similarity
    Modified residuei751 – 7511N6-succinyllysine; alternateBy similarity
    Modified residuei757 – 7571N6-acetyllysine; alternateBy similarity
    Modified residuei757 – 7571N6-glutaryllysineBy similarity
    Modified residuei757 – 7571N6-succinyllysine; alternateBy similarity
    Modified residuei772 – 7721N6-acetyllysineBy similarity
    Modified residuei772 – 7721N6-glutaryllysineBy similarity
    Modified residuei793 – 7931N6-acetyllysine; alternateBy similarity
    Modified residuei793 – 7931N6-glutaryllysineBy similarity
    Modified residuei793 – 7931N6-succinyllysine; alternateBy similarity
    Modified residuei811 – 8111N6-acetyllysineBy similarity
    Modified residuei811 – 8111N6-glutaryllysineBy similarity
    Modified residuei831 – 8311N6-acetyllysine; alternateBy similarity
    Modified residuei831 – 8311N6-succinyllysine; alternateBy similarity
    Modified residuei841 – 8411N6-acetyllysineBy similarity
    Modified residuei841 – 8411N6-glutaryllysineBy similarity
    Modified residuei856 – 8561N6-acetyllysineBy similarity
    Modified residuei856 – 8561N6-glutaryllysineBy similarity
    Modified residuei869 – 8691N6-glutaryllysineBy similarity
    Modified residuei875 – 8751N6-acetyllysine; alternateBy similarity
    Modified residuei875 – 8751N6-glutaryllysineBy similarity
    Modified residuei875 – 8751N6-succinyllysine; alternateBy similarity
    Modified residuei889 – 8891N6-acetyllysine; alternateBy similarity
    Modified residuei889 – 8891N6-glutaryllysineBy similarity
    Modified residuei889 – 8891N6-succinyllysine; alternateBy similarity
    Modified residuei892 – 8921N6-acetyllysine; alternateBy similarity
    Modified residuei892 – 8921N6-glutaryllysineBy similarity
    Modified residuei892 – 8921N6-succinyllysine; alternateBy similarity
    Modified residuei908 – 9081N6-acetyllysineBy similarity
    Modified residuei908 – 9081N6-glutaryllysineBy similarity
    Modified residuei915 – 9151N6-acetyllysine; alternateBy similarity
    Modified residuei915 – 9151N6-glutaryllysineBy similarity
    Modified residuei915 – 9151N6-succinyllysine; alternateBy similarity
    Modified residuei919 – 9191N6-acetyllysine; alternateBy similarity
    Modified residuei919 – 9191N6-glutaryllysineBy similarity
    Modified residuei919 – 9191N6-succinyllysine; alternateBy similarity
    Modified residuei935 – 9351N6-acetyllysineBy similarity
    Modified residuei1074 – 10741N6-acetyllysine; alternateBy similarity
    Modified residuei1074 – 10741N6-glutaryllysineBy 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-glutaryllysineBy similarity
    Modified residuei1168 – 11681N6-succinyllysine; alternateBy similarity
    Modified residuei1183 – 11831N6-acetyllysine; alternateBy similarity
    Modified residuei1183 – 11831N6-glutaryllysineBy similarity
    Modified residuei1183 – 11831N6-succinyllysine; alternateBy similarity
    Modified residuei1203 – 12031PhosphoserineBy similarity
    Modified residuei1222 – 12221N6-acetyllysineBy similarity
    Modified residuei1224 – 12241N6-glutaryllysineBy 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-glutaryllysineBy similarity
    Modified residuei1356 – 13561N6-succinyllysine; alternateBy similarity
    Modified residuei1360 – 13601N6-glutaryllysineBy similarity
    Modified residuei1360 – 13601N6-succinyllysineBy similarity
    Modified residuei1419 – 14191PhosphoserineBy similarity
    Modified residuei1431 – 14311PhosphoserineBy 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-glutaryllysineBy similarity
    Modified residuei1479 – 14791N6-succinyllysine; alternateBy similarity
    Modified residuei1486 – 14861N6-acetyllysine; alternateBy similarity
    Modified residuei1486 – 14861N6-glutaryllysineBy 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
    Glutarylated. Glutarylation levels increase during fasting. Deglutarylated by SIRT5 at Lys-55, Lys-219, Lys-412, Lys-889, Lys-892, Lys-915, Lys-1360 and Lys-1486, leading to activation.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

    GenevisibleiP07756. RN.

    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.
    OMAiIIFKMTR.
    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

            10         20         30         40         50
    MTRILTACKV VKTLKSGFGL ANVTSKRQWD FSRPGIRLLS VKAQTAHIVL
    60 70 80 90 100
    EDGTKMKGYS FGHPSSVAGE VVFNTGLGGY SEALTDPAYK GQILTMANPI
    110 120 130 140 150
    IGNGGAPDTT ARDELGLNKY MESDGIKVAG LLVLNYSHDY NHWLATKSLG
    160 170 180 190 200
    QWLQEEKVPA IYGVDTRMLT KIIRDKGTML GKIEFEGQSV DFVDPNKQNL
    210 220 230 240 250
    IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA EVHLVPWNHD
    260 270 280 290 300
    FTQMDYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT
    310 320 330 340 350
    GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK
    360 370 380 390 400
    PLFVNVNDQT NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK
    410 420 430 440 450
    GKGTTITSVL PKPALVASRV EVSKVLILGS GGLSIGQAGE FDYSGSQAVK
    460 470 480 490 500
    AMKEENVKTV LMNPNIASVQ TNEVGLKQAD AVYFLPITPQ FVTEVIKAER
    510 520 530 540 550
    PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES IMATEDRQLF
    560 570 580 590 600
    SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC
    610 620 630 640 650
    PNKETLMDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM
    660 670 680 690 700
    ENVDAMGVHT GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ
    710 720 730 740 750
    FALHPTSMEY CIIEVNARLS RSSALASKAT GYPLAFIAAK IALGIPLPEI
    760 770 780 790 800
    KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR FHGTSSRIGS SMKSVGEVMA
    810 820 830 840 850
    IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLR KELSEPSSTR
    860 870 880 890 900
    IYAIAKALEN NMSLDEIVKL TSIDKWFLYK MRDILNMDKT LKGLNSESVT
    910 920 930 940 950
    EETLRQAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE
    960 970 980 990 1000
    YPSVTNYLYV TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI
    1010 1020 1030 1040 1050
    RTLRQLGKKT VVVNCNPETV STDFDECDKL YFEELSLERI LDIYHQEACN
    1060 1070 1080 1090 1100
    GCIISVGGQI PNNLAVPLYK NGVKIMGTSP LQIDRAEDRS IFSAVLDELK
    1110 1120 1130 1140 1150
    VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN VVFSEDEMKR
    1160 1170 1180 1190 1200
    FLEEATRVSQ EHPVVLTKFI EGAREVEMDA VGKEGRVISH AISEHVEDAG
    1210 1220 1230 1240 1250
    VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND
    1260 1270 1280 1290 1300
    VLVIECNLRA SRSFPFVSKT LGVDFIDVAT KVMIGESVDE KHLPTLEQPI
    1310 1320 1330 1340 1350
    IPSDYVAIKA PMFSWPRLRD ADPILRCEMA STGEVACFGE GIHTAFLKAM
    1360 1370 1380 1390 1400
    LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ LHNEGFKLFA TEATSDWLNA
    1410 1420 1430 1440 1450
    NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN NNTKFVHDNY
    1460 1470 1480 1490 1500
    VIRRTAVDSG IALLTNFQVT KLFAEAVQKA RTVDSKSLFH YRQYSAGKAA
    Length:1,500
    Mass (Da):164,580
    Last modified:August 1, 1988 - v1
    Checksum:i038E8F893DE1C34D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000019021.

    Protein family/group databases

    MEROPSiC26.951.

    PTM databases

    PhosphoSiteiP07756.

    Proteomic databases

    PaxDbiP07756.
    PRIDEiP07756.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi1373.
    RGDi2395. Cps1.

    Phylogenomic databases

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

    Enzyme and pathway databases

    ReactomeiREACT_328693. Urea cycle.
    SABIO-RKP07756.

    Miscellaneous databases

    NextBioi697797.
    PROiP07756.

    Gene expression databases

    GenevisibleiP07756. RN.

    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]
    ProtoNetiSearch...

    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: July 22, 2015
    This is version 139 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.