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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 + HCO3- = 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)DescriptionActionsGraphical viewLength
    Binding sitei1391Allosteric activator1
    Binding sitei1394Allosteric activator1
    Binding sitei1410Allosteric activator1
    Binding sitei1437Allosteric activator1
    Binding sitei1440Allosteric activator1
    Binding sitei1449Allosteric activator1

    GO - Molecular functioni

    • aspartate carbamoyltransferase activity Source: GO_Central
    • 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
    • dihydroorotase 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: GO_Central
    • 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
    • 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

    ReactomeiR-RNO-70635. 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
    Proteomesi
    • UP000002494 Componenti: Chromosome 9

    Organism-specific databases

    RGDi2395. Cps1.

    Subcellular locationi

    • Mitochondrion
    • Nucleusnucleolus By similarity

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi1391T → V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG. 1 Publication1
    Mutagenesisi1394T → A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG. 1 Publication1
    Mutagenesisi1410W → K: 60-fold increase in the activation constant of NAG. 1 Publication1
    Mutagenesisi1437N → D: 70-fold increase in the activation constant of NAG. 1 Publication1
    Mutagenesisi1440N → D: 110-fold increase in the activation constant of NAG. Modifies the specificity for the activator: Binds Phe-NAG considerably better than NAG. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 38MitochondrionAdd BLAST38
    ChainiPRO_000002989939 – 1500Carbamoyl-phosphate synthase [ammonia], mitochondrialAdd BLAST1462

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei55N6-acetyllysine; alternateBy similarity1
    Modified residuei55N6-glutaryllysine; alternateBy similarity1
    Modified residuei55N6-succinyllysine; alternateBy similarity1
    Modified residuei57N6-acetyllysine; alternateBy similarity1
    Modified residuei57N6-succinyllysine; alternateBy similarity1
    Modified residuei119N6-acetyllysine; alternateBy similarity1
    Modified residuei119N6-succinyllysine; alternateBy similarity1
    Modified residuei148PhosphoserineCombined sources1
    Modified residuei157N6-acetyllysine; alternateBy similarity1
    Modified residuei157N6-succinyllysine; alternateBy similarity1
    Modified residuei171N6-acetyllysine; alternateBy similarity1
    Modified residuei171N6-glutaryllysine; alternateBy similarity1
    Modified residuei176N6-glutaryllysineBy similarity1
    Modified residuei182N6-acetyllysineBy similarity1
    Modified residuei189PhosphoserineCombined sources1
    Modified residuei197N6-acetyllysineBy similarity1
    Modified residuei207N6-acetyllysine; alternateBy similarity1
    Modified residuei207N6-glutaryllysine; alternateBy similarity1
    Modified residuei207N6-succinyllysine; alternateBy similarity1
    Modified residuei210N6-acetyllysine; alternateBy similarity1
    Modified residuei210N6-glutaryllysine; alternateBy similarity1
    Modified residuei214N6-acetyllysine; alternateBy similarity1
    Modified residuei214N6-glutaryllysine; alternateBy similarity1
    Modified residuei214N6-succinyllysine; alternateBy similarity1
    Modified residuei219N6-acetyllysine; alternateBy similarity1
    Modified residuei219N6-glutaryllysine; alternateBy similarity1
    Modified residuei228N6-acetyllysine; alternateBy similarity1
    Modified residuei228N6-glutaryllysine; alternateBy similarity1
    Modified residuei237N6-glutaryllysineBy similarity1
    Modified residuei279N6-acetyllysineBy similarity1
    Modified residuei280N6-acetyllysine; alternateBy similarity1
    Modified residuei280N6-glutaryllysine; alternateBy similarity1
    Modified residuei287N6-acetyllysine; alternateBy similarity1
    Modified residuei287N6-succinyllysine; alternateBy similarity1
    Modified residuei307N6-acetyllysine; alternateBy similarity1
    Modified residuei307N6-glutaryllysine; alternateBy similarity1
    Modified residuei307N6-succinyllysine; alternateBy similarity1
    Modified residuei310N6-acetyllysine; alternateBy similarity1
    Modified residuei310N6-glutaryllysine; alternateBy similarity1
    Modified residuei400N6-succinyllysineBy similarity1
    Modified residuei402N6-glutaryllysine; alternateBy similarity1
    Modified residuei402N6-succinyllysine; alternateBy similarity1
    Modified residuei412N6-acetyllysine; alternateBy similarity1
    Modified residuei412N6-glutaryllysine; alternateBy similarity1
    Modified residuei412N6-succinyllysine; alternateBy similarity1
    Modified residuei453N6-acetyllysine; alternateBy similarity1
    Modified residuei453N6-glutaryllysine; alternateBy similarity1
    Modified residuei458N6-acetyllysine; alternateBy similarity1
    Modified residuei458N6-glutaryllysine; alternateBy similarity1
    Modified residuei458N6-succinyllysine; alternateBy similarity1
    Modified residuei522N6-acetyllysine; alternateBy similarity1
    Modified residuei522N6-succinyllysine; alternateBy similarity1
    Modified residuei527N6-acetyllysine; alternateBy similarity1
    Modified residuei527N6-glutaryllysine; alternateBy similarity1
    Modified residuei527N6-succinyllysine; alternateBy similarity1
    Modified residuei532N6-acetyllysine; alternateBy similarity1
    Modified residuei532N6-glutaryllysine; alternateBy similarity1
    Modified residuei537Phosphoserine; alternateCombined sources1
    Glycosylationi537O-linked (GlcNAc); alternate1 Publication1
    Modified residuei540PhosphoserineCombined sources1
    Modified residuei553N6-acetyllysine; alternateBy similarity1
    Modified residuei553N6-glutaryllysine; alternateBy similarity1
    Modified residuei553N6-succinyllysine; alternateBy similarity1
    Modified residuei560N6-acetyllysine; alternateBy similarity1
    Modified residuei560N6-succinyllysine; alternateBy similarity1
    Modified residuei569PhosphoserineBy similarity1
    Modified residuei575N6-acetyllysine; alternateBy similarity1
    Modified residuei575N6-succinyllysine; alternateBy similarity1
    Modified residuei603N6-acetyllysine; alternateBy similarity1
    Modified residuei603N6-succinyllysine; alternateBy similarity1
    Modified residuei612N6-acetyllysine; alternateBy similarity1
    Modified residuei612N6-succinyllysine; alternateBy similarity1
    Modified residuei630N6-acetyllysineBy similarity1
    Modified residuei728N6-glutaryllysineBy similarity1
    Modified residuei751N6-acetyllysine; alternateBy similarity1
    Modified residuei751N6-succinyllysine; alternateBy similarity1
    Modified residuei757N6-acetyllysine; alternateBy similarity1
    Modified residuei757N6-glutaryllysine; alternateBy similarity1
    Modified residuei757N6-succinyllysine; alternateBy similarity1
    Modified residuei772N6-acetyllysine; alternateBy similarity1
    Modified residuei772N6-glutaryllysine; alternateBy similarity1
    Modified residuei793N6-acetyllysine; alternateBy similarity1
    Modified residuei793N6-glutaryllysine; alternateBy similarity1
    Modified residuei793N6-succinyllysine; alternateBy similarity1
    Modified residuei811N6-acetyllysine; alternateBy similarity1
    Modified residuei811N6-glutaryllysine; alternateBy similarity1
    Modified residuei831N6-acetyllysine; alternateBy similarity1
    Modified residuei831N6-succinyllysine; alternateBy similarity1
    Modified residuei841N6-acetyllysine; alternateBy similarity1
    Modified residuei841N6-glutaryllysine; alternateBy similarity1
    Modified residuei856N6-acetyllysine; alternateBy similarity1
    Modified residuei856N6-glutaryllysine; alternateBy similarity1
    Modified residuei869N6-glutaryllysineBy similarity1
    Modified residuei875N6-acetyllysine; alternateBy similarity1
    Modified residuei875N6-glutaryllysine; alternateBy similarity1
    Modified residuei875N6-succinyllysine; alternateBy similarity1
    Modified residuei889N6-acetyllysine; alternateBy similarity1
    Modified residuei889N6-glutaryllysine; alternateBy similarity1
    Modified residuei889N6-succinyllysine; alternateBy similarity1
    Modified residuei892N6-acetyllysine; alternateBy similarity1
    Modified residuei892N6-glutaryllysine; alternateBy similarity1
    Modified residuei892N6-succinyllysine; alternateBy similarity1
    Modified residuei896PhosphoserineCombined sources1
    Modified residuei898PhosphoserineCombined sources1
    Modified residuei908N6-acetyllysine; alternateBy similarity1
    Modified residuei908N6-glutaryllysine; alternateBy similarity1
    Modified residuei915N6-acetyllysine; alternateBy similarity1
    Modified residuei915N6-glutaryllysine; alternateBy similarity1
    Modified residuei915N6-succinyllysine; alternateBy similarity1
    Modified residuei919N6-acetyllysine; alternateBy similarity1
    Modified residuei919N6-glutaryllysine; alternateBy similarity1
    Modified residuei919N6-succinyllysine; alternateBy similarity1
    Modified residuei935N6-acetyllysineBy similarity1
    Modified residuei1036PhosphoserineCombined sources1
    Modified residuei1074N6-acetyllysine; alternateBy similarity1
    Modified residuei1074N6-glutaryllysine; alternateBy similarity1
    Modified residuei1074N6-succinyllysine; alternateBy similarity1
    Modified residuei1079PhosphoserineBy similarity1
    Modified residuei1090PhosphoserineCombined sources1
    Modified residuei1093PhosphoserineCombined sources1
    Modified residuei1100N6-acetyllysine; alternateBy similarity1
    Modified residuei1100N6-succinyllysine; alternateBy similarity1
    Modified residuei1149N6-succinyllysineBy similarity1
    Modified residuei1168N6-acetyllysine; alternateBy similarity1
    Modified residuei1168N6-glutaryllysine; alternateBy similarity1
    Modified residuei1168N6-succinyllysine; alternateBy similarity1
    Modified residuei1183N6-acetyllysine; alternateBy similarity1
    Modified residuei1183N6-glutaryllysine; alternateBy similarity1
    Modified residuei1183N6-succinyllysine; alternateBy similarity1
    Modified residuei1203PhosphoserineBy similarity1
    Modified residuei1222N6-acetyllysineBy similarity1
    Modified residuei1224N6-glutaryllysineBy similarity1
    Modified residuei1232N6-acetyllysine; alternateBy similarity1
    Modified residuei1232N6-succinyllysine; alternateBy similarity1
    Modified residuei1269N6-acetyllysine; alternateBy similarity1
    Modified residuei1269N6-succinyllysine; alternateBy similarity1
    Modified residuei1291N6-acetyllysine; alternateBy similarity1
    Modified residuei1291N6-succinyllysine; alternateBy similarity1
    Glycosylationi1331O-linked (GlcNAc)1 Publication1
    Glycosylationi1332O-linked (GlcNAc)1 Publication1
    Modified residuei1356N6-acetyllysine; alternateBy similarity1
    Modified residuei1356N6-glutaryllysine; alternateBy similarity1
    Modified residuei1356N6-succinyllysine; alternateBy similarity1
    Modified residuei1360N6-glutaryllysine; alternateBy similarity1
    Modified residuei1360N6-succinyllysine; alternateBy similarity1
    Modified residuei1419PhosphoserineBy similarity1
    Modified residuei1431PhosphoserineCombined sources1
    Modified residuei1444N6-acetyllysine; alternateBy similarity1
    Modified residuei1444N6-succinyllysine; alternateBy similarity1
    Modified residuei1471N6-acetyllysine; alternateBy similarity1
    Modified residuei1471N6-succinyllysine; alternateBy similarity1
    Modified residuei1479N6-acetyllysine; alternateBy similarity1
    Modified residuei1479N6-glutaryllysine; alternateBy similarity1
    Modified residuei1479N6-succinyllysine; alternateBy similarity1
    Modified residuei1486N6-acetyllysine; alternateBy similarity1
    Modified residuei1486N6-glutaryllysine; alternateBy similarity1
    Modified residuei1486N6-succinyllysine; alternateBy similarity1

    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. Undergoes proteolytic cleavage in the C-terminal region corresponding to the loss of approximately 12 AA residues from the C-terminus (PubMed:23649895).1 Publication
    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

    iPTMnetiP07756.
    PhosphoSitePlusiP07756.
    SwissPalmiP07756.

    Expressioni

    Tissue specificityi

    Primarily in the liver and small intestine.

    Gene expression databases

    BgeeiENSRNOG00000013704.
    GenevisibleiP07756. RN.

    Interactioni

    Subunit structurei

    Can form homooligomers (monomers as predominant form and dimers).By similarity

    GO - Molecular functioni

    • protein complex binding Source: RGD

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000019021.

    Structurei

    3D structure databases

    ProteinModelPortaliP07756.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini219 – 404Glutamine amidotransferase type-1Add BLAST186
    Domaini551 – 743ATP-grasp 1Add BLAST193
    Domaini1093 – 1284ATP-grasp 2Add BLAST192

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni39 – 218Anthranilate phosphoribosyltransferase homologAdd BLAST180

    Domaini

    The type-1 glutamine amidotransferase domain is defective.

    Sequence similaritiesi

    Contains 2 ATP-grasp domains.Curated

    Keywords - Domaini

    Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiKOG0370. Eukaryota.
    COG0458. LUCA.
    COG0505. LUCA.
    GeneTreeiENSGT00390000015604.
    HOGENOMiHOG000234583.
    HOVERGENiHBG000279.
    InParanoidiP07756.
    KOiK01948.
    OMAiMPWSRFR.
    OrthoDBiEOG091G00DC.
    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. 1 hit.
    InterProiIPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR006275. CarbamoylP_synth_lsu.
    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]
    PfamiPF02786. 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_017072.2.
    XP_017452081.1. XM_017596592.1.
    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_017072.2.
    XP_017452081.1. XM_017596592.1.
    UniGeneiRn.53968.

    3D structure databases

    ProteinModelPortaliP07756.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000019021.

    Protein family/group databases

    MEROPSiC26.951.

    PTM databases

    iPTMnetiP07756.
    PhosphoSitePlusiP07756.
    SwissPalmiP07756.

    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

    eggNOGiKOG0370. Eukaryota.
    COG0458. LUCA.
    COG0505. LUCA.
    GeneTreeiENSGT00390000015604.
    HOGENOMiHOG000234583.
    HOVERGENiHBG000279.
    InParanoidiP07756.
    KOiK01948.
    OMAiMPWSRFR.
    OrthoDBiEOG091G00DC.
    PhylomeDBiP07756.

    Enzyme and pathway databases

    ReactomeiR-RNO-70635. Urea cycle.
    SABIO-RKP07756.

    Miscellaneous databases

    PROiP07756.

    Gene expression databases

    BgeeiENSRNOG00000013704.
    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. 1 hit.
    InterProiIPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR006275. CarbamoylP_synth_lsu.
    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]
    PfamiPF02786. 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...

    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: November 30, 2016
    This is version 152 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

    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 one 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.