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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

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

GO - Biological processi

  1. anion homeostasis Source: RGD
  2. arginine biosynthetic process Source: GO_Central
  3. carbamoyl phosphate biosynthetic process Source: InterPro
  4. cellular response to cAMP Source: RGD
  5. cellular response to fibroblast growth factor stimulus Source: RGD
  6. cellular response to glucagon stimulus Source: RGD
  7. cellular response to oleic acid Source: RGD
  8. glutamine catabolic process Source: InterPro
  9. glycogen catabolic process Source: Ensembl
  10. hepatocyte differentiation Source: RGD
  11. homocysteine metabolic process Source: Ensembl
  12. liver development Source: RGD
  13. midgut development Source: RGD
  14. nitric oxide metabolic process Source: Ensembl
  15. positive regulation of vasodilation Source: Ensembl
  16. proteolysis Source: GOC
  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
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

  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
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-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 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 – 5371Phosphoserine; alternateBy similarity
Glycosylationi537 – 5371O-linked (GlcNAc); alternate1 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 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 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 residuei1203 – 12031PhosphoserineBy 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 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-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.
OMAiQFIEFEG.
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.
OMAiQFIEFEG.
OrthoDBiEOG7M6D6F.
PhylomeDBiP07756.

Enzyme and pathway databases

ReactomeiREACT_328693. Urea cycle.
SABIO-RKP07756.

Miscellaneous databases

NextBioi697797.
PROiP07756.

Gene expression databases

GenevestigatoriP07756.

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: April 1, 2015
This is version 137 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.