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Reviewed, UniProtKB/Swiss-Prot P07756 (CPSM_RAT)

Last modified October 13, 2009. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Carbamoyl-phosphate synthase [ammonia], mitochondrial
    EC=6.3.4.16
Alternative name(s):
    Carbamoyl-phosphate synthetase I
      Short name=CPSase I
Gene names
Name: Cps1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length1500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

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

Catalytic activity

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

Enzyme regulation

Requires N-acetylglutamate as an allosteric activator.

Subcellular location

Mitochondrion.

Tissue specificity

Primarily in the liver and small intestine.

Domain

The type-1 glutamine amidotransferase domain is defective.

Post-translational modification

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.

Sequence similarities

Contains 2 ATP-grasp domains.

Contains 1 glutamine amidotransferase type-1 domain.

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Ontologies

Keywords
   Biological processUrea cycle
   Cellular componentMitochondrion
   DomainRepeat
Transit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological processanion homeostasis

Inferred from direct assay. Source: RGD

glutamine metabolic process

Inferred from electronic annotation. Source: InterPro

response to amine stimulus

Inferred from expression pattern. Source: RGD

response to cAMP

Inferred from expression pattern. Source: RGD

response to drug

Inferred from expression pattern. Source: RGD

response to glucagon stimulus

Inferred from expression pattern. Source: RGD

response to glucocorticoid stimulus

Inferred from expression pattern. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern. Source: RGD

response to oleic acid

Inferred from expression pattern. Source: RGD

response to starvation

Inferred from expression pattern. Source: RGD

urea cycle

Inferred from direct assay. Source: RGD

   Cellular componentmitochondrial inner membrane

Inferred from direct assay. Source: RGD

protein complex

Inferred from direct assay. Source: RGD

   Molecular functionATP binding

Inferred from direct assay. Source: RGD

carbamoyl-phosphate synthase (ammonia) activity

Inferred from direct assay. Source: RGD

phospholipid binding

Inferred from direct assay. Source: RGD

protein complex binding

Inferred from direct assay. Source: RGD

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3838Mitochondrion
Chain39 – 15001462Carbamoyl-phosphate synthase [ammonia], mitochondrial
PRO_0000029899

Regions

Domain219 – 404186Glutamine amidotransferase type-1
Domain551 – 743193ATP-grasp 1
Domain1093 – 1284192ATP-grasp 2
Region39 – 218180Anthranilate phosphoribosyltransferase homolog

Amino acid modifications

Modified residue551N6-acetyllysine By similarity
Modified residue1191N6-acetyllysine By similarity
Modified residue2871N6-acetyllysine By similarity
Modified residue5271N6-acetyllysine By similarity
Modified residue6031N6-acetyllysine By similarity
Modified residue8411N6-acetyllysine By similarity
Modified residue8921N6-acetyllysine By similarity
Modified residue8981Phosphoserine By similarity
Modified residue12911N6-acetyllysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
P07756-1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 038E8F893DE1C34D

FASTA1,500164,580
        10         20         30         40         50         60 
MTRILTACKV VKTLKSGFGL ANVTSKRQWD FSRPGIRLLS VKAQTAHIVL EDGTKMKGYS 

        70         80         90        100        110        120 
FGHPSSVAGE VVFNTGLGGY SEALTDPAYK GQILTMANPI IGNGGAPDTT ARDELGLNKY 

       130        140        150        160        170        180 
MESDGIKVAG LLVLNYSHDY NHWLATKSLG QWLQEEKVPA IYGVDTRMLT KIIRDKGTML 

       190        200        210        220        230        240 
GKIEFEGQSV DFVDPNKQNL IAEVSTKDVK VFGKGNPTKV VAVDCGIKNN VIRLLVKRGA 

       250        260        270        280        290        300 
EVHLVPWNHD FTQMDYDGLL IAGGPGNPAL AQPLIQNVKK ILESDRKEPL FGISTGNIIT 

       310        320        330        340        350        360 
GLAAGAKSYK MSMANRGQNQ PVLNITNRQA FITAQNHGYA LDNTLPAGWK PLFVNVNDQT 

       370        380        390        400        410        420 
NEGIMHESKP FFAVQFHPEV SPGPTDTEYL FDSFFSLIKK GKGTTITSVL PKPALVASRV 

       430        440        450        460        470        480 
EVSKVLILGS GGLSIGQAGE FDYSGSQAVK AMKEENVKTV LMNPNIASVQ TNEVGLKQAD 

       490        500        510        520        530        540 
AVYFLPITPQ FVTEVIKAER PDGLILGMGG QTALNCGVEL FKRGVLKEYG VKVLGTSVES 

       550        560        570        580        590        600 
IMATEDRQLF SDKLNEINEK IAPSFAVESM EDALKAADTI GYPVMIRSAY ALGGLGSGIC 

       610        620        630        640        650        660 
PNKETLMDLG TKAFAMTNQI LVERSVTGWK EIEYEVVRDA DDNCVTVCNM ENVDAMGVHT 

       670        680        690        700        710        720 
GDSVVVAPAQ TLSNAEFQML RRTSINVVRH LGIVGECNIQ FALHPTSMEY CIIEVNARLS 

       730        740        750        760        770        780 
RSSALASKAT GYPLAFIAAK IALGIPLPEI KNVVSGKTSA CFEPSLDYMV TKIPRWDLDR 

       790        800        810        820        830        840 
FHGTSSRIGS SMKSVGEVMA IGRTFEESFQ KALRMCHPSV DGFTPRLPMN KEWPANLDLR 

       850        860        870        880        890        900 
KELSEPSSTR IYAIAKALEN NMSLDEIVKL TSIDKWFLYK MRDILNMDKT LKGLNSESVT 

       910        920        930        940        950        960 
EETLRQAKEI GFSDKQISKC LGLTEAQTRE LRLKKNIHPW VKQIDTLAAE YPSVTNYLYV 

       970        980        990       1000       1010       1020 
TYNGQEHDIK FDEHGIMVLG CGPYHIGSSV EFDWCAVSSI RTLRQLGKKT VVVNCNPETV 

      1030       1040       1050       1060       1070       1080 
STDFDECDKL YFEELSLERI LDIYHQEACN GCIISVGGQI PNNLAVPLYK NGVKIMGTSP 

      1090       1100       1110       1120       1130       1140 
LQIDRAEDRS IFSAVLDELK VAQAPWKAVN TLNEALEFAN SVGYPCLLRP SYVLSGSAMN 

      1150       1160       1170       1180       1190       1200 
VVFSEDEMKR FLEEATRVSQ EHPVVLTKFI EGAREVEMDA VGKEGRVISH AISEHVEDAG 

      1210       1220       1230       1240       1250       1260 
VHSGDATLML PTQTISQGAI EKVKDATRKI AKAFAISGPF NVQFLVKGND VLVIECNLRA 

      1270       1280       1290       1300       1310       1320 
SRSFPFVSKT LGVDFIDVAT KVMIGESVDE KHLPTLEQPI IPSDYVAIKA PMFSWPRLRD 

      1330       1340       1350       1360       1370       1380 
ADPILRCEMA STGEVACFGE GIHTAFLKAM LSTGFKIPQK GILIGIQQSF RPRFLGVAEQ 

      1390       1400       1410       1420       1430       1440 
LHNEGFKLFA TEATSDWLNA NNVPATPVAW PSQEGQNPSL SSIRKLIRDG SIDLVINLPN 

      1450       1460       1470       1480       1490       1500 
NNTKFVHDNY VIRRTAVDSG IALLTNFQVT KLFAEAVQKA RTVDSKSLFH YRQYSAGKAA

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References

[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: 2991241] [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: 3038878] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M12335 expand/collapse EMBL AC list , M11710, M12318, M12319, M12320, M12321, M12322, M12323, M12324, M12325, M12326, M12327, M12328 Genomic DNA. Translation: AAB59717.1.
J02805 Genomic DNA. Translation: AAA40959.1.
IPIIPI00210644.
PIRSYRTCA. A28481.
RefSeqNP_058768.1.
UniGeneRn.53968

3D structure databases

HSSPHSSP built from PDB template 1M6V based on UniProtKB P00968.
ModBaseSearch...

Protein-protein interaction databases

STRINGP07756.

Protein family/group databases

MEROPSC26.951.

PTM databases

PhosphoSiteP07756.

Proteomic databases

PRIDEP07756.

Genome annotation databases

EnsemblENSRNOT00000019023; ENSRNOP00000019021; ENSRNOG00000013704; Rattus norvegicus. [Genome view]
GeneID497840.
KEGGrno:497840.

Organism-specific databases

CTD497840.
RGD2395. Cps1.

Phylogenomic databases

HOVERGENP07756.

Enzyme and pathway databases

BRENDA6.3.4.16. 248.

Gene expression databases

ArrayExpressP07756.
GenevestigatorP07756.
GermOnlineENSRNOG00000013704. Rattus norvegicus.

Family and domain databases

InterProIPR011761. ATP-grasp.
IPR013816. ATP_grasp_subdomain_2.
IPR001317. CarbamoylP_synth_GATase.
IPR005483. CarbamoylP_synth_lsu.
IPR005479. CarbamoylP_synth_lsu_ATP-bd.
IPR006275. CarbamoylP_synth_lsu_Gln-dep.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
IPR011607. MGS.
IPR013817. Pre-ATP_grasp.
[Graphical view]
Gene3DG3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits.
G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
PfamPF00289. 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]
PRINTSPR00098. CPSASE.
PR00099. CPSGATASE.
TIGRFAMsTIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio697797.

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Entry information

Entry nameCPSM_RAT
AccessionPrimary (citable) accession number: P07756
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 13, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents