CAD protein

Search for
Structures	Swiss-model
Domains	InterPro

carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase
carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase
Identifiers
Symbol	CAD
NCBI gene	790
HGNC	1424
OMIM	114010
RefSeq	NM_004341
UniProt	P27708
Other data
EC number	2.1.3.2
Locus	Chr. 2 p21
Structures
Search for
Structures	Swiss-model
Domains	InterPro

CAD
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4BY3, 4C6B, 4C6C, 4C6D, 4C6E, 4C6F, 4C6I, 4C6J, 4C6K, 4C6L, 4C6M, 4C6N, 4C6O, 4C6P, 4C6Q, 5G1P, 5G1O, 5G1N
Identifiers
Aliases	CAD, CDG1Z, carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase, GATD4, EIEE50, DEE50
External IDs	OMIM: 114010; MGI: 1916969; HomoloGene: 1412; GeneCards: CAD; OMA:CAD - orthologs
Gene location (Human)
Chr.	Chromosome 2 (human)
End	27,243,943 bp
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	31,235,823 bp
RNA expression pattern
	Top expressed in
	stromal cell of endometrium; ; right lobe of liver; ; right uterine tube; ; right lobe of thyroid gland; ; left uterine tube; ; anterior pituitary; ; tibial nerve; ; canal of the cervix; ; endothelial cell; ; left lobe of thyroid gland;
	Top expressed in
	internal carotid artery; ; external carotid artery; ; primitive streak; ; hair follicle; ; somite; ; condyle; ; yolk sac; ; abdominal wall; ; renal corpuscle; ; tongue;
	More reference expression data
	n/a
Gene ontology
Molecular function	transferase activity; protein kinase activity; nucleotide binding; amino acid binding; aspartate binding; zinc ion binding; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; metal ion binding; dihydroorotase activity; ligase activity; catalytic activity; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; carboxyl- or carbamoyltransferase activity; enzyme binding; hydrolase activity; ATP binding; aspartate carbamoyltransferase activity; carbamoyl-phosphate synthase (ammonia) activity; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; identical protein binding;
Cellular component	cytoplasm; membrane; nuclear matrix; nucleoplasm; extracellular exosome; nucleus; cytosol; cell projection; neuronal cell body; terminal bouton; protein-containing complex;
Biological process	cellular amino acid metabolic process; pyrimidine nucleoside biosynthetic process; glutamine metabolic process; nitrogen compound metabolic process; 'de novo' pyrimidine nucleobase biosynthetic process; pyrimidine nucleotide biosynthetic process; protein autophosphorylation; metabolism; peptidyl-threonine phosphorylation; 'de novo' UMP biosynthetic process; urea cycle; arginine biosynthetic process; liver development; UTP biosynthetic process; heart development; female pregnancy; lactation; response to amine; citrulline biosynthetic process; response to caffeine; animal organ regeneration; response to insulin; response to testosterone; response to starvation; response to cortisol; carbamoyl phosphate biosynthetic process; cellular response to epidermal growth factor stimulus;
	Sources:Amigo / QuickGO
Orthologs
	790
	69719
	ENSG00000084774
	ENSMUSG00000013629
	P27708
	B2RQC6
	NM_001306079; NM_004341
	NM_001289522; NM_001289523; NM_023525
	NP_001293008; NP_004332
	NP_001276451; NP_001276452; NP_076014; NP_001390328; NP_001390329
	Wikidata
View/Edit Human	View/Edit Mouse

CAD protein (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) is a trifunctional multi-domain enzyme involved in the first three steps of pyrimidine biosynthesis. De-novo synthesis starts with cytosolic carbamoylphosphate synthetase II which uses glutamine, carbon dioxide and ATP. This enzyme is inhibited by uridine triphosphate (feedback inhibition).

In 2015, the first observed pathological mutations of CAD were found in a four-year-old boy.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000084774 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000013629 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Ng, B. G.; Wolfe, L. A.; Ichikawa, M.; Markello, T.; He, M.; Tifft, C. J.; Gahl, W. A.; Freeze, H. H. (12 February 2015). "Biallelic mutations in CAD, impair de novo pyrimidine biosynthesis and decrease glycosylation precursors". Human Molecular Genetics. 24 (11): 3050–3057. doi:10.1093/hmg/ddv057.

External links

CAD+trifunctional+enzyme at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This biochemistry article is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000084774 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000013629 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] Ng, B. G.; Wolfe, L. A.; Ichikawa, M.; Markello, T.; He, M.; Tifft, C. J.; Gahl, W. A.; Freeze, H. H. (12 February 2015). "Biallelic mutations in CAD, impair de novo pyrimidine biosynthesis and decrease glycosylation precursors". Human Molecular Genetics. 24 (11): 3050–3057. doi:10.1093/hmg/ddv057.

[1]

[2]

[3]

[4]

[5]

v t e Enzymes: multienzyme complexes
Photosynthesis	Photosynthetic reaction center complex proteins Photosystem I II
Dehydrogenase	Pyruvate dehydrogenase complex E1 E2 E3 Oxoglutarate dehydrogenase OGDH DLST DLD Branched-chain alpha-keto acid dehydrogenase complex BCKDHA BCKDHB DBT DLD
Other	CAD Carbamoyl phosphate synthase II Aspartate carbamoyltransferase Dihydroorotase P450-containing systems Cytochrome b6f complex Electron transport chain Fatty acid synthetase complex Glycine decarboxylase complex Mitochondrial trifunctional protein HADHA HADHB Phosphoenolpyruvate sugar phosphotransferase system Polyketide synthase Sucrase-isomaltase complex Tryptophan synthase

v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase
3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase
3.5.5: Nitriles/ Aminohydrolases	Nitrilase
3.5.99: Other	Riboflavinase Thiaminase II

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)