Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

CAD protein

Gene

Cad

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).By similarity

Miscellaneous

GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 3 Zn2+ ions per subunit (for dihydroorotase activity).By similarity
  • Mg2+PROSITE-ProRule annotation, Mn2+PROSITE-ProRule annotationNote: Binds 4 magnesium or manganese ions per subunit.PROSITE-ProRule annotation

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Allosterically regulated and controlled by phosphorylation. 5-phosphoribose 1-diphosphate (PRPP) is an activator while UMP and UTP are inhibitors of the CPSase reaction (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1, 2 and 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. CAD protein (Cad)
  2. CAD protein (Cad)
  3. CAD protein (Cad)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei252Nucleophile; for GATase activityPROSITE-ProRule annotation1
Active sitei336For GATase activityPROSITE-ProRule annotation1
Active sitei338For GATase activityPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi668Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi682Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi682Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi684Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi1202Magnesium or manganese 3PROSITE-ProRule annotation1
Metal bindingi1214Magnesium or manganese 3PROSITE-ProRule annotation1
Metal bindingi1214Magnesium or manganese 4PROSITE-ProRule annotation1
Metal bindingi1216Magnesium or manganese 4PROSITE-ProRule annotation1
Metal bindingi1471Zinc 1; via tele nitrogenBy similarity1
Metal bindingi1471Zinc 2; via pros nitrogenBy similarity1
Metal bindingi1473Zinc 1; via tele nitrogenBy similarity1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1475N-carbamoyl-L-aspartateBy similarity1
Binding sitei1505N-carbamoyl-L-aspartateBy similarity1
Metal bindingi1556Zinc 1; via carbamate groupBy similarity1
Metal bindingi1556Zinc 3; via carbamate groupBy similarity1
Metal bindingi1590Zinc 3; via pros nitrogenBy similarity1
Metal bindingi1613Zinc 2By similarity1
Metal bindingi1614Zinc 3; via tele nitrogenBy similarity1
Metal bindingi1637Zinc 2By similarity1
Binding sitei1661N-carbamoyl-L-aspartate; via amide nitrogen and carbonyl oxygenBy similarity1
Metal bindingi1686Zinc 1By similarity1
Binding sitei1686N-carbamoyl-L-aspartateBy similarity1
Binding sitei1690N-carbamoyl-L-aspartateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi545 – 600ATPPROSITE-ProRule annotationAdd BLAST56
Nucleotide bindingi1078 – 1135ATPPROSITE-ProRule annotationAdd BLAST58

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Hydrolase, Ligase, Multifunctional enzyme, Transferase
Biological processPyrimidine biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-500753 Pyrimidine biosynthesis

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00070;UER00115

UPA00070;UER00116

UPA00070;UER00117

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
CAD protein
Including the following 3 domains:
Glutamine-dependent carbamoyl-phosphate synthase (EC:6.3.5.5By similarity)
Aspartate carbamoyltransferase (EC:2.1.3.2By similarity)
Dihydroorotase (EC:3.5.2.3By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Cad
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1916969 Cad

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2774

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004259552 – 2225CAD proteinAdd BLAST2224

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
Modified residuei456Phosphothreonine; by MAPK1By similarity1
Modified residuei747N6-acetyllysineBy similarity1
Modified residuei1038PhosphoserineBy similarity1
Modified residuei1406Phosphoserine; by PKABy similarity1
Modified residuei1411N6-acetyllysineBy similarity1
Modified residuei1556N6-carboxylysineBy similarity1
Modified residuei1859PhosphoserineCombined sources1
Modified residuei1884PhosphothreonineBy similarity1
Modified residuei1900PhosphoserineBy similarity1
Modified residuei1938PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Activated by MAP kinase (Erk1/2) phosphorylation just prior to the S phase of the cell cycle, when the demand for pyrimidine nucleotides is greatest, and down-regulated as the cells emerge from S phase by protein kinase A (PKA) phosphorylation. Phosphorylation at Ser-1859 by RPS6KB1 downstream of MTOR promotes oligomerization and stimulates dihydroorotase activity. Phosphorylation at Ser-1406 reduces sensitivy to feedback inhibition by UTP (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
B2RQC6

MaxQB - The MaxQuant DataBase

More...
MaxQBi
B2RQC6

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
B2RQC6

PeptideAtlas

More...
PeptideAtlasi
B2RQC6

PRoteomics IDEntifications database

More...
PRIDEi
B2RQC6

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
B2RQC6

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
B2RQC6

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
B2RQC6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000013629 Expressed in 279 organ(s), highest expression level in white adipose tissue

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
B2RQC6 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
B2RQC6 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer. Interacts with CIPC.By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
213636, 12 interactors

Database of interacting proteins

More...
DIPi
DIP-61412N

Protein interaction database and analysis system

More...
IntActi
B2RQC6, 12 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000013773

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
B2RQC6

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
B2RQC6

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
B2RQC6

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini177 – 363Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd BLAST187
Domaini519 – 711ATP-grasp 1PROSITE-ProRule annotationAdd BLAST193
Domaini1052 – 1243ATP-grasp 2PROSITE-ProRule annotationAdd BLAST192
Domaini1308 – 1462MGS-likePROSITE-ProRule annotationAdd BLAST155

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 365GATase (Glutamine amidotransferase)By similarityAdd BLAST364
Regioni366 – 394LinkerBy similarityAdd BLAST29
Regioni395 – 1455CPSase (Carbamoyl-phosphate synthase)By similarityAdd BLAST1061
Regioni395 – 933CPSase ABy similarityAdd BLAST539
Regioni934 – 1455CPSase BBy similarityAdd BLAST522
Regioni1456 – 1788DHOase (dihydroorotase)By similarityAdd BLAST333
Regioni1789 – 1917LinkerBy similarityAdd BLAST129
Regioni1918 – 2225ATCase (Aspartate transcarbamylase)By similarityAdd BLAST308

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.Curated

Keywords - Domaini

Glutamine amidotransferase, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0370 Eukaryota
COG0458 LUCA
COG0505 LUCA
COG0540 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157241

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234584

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000279

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
B2RQC6

KEGG Orthology (KO)

More...
KOi
K11540

Identification of Orthologs from Complete Genome Data

More...
OMAi
FTNANDH

Database of Orthologous Groups

More...
OrthoDBi
EOG091G00DC

Database for complete collections of gene phylogenies

More...
PhylomeDBi
B2RQC6

TreeFam database of animal gene trees

More...
TreeFami
TF105604

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01744 GATase1_CPSase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1030.10, 1 hit
3.30.1490.20, 1 hit
3.40.50.1370, 2 hits
3.40.50.1380, 1 hit
3.40.50.880, 1 hit
3.50.30.20, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00001 Asp_carb_tr, 1 hit
MF_01209 CPSase_S_chain, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006680 Amidohydro-rel
IPR006132 Asp/Orn_carbamoyltranf_P-bd
IPR006130 Asp/Orn_carbamoylTrfase
IPR036901 Asp/Orn_carbamoylTrfase_sf
IPR002082 Asp_carbamoyltransf
IPR006131 Asp_carbamoyltransf_Asp/Orn-bd
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR006275 CarbamoylP_synth_lsu
IPR005480 CarbamoylP_synth_lsu_oligo
IPR036897 CarbamoylP_synth_lsu_oligo_sf
IPR006274 CarbamoylP_synth_ssu
IPR002474 CarbamoylP_synth_ssu_N
IPR036480 CarbP_synth_ssu_N_sf
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR005483 CbamoylP_synth_lsu_CPSase_dom
IPR029062 Class_I_gatase-like
IPR035686 CPSase_GATase1
IPR002195 Dihydroorotase_CS
IPR017926 GATASE
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR016185 PreATP-grasp_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01979 Amidohydro_1, 1 hit
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
PF00185 OTCace, 1 hit
PF02729 OTCace_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00100 AOTCASE
PR00101 ATCASE
PR00098 CPSASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01096 CPSase_L_D3, 1 hit
SM01097 CPSase_sm_chain, 1 hit
SM00851 MGS, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48108 SSF48108, 1 hit
SSF51338 SSF51338, 1 hit
SSF51556 SSF51556, 1 hit
SSF52021 SSF52021, 1 hit
SSF52317 SSF52317, 1 hit
SSF52335 SSF52335, 1 hit
SSF52440 SSF52440, 2 hits
SSF53671 SSF53671, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00670 asp_carb_tr, 1 hit
TIGR01369 CPSaseII_lrg, 1 hit
TIGR01368 CPSaseIIsmall, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50975 ATP_GRASP, 2 hits
PS00097 CARBAMOYLTRANSFERASE, 1 hit
PS00866 CPSASE_1, 2 hits
PS00867 CPSASE_2, 2 hits
PS00482 DIHYDROOROTASE_1, 1 hit
PS00483 DIHYDROOROTASE_2, 1 hit
PS51273 GATASE_TYPE_1, 1 hit
PS51855 MGS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: B2RQC6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL
60 70 80 90 100
VLTYPLIGNY GIPSDEEDEF GLSKWFESSE IHVAGLVVGE CCPTPSHWSA
110 120 130 140 150
NCTLHEWLQQ RGIPGLQGVD TRELTKKLRE QGSLLGKLVQ KGTEPSALPF
160 170 180 190 200
VDPNARPLAP EVSIKTPRVF NAGGAPRICA LDCGLKYNQI RCLCQLGAEV
210 220 230 240 250
TVVPWDHELD SQKYDGLFLS NGPGDPASYP GVVSTLSRVL SEPNPRPVFG
260 270 280 290 300
ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD
310 320 330 340 350
ADSLPAGWAP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF
360 370 380 390 400
DVFLETVREA AAGNIGGQTV RERLAQRLCP PELPIPGSGL PPPRKVLILG
410 420 430 440 450
SGGLSIGQAG EFDYSGSQAI KALKEENIQT LLINPNIATV QTSQGLADKV
460 470 480 490 500
YFLPITLHYV TQVIRNERPD GVLLTFGGQT ALNCGVELTK AGVLARYGVR
510 520 530 540 550
VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ AQAAAERLGY
560 570 580 590 600
PVLVRAAFAL GGLGSGFAST KEELSALVAP AFAHTSQVLI DKSLKGWKEI
610 620 630 640 650
EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRR
660 670 680 690 700
TAIKVTQHLG IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY
710 720 730 740 750
PLAYVAAKLA LGIPLPELRN SVTGGTAAFE PSLDYCVVKI PRWDLSKFLR
760 770 780 790 800
VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL RMVDENCVGF DHTVKPVSDM
810 820 830 840 850
ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM KRIVTHAQLL
860 870 880 890 900
EQHRGQALPQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
910 920 930 940 950
KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RAPHVLVLGS GVYRIGSSVE
960 970 980 990 1000
FDWCAVGCIQ QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM
1010 1020 1030 1040 1050
DIYELENPEG VILSMGGQLP NNMAMALHRQ QCRVLGTSPE AIDSAENRFK
1060 1070 1080 1090 1100
FSRLLDTIGI SQPQWRELSD LESARQFCHT VGYPCVVRPS YVLSGAAMNV
1110 1120 1130 1140 1150
AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV ACDGIVSAIA
1160 1170 1180 1190 1200
ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN
1210 1220 1230 1240 1250
LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPV
1260 1270 1280 1290 1300
GLMTGSGVVG VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL
1310 1320 1330 1340 1350
KAMLSTGFKI PEKNILLTIG SYKNKSELLP TVRLLESLGY SLYASLGTAD
1360 1370 1380 1390 1400
FYTEHGVKVT AVDWHFEEAV DGECPPQRSI LDQLAENHFE LVINLSMRGA
1410 1420 1430 1440 1450
GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL GQIGPAPPLK
1460 1470 1480 1490 1500
VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGVTMV
1510 1520 1530 1540 1550
CAMPNTRPPI IDAPALALAQ KLAEAGARCD FTLFLGASSE NAGTLGAVAG
1560 1570 1580 1590 1600
SAAGLKLYLN ETFSELRLDS VAQWMEHFET WPAHLPIVAH AERQSVAAVL
1610 1620 1630 1640 1650
MVAQLTQRPV HICHVARKEE ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL
1660 1670 1680 1690 1700
ERLGPGKGEV RPELGSREDM EALWENMAVI DCFASDHAPH TLEEKCGPKP
1710 1720 1730 1740 1750
PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF HLPLQEDTYV
1760 1770 1780 1790 1800
EVDLEHEWTV PSHMPFSKAR WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL
1810 1820 1830 1840 1850
VPPGYGQDVR KWPQGVVPQP PPSTPATTEI TTTPERPRRV IPGLPDGRFH
1860 1870 1880 1890 1900
LPPRIHRASD PGLPAEEPKE KPPRKVVEPE LMGTPDGPCY PAPPVPRQAS
1910 1920 1930 1940 1950
PQNLGSSGLL HPQMSPLLHS LVGQHILSVK QFTKDQMSHL FNVAHTLRMM
1960 1970 1980 1990 2000
VQKERSLDIL KGKVMASMFY EVSTRTSSSF AAAMARLGGA VLSFSEATSS
2010 2020 2030 2040 2050
VQKGESLADS VQTMSCYADV IVLRHPQPGA VELAAKHCRR PVINAGDGVG
2060 2070 2080 2090 2100
EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
2110 2120 2130 2140 2150
LRYVAPPSLR MPPSVRDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE
2160 2170 2180 2190 2200
RFGSVQEYEA CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR
2210 2220
AAYFRQAENG MYIRMALLAT VLGRF
Length:2,225
Mass (Da):243,238
Last modified:July 1, 2008 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE7E606A0F650ABB4
GO
Isoform 2 (identifier: B2RQC6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1962-2032: Missing.

Show »
Length:2,154
Mass (Da):235,851
Checksum:iA83FA6E22929070C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3UWN2G3UWN2_MOUSE
CAD protein
Cad
2,164Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9QAI5E9QAI5_MOUSE
CAD protein
Cad
2,162Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9QAT6E9QAT6_MOUSE
CAD protein
Cad
971Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F6S3Z3F6S3Z3_MOUSE
CAD protein
Cad
194Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0539121962 – 2032Missing in isoform 2. 1 PublicationAdd BLAST71

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AC109608 Genomic DNA No translation available.
CH466524 Genomic DNA Translation: EDL37329.1
BC137856 mRNA Translation: AAI37857.1
BC144972 mRNA Translation: AAI44973.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS19171.1 [B2RQC6-1]
CCDS80246.1 [B2RQC6-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001276451.1, NM_001289522.1 [B2RQC6-2]
NP_076014.1, NM_023525.2 [B2RQC6-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.305535

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000013773; ENSMUSP00000013773; ENSMUSG00000013629 [B2RQC6-1]
ENSMUST00000201182; ENSMUSP00000144684; ENSMUSG00000013629 [B2RQC6-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
69719

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:69719

UCSC genome browser

More...
UCSCi
uc008wwz.2 mouse [B2RQC6-1]
uc012duk.2 mouse [B2RQC6-2]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC109608 Genomic DNA No translation available.
CH466524 Genomic DNA Translation: EDL37329.1
BC137856 mRNA Translation: AAI37857.1
BC144972 mRNA Translation: AAI44973.1
CCDSiCCDS19171.1 [B2RQC6-1]
CCDS80246.1 [B2RQC6-2]
RefSeqiNP_001276451.1, NM_001289522.1 [B2RQC6-2]
NP_076014.1, NM_023525.2 [B2RQC6-1]
UniGeneiMm.305535

3D structure databases

ProteinModelPortaliB2RQC6
SMRiB2RQC6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213636, 12 interactors
DIPiDIP-61412N
IntActiB2RQC6, 12 interactors
STRINGi10090.ENSMUSP00000013773

Chemistry databases

BindingDBiB2RQC6
ChEMBLiCHEMBL2774

PTM databases

iPTMnetiB2RQC6
PhosphoSitePlusiB2RQC6
SwissPalmiB2RQC6

Proteomic databases

EPDiB2RQC6
MaxQBiB2RQC6
PaxDbiB2RQC6
PeptideAtlasiB2RQC6
PRIDEiB2RQC6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000013773; ENSMUSP00000013773; ENSMUSG00000013629 [B2RQC6-1]
ENSMUST00000201182; ENSMUSP00000144684; ENSMUSG00000013629 [B2RQC6-2]
GeneIDi69719
KEGGimmu:69719
UCSCiuc008wwz.2 mouse [B2RQC6-1]
uc012duk.2 mouse [B2RQC6-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
790
MGIiMGI:1916969 Cad

Phylogenomic databases

eggNOGiKOG0370 Eukaryota
COG0458 LUCA
COG0505 LUCA
COG0540 LUCA
GeneTreeiENSGT00940000157241
HOGENOMiHOG000234584
HOVERGENiHBG000279
InParanoidiB2RQC6
KOiK11540
OMAiFTNANDH
OrthoDBiEOG091G00DC
PhylomeDBiB2RQC6
TreeFamiTF105604

Enzyme and pathway databases

UniPathwayi
UPA00070;UER00115

UPA00070;UER00116

UPA00070;UER00117

ReactomeiR-MMU-500753 Pyrimidine biosynthesis

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Cad mouse

Protein Ontology

More...
PROi
PR:B2RQC6

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000013629 Expressed in 279 organ(s), highest expression level in white adipose tissue
ExpressionAtlasiB2RQC6 baseline and differential
GenevisibleiB2RQC6 MM

Family and domain databases

CDDicd01744 GATase1_CPSase, 1 hit
Gene3Di1.10.1030.10, 1 hit
3.30.1490.20, 1 hit
3.40.50.1370, 2 hits
3.40.50.1380, 1 hit
3.40.50.880, 1 hit
3.50.30.20, 1 hit
HAMAPiMF_00001 Asp_carb_tr, 1 hit
MF_01209 CPSase_S_chain, 1 hit
InterProiView protein in InterPro
IPR006680 Amidohydro-rel
IPR006132 Asp/Orn_carbamoyltranf_P-bd
IPR006130 Asp/Orn_carbamoylTrfase
IPR036901 Asp/Orn_carbamoylTrfase_sf
IPR002082 Asp_carbamoyltransf
IPR006131 Asp_carbamoyltransf_Asp/Orn-bd
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR006275 CarbamoylP_synth_lsu
IPR005480 CarbamoylP_synth_lsu_oligo
IPR036897 CarbamoylP_synth_lsu_oligo_sf
IPR006274 CarbamoylP_synth_ssu
IPR002474 CarbamoylP_synth_ssu_N
IPR036480 CarbP_synth_ssu_N_sf
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR005483 CbamoylP_synth_lsu_CPSase_dom
IPR029062 Class_I_gatase-like
IPR035686 CPSase_GATase1
IPR002195 Dihydroorotase_CS
IPR017926 GATASE
IPR011059 Metal-dep_hydrolase_composite
IPR032466 Metal_Hydrolase
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR016185 PreATP-grasp_dom_sf
PfamiView protein in Pfam
PF01979 Amidohydro_1, 1 hit
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
PF00185 OTCace, 1 hit
PF02729 OTCace_N, 1 hit
PRINTSiPR00100 AOTCASE
PR00101 ATCASE
PR00098 CPSASE
SMARTiView protein in SMART
SM01096 CPSase_L_D3, 1 hit
SM01097 CPSase_sm_chain, 1 hit
SM00851 MGS, 1 hit
SUPFAMiSSF48108 SSF48108, 1 hit
SSF51338 SSF51338, 1 hit
SSF51556 SSF51556, 1 hit
SSF52021 SSF52021, 1 hit
SSF52317 SSF52317, 1 hit
SSF52335 SSF52335, 1 hit
SSF52440 SSF52440, 2 hits
SSF53671 SSF53671, 1 hit
TIGRFAMsiTIGR00670 asp_carb_tr, 1 hit
TIGR01369 CPSaseII_lrg, 1 hit
TIGR01368 CPSaseIIsmall, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 2 hits
PS00097 CARBAMOYLTRANSFERASE, 1 hit
PS00866 CPSASE_1, 2 hits
PS00867 CPSASE_2, 2 hits
PS00482 DIHYDROOROTASE_1, 1 hit
PS00483 DIHYDROOROTASE_2, 1 hit
PS51273 GATASE_TYPE_1, 1 hit
PS51855 MGS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPYR1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: B2RQC6
Secondary accession number(s): B7ZN27
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: July 1, 2008
Last modified: December 5, 2018
This is version 108 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again