Q4VK78 (ARGI2_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 48.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Arginase-2, mitochondrial EC=3.5.3.1 Alternative name(s): Type II arginase | ||
| Gene names |
| ||
| Organism | Oryctolagus cuniculus (Rabbit) [Complete proteome] | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 354 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis By similarity. |
| Catalytic activity | L-arginine + H2O = L-ornithine + urea. |
| Cofactor | Binds 2 manganese ions per subunit By similarity. |
| Pathway | Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. |
| Subunit structure | Homotrimer By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the arginase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Arginine metabolism Urea cycle |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Manganese Metal-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | arginine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW urea cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | arginase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 22 | 22 | Mitochondrion Potential | ||||||
| Chain | 23 – 354 | 332 | Arginase-2, mitochondrial | PRO_0000044614 | |||||
Regions | |||||||||
| Region | 145 – 149 | 5 | Substrate binding By similarity | ||||||
| Region | 156 – 158 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 120 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 143 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 143 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 145 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 147 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 251 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 251 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 253 | 1 | Manganese 2 By similarity | ||||||
| Binding site | 202 | 1 | Substrate By similarity | ||||||
| Binding site | 296 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Chondrocyte phenotype-specific gene." Ah-Ra K., Yun Hyun H., Jang-Soo C. Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY864853 mRNA. Translation: AAX58119.1. |
| RefSeq | NP_001075650.1. NM_001082181.1. |
| UniGene | Ocu.3304. |
3D structure databases | |
| ProteinModelPortal | Q4VK78. |
| SMR | Q4VK78. Positions 24-329. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q4VK78. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100008967. |
Organism-specific databases | |
| CTD | 384. |
Phylogenomic databases | |
| GeneTree | ENSGT00530000063082. |
| HOVERGEN | HBG003030. |
| OrthoDB | EOG4FR0S2. |
Family and domain databases | |
| InterPro | IPR014033. Arginase_subgr. IPR006035. Ureohydrolase. IPR023696. Ureohydrolase_domain. IPR020855. Ureohydrolase_Mn_BS. [Graphical view] |
| Gene3D | G3DSA:3.40.800.10. Ureohydrolase. 1 hit. |
| PANTHER | PTHR11358:SF2. Arginase_sub. 1 hit. PTHR11358. Ureohydrolase. 1 hit. |
| Pfam | PF00491. Arginase. 1 hit. [Graphical view] |
| PIRSF | PIRSF036979. Arginase. 1 hit. |
| PRINTS | PR00116. ARGINASE. |
| TIGRFAMs | TIGR01229. RocF_arginase. 1 hit. |
| PROSITE | PS01053. ARGINASE_1. 1 hit. PS51409. ARGINASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ARGI2_RABIT | ||||||||
| Accession | Primary (citable) accession number: Q4VK78 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with