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Q4VK78 (ARGI2_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginase-2, mitochondrial

EC=3.5.3.1
Alternative name(s):
Type II arginase
Gene names
Name:ARG2
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Mitochondrion.

Sequence similarities

Belongs to the arginase family.

Ontologies

Keywords
   Biological processArginine metabolism
Urea cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

urea cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionarginase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion Potential
Chain23 – 354332Arginase-2, mitochondrial
PRO_0000044614

Regions

Region145 – 1495Substrate binding By similarity
Region156 – 1583Substrate binding By similarity

Sites

Metal binding1201Manganese 1 By similarity
Metal binding1431Manganese 1 By similarity
Metal binding1431Manganese 2 By similarity
Metal binding1451Manganese 2 By similarity
Metal binding1471Manganese 1 By similarity
Metal binding2511Manganese 1 By similarity
Metal binding2511Manganese 2 By similarity
Metal binding2531Manganese 2 By similarity
Binding site2021Substrate By similarity
Binding site2961Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4VK78 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 23313E232A8B6E8E

FASTA35438,393
        10         20         30         40         50         60 
MSYGSCVSRL LRTRVQSVLK KSVHSVAVIG APFSQGQKRK GVECGPAAIR DAGLVKRLSD 

        70         80         90        100        110        120 
LGCRLKDYGD LSFTPVPKDD LYNNLIVNPR SVGLANQELA EVVNRAVSGG YSCVTVGGDH 

       130        140        150        160        170        180 
SLAIGTISGH ARHCPDLCVV WVDAHADINT PLTTSSGNLH GQPVSFLLRE LQDKVPQLPG 

       190        200        210        220        230        240 
FSWIKPCISS PSIVYIGLRD VDPPEHFILK KYDIQYFSMR DIDRLGIQKV MEQTFDLLIG 

       250        260        270        280        290        300 
KKQRPIHLSF DIDAFDPTLA PATGTPGCGG ADLSRRMYIS EEIHNTGLLS ALDLVEVNPR 

       310        320        330        340        350 
LAASDEEAKA TASLAVDVIA SSFGQTREGG HTVYEQLPPP SSPHESENAE RVRI 

« Hide

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.
RefSeqNP_001075650.1. NM_001082181.1.
UniGeneOcu.3304.

3D structure databases

ProteinModelPortalQ4VK78.
SMRQ4VK78. Positions 24-329.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4VK78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100008967.

Organism-specific databases

CTD384.

Phylogenomic databases

GeneTreeENSGT00530000063082.
HOVERGENHBG003030.
OrthoDBEOG4FR0S2.

Family and domain databases

InterProIPR014033. Arginase_subgr.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
PANTHERPTHR11358:SF2. Arginase_sub. 1 hit.
PTHR11358. Ureohydrolase. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01229. RocF_arginase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGI2_RABIT
AccessionPrimary (citable) accession number: Q4VK78
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2005
Last modified: November 16, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families