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Reviewed, UniProtKB/Swiss-Prot Q91554 (ARGN2_XENLA)

Last modified September 1, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
    Arginase, non-hepatic 2
    EC=3.5.3.1
Gene names
Name: arg2-B
Synonyms: arg2
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

As well as its role in the urea cycle, may be involved in tissue remodeling.

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.

Tissue specificity

Expressed at differing tadpole stages in tail, intestine, hindlimb and trunk region. Strongest in tadpole tail.

Developmental stage

First detected in neurula (stage 16/17). Highest levels in whole tadpole found around stage 47/48. In the intestine, increased levels are found during metamorphosis (stages 58-64) and in the hindlimb, expressed at low levels during metamorphosis until stage 66 when levels dramatically increase. In the tail, a constant high level of expression is found throughout metamorphosis.

Induction

By thyroid hormone (T3).

Sequence similarities

Belongs to the arginase family.

Ontologies

Keywords
   Biological processArginine metabolism
Urea cycle
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processarginine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

urea cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionarginase activity

Inferred from electronic annotation. Source: EC

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360Arginase, non-hepatic 2
PRO_0000173700

Regions

Region147 – 1515Substrate binding By similarity
Region158 – 1603Substrate binding By similarity

Sites

Metal binding1221Manganese 1 By similarity
Metal binding1451Manganese 1 By similarity
Metal binding1451Manganese 2 By similarity
Metal binding1471Manganese 2 By similarity
Metal binding1491Manganese 1 By similarity
Metal binding2531Manganese 1 By similarity
Metal binding2531Manganese 2 By similarity
Metal binding2551Manganese 2 By similarity
Binding site2041Substrate By similarity
Binding site2981Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91554-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 44A4E61915DD0833

FASTA36039,155
        10         20         30         40         50         60 
MSIRSNFVRL LKKQVSIIKL QKKCSHSVAV IGAPFSKGQK RRGVEHGPAA IRSAGLIERL 

        70         80         90        100        110        120 
SNLGCNVCDF GDLHFSKVPN DELYNSIVKH PRTVGLACKV LAEEVSKAVG AGHTCVTLGG 

       130        140        150        160        170        180 
DHSLAFGSIT GHAQQCPDLC VIWVDAHADI NTPLTTPSGN LHGQPVSFLL RELQDKVPPI 

       190        200        210        220        230        240 
PGFSWAKPCL SKSDIVYIGL RDLDPAEQFI LKNYNISYYS MRHIDCMGIK KVMEKTFDQL 

       250        260        270        280        290        300 
LGRRDRPIHL SFDIDAFDPA LAPATGTPVI GGLTYREGVY ITEEIHNTGM LSAVDLVEVN 

       310        320        330        340        350        360 
PVLAATSEEV KATANLAVDV IASCFGQTRE GAHTRADTII DVLPTPSTSY ESDNEEQVRI 

« Hide

References

[1]"Thyroid hormone-dependent differential regulation of multiple arginase genes during amphibian metamorphosis."
Patterton D., Shi Y.-B.
J. Biol. Chem. 269:25328-25334(1994) [PubMed: 7929226] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Intestine.

Cross-references

Sequence databases

U08407 mRNA. Translation: AAA56892.1.
PIRI51664.
RefSeqNP_001079511.1.
UniGeneXl.892

3D structure databases

HSSPHSSP built from PDB template 1PQ3 based on UniProtKB P78540.
SMRQ91554. Positions 26-331.
ModBaseSearch...

Genome annotation databases

GeneID379198.
KEGGxla:379198.

Organism-specific databases

CTD379198.

Phylogenomic databases

HOVERGENQ91554.

Enzyme and pathway databases

BRENDA3.5.3.1. 648.

Family and domain databases

InterProIPR005924. Arginase.
IPR014033. Arginase_sub.
IPR006035. Ureohydrolase.
[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]
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01229. rocF_arginase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGN2_XENLA
AccessionPrimary (citable) accession number: Q91554
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 1, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectXenopus annotation project

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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