Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q91553 (ARGN1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 71. 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, non-hepatic 1

EC=3.5.3.1
Gene names
Name:arg2-a
Synonyms:arg1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
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. Most abundant 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). Low levels expressed in hindlimb until stage 66 after which, 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

metal 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 1
PRO_0000173699

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
Q91553 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 07B119D8E5F4DA31

FASTA36039,156
        10         20         30         40         50         60 
MSIRSNFVRL LKKQVSIIKL QKKCSHSVAV IGAPFSKGQK RRGVEHGPAA IRSAGLIERL 

        70         80         90        100        110        120 
SNLGCNVCDF GDLHFSQVPN 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 LKNYDISYYS 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

« Hide 'large scale' 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.
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08406 mRNA. Translation: AAA56891.1.
BC043964 mRNA. Translation: AAH43964.1.
PIRI51663.
UniGeneXl.892.

3D structure databases

ProteinModelPortalQ91553.
SMRQ91553. Positions 26-331.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

XenbaseXB-GENE-6251613. arg2.

Phylogenomic databases

HOVERGENHBG003030.

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 nameARGN1_XENLA
AccessionPrimary (citable) accession number: Q91553
Secondary accession number(s): Q5D0B7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 27, 2011
This is version 71 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