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Reviewed, UniProtKB/Swiss-Prot Q61176 (ARGI1_MOUSE)

Last modified October 13, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-1
    EC=3.5.3.1
Alternative name(s):
    Type I arginase
    Liver-type arginase
Gene names
Name: Arg1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

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

Cytoplasm.

Sequence similarities

Belongs to the arginase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

urea cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionarginase activity

Inferred from direct assay. Source: MGI

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 – 323323Arginase-1
PRO_0000173694

Regions

Region126 – 1305Substrate binding By similarity
Region137 – 1393Substrate binding By similarity

Sites

Metal binding1011Manganese 1 By similarity
Metal binding1241Manganese 1 By similarity
Metal binding1241Manganese 2 By similarity
Metal binding1261Manganese 2 By similarity
Metal binding1281Manganese 1 By similarity
Metal binding2321Manganese 1 By similarity
Metal binding2321Manganese 2 By similarity
Metal binding2341Manganese 2 By similarity
Binding site1831Substrate By similarity

Amino acid modifications

Modified residue31Phosphoserine Ref.6
Modified residue2301Phosphoserine Ref.5

Experimental info

Sequence conflict1091S → T in BAE28901. Ref.2
Sequence conflict3061T → A in CAJ18381. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q61176-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 6D0231978AC1B977

FASTA32334,808
        10         20         30         40         50         60 
MSSKPKSLEI IGAPFSKGQP RGGVEKGPAA LRKAGLLEKL KETEYDVRDH GDLAFVDVPN 

        70         80         90        100        110        120 
DSSFQIVKNP RSVGKANEEL AGVVAEVQKN GRVSVVLGGD HSLAVGSISG HARVHPDLCV 

       130        140        150        160        170        180 
IWVDAHTDIN TPLTTSSGNL HGQPVSFLLK ELKGKFPDVP GFSWVTPCIS AKDIVYIGLR 

       190        200        210        220        230        240 
DVDPGEHYII KTLGIKYFSM TEVDKLGIGK VMEETFSYLL GRKKRPIHLS FDVDGLDPAF 

       250        260        270        280        290        300 
TPATGTPVLG GLSYREGLYI TEEIYKTGLL SGLDIMEVNP TLGKTAEEVK STVNTAVALT 

       310        320 
LACFGTQREG NHKPGTDYLK PPK 

« Hide

References

« Hide 'large scale' references
[1]Chieko H.
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[3]"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver and Mammary gland.
[5]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, MASS SPECTROMETRY.
Tissue: Liver.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

U51805 mRNA. Translation: AAA98611.1.
AK149471 mRNA. Translation: BAE28901.1. Different initiation.
AK171417 mRNA. Translation: BAE42440.1.
CT010173 mRNA. Translation: CAJ18381.1.
BC013341 mRNA. Translation: AAH13341.1.
BC050005 mRNA. Translation: AAH50005.2.
IPIIPI00117914.
RefSeqNP_031508.1.
UniGeneMm.154144

3D structure databases

HSSPHSSP built from PDB template 1D3V based on UniProtKB P07824.
SMRQ61176. Positions 6-319.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ61176.

PTM databases

PhosphoSiteQ61176.

2-D gel databases

SWISS-2DPAGEQ61176.

Proteomic databases

PRIDEQ61176.

Genome annotation databases

EnsemblENSMUST00000020161; ENSMUSP00000020161; ENSMUSG00000019987; Mus musculus. [Genome view]
GeneID11846.
KEGGmmu:11846.
NMPDRfig|10090.3.peg.13476.
UCSCuc007erg.1. mouse.

Organism-specific databases

CTD11846.
MGIMGI:88070. Arg1.

Phylogenomic databases

HOVERGENQ61176.

Enzyme and pathway databases

BRENDA3.5.3.1. 244.

Gene expression databases

ArrayExpressQ61176.
BgeeQ61176.
CleanExMM_ARG1.
GenevestigatorQ61176.
GermOnlineENSMUSG00000019987. Mus musculus.

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...

Other Resources

NextBio279807.
SOURCESearch...

Entry information

Entry nameARGI1_MOUSE
AccessionPrimary (citable) accession number: Q61176
Secondary accession number(s): Q3TB74 expand/collapse secondary AC list , Q3UEL0, Q4FK78, Q80VI4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 13, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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