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Protein

Arginase-1

Gene

Arg1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-arginine + H2O = L-ornithine + urea.

Cofactori

Mn2+PROSITE-ProRule annotationNote: Binds 2 manganese ions per subunit.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi101 – 1011Manganese 1PROSITE-ProRule annotation
Metal bindingi124 – 1241Manganese 1PROSITE-ProRule annotation
Metal bindingi124 – 1241Manganese 2PROSITE-ProRule annotation
Metal bindingi126 – 1261Manganese 2PROSITE-ProRule annotation
Metal bindingi128 – 1281Manganese 1PROSITE-ProRule annotation
Binding sitei183 – 1831SubstrateBy similarity
Metal bindingi232 – 2321Manganese 1PROSITE-ProRule annotation
Metal bindingi232 – 2321Manganese 2PROSITE-ProRule annotation
Metal bindingi234 – 2341Manganese 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. arginase activity Source: MGI
  2. manganese ion binding Source: Ensembl

GO - Biological processi

  1. arginine metabolic process Source: UniProtKB-KW
  2. cellular response to dexamethasone stimulus Source: Ensembl
  3. cellular response to glucagon stimulus Source: Ensembl
  4. cellular response to hydrogen peroxide Source: Ensembl
  5. cellular response to interleukin-4 Source: Ensembl
  6. cellular response to lipopolysaccharide Source: Ensembl
  7. cellular response to transforming growth factor beta stimulus Source: Ensembl
  8. collagen biosynthetic process Source: Ensembl
  9. liver development Source: Ensembl
  10. lung development Source: Ensembl
  11. mammary gland involution Source: Ensembl
  12. maternal process involved in female pregnancy Source: Ensembl
  13. positive regulation of endothelial cell proliferation Source: Ensembl
  14. protein homotrimerization Source: Ensembl
  15. regulation of L-arginine import Source: Ensembl
  16. response to amine Source: Ensembl
  17. response to amino acid Source: Ensembl
  18. response to axon injury Source: Ensembl
  19. response to cadmium ion Source: Ensembl
  20. response to drug Source: Ensembl
  21. response to herbicide Source: Ensembl
  22. response to manganese ion Source: Ensembl
  23. response to methylmercury Source: Ensembl
  24. response to selenium ion Source: Ensembl
  25. response to vitamin A Source: Ensembl
  26. response to vitamin E Source: Ensembl
  27. response to zinc ion Source: Ensembl
  28. urea cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arginine metabolism, Urea cycle

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi3.5.3.1. 3474.
ReactomeiREACT_315699. Urea cycle.
SABIO-RKQ61176.
UniPathwayiUPA00158; UER00270.

Names & Taxonomyi

Protein namesi
Recommended name:
Arginase-1 (EC:3.5.3.1)
Alternative name(s):
Liver-type arginase
Type I arginase
Gene namesi
Name:Arg1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:88070. Arg1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: MGI
  4. neuronal cell body Source: Ensembl
  5. neuron projection Source: Ensembl
  6. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Arginase-1PRO_0000173694Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphoserine1 Publication
Modified residuei17 – 171N6-succinyllysine1 Publication
Modified residuei62 – 621PhosphoserineBy similarity
Modified residuei72 – 721Phosphoserine1 Publication
Modified residuei75 – 751N6-succinyllysine1 Publication
Modified residuei163 – 1631PhosphoserineBy similarity
Modified residuei217 – 2171PhosphoserineBy similarity
Modified residuei281 – 2811Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ61176.
PaxDbiQ61176.
PRIDEiQ61176.

2D gel databases

SWISS-2DPAGEQ61176.

PTM databases

PhosphoSiteiQ61176.

Expressioni

Gene expression databases

BgeeiQ61176.
CleanExiMM_ARG1.
GenevestigatoriQ61176.

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

BioGridi198190. 1 interaction.
IntActiQ61176. 4 interactions.
MINTiMINT-1854942.

Structurei

3D structure databases

ProteinModelPortaliQ61176.
SMRiQ61176. Positions 6-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni126 – 1305Substrate bindingBy similarity
Regioni137 – 1393Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0010.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
InParanoidiQ61176.
KOiK01476.
OMAiDYGDLPF.
OrthoDBiEOG747PJ5.
PhylomeDBiQ61176.
TreeFamiTF300034.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61176-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKPKSLEI IGAPFSKGQP RGGVEKGPAA LRKAGLLEKL KETEYDVRDH
60 70 80 90 100
GDLAFVDVPN DSSFQIVKNP RSVGKANEEL AGVVAEVQKN GRVSVVLGGD
110 120 130 140 150
HSLAVGSISG HARVHPDLCV IWVDAHTDIN TPLTTSSGNL HGQPVSFLLK
160 170 180 190 200
ELKGKFPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYII KTLGIKYFSM
210 220 230 240 250
TEVDKLGIGK VMEETFSYLL GRKKRPIHLS FDVDGLDPAF TPATGTPVLG
260 270 280 290 300
GLSYREGLYI TEEIYKTGLL SGLDIMEVNP TLGKTAEEVK STVNTAVALT
310 320
LACFGTQREG NHKPGTDYLK PPK
Length:323
Mass (Da):34,808
Last modified:November 1, 1997 - v1
Checksum:i6D0231978AC1B977
GO

Sequence cautioni

The sequence BAE28901.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091S → T in BAE28901 (PubMed:16141072).Curated
Sequence conflicti306 – 3061T → A in CAJ18381 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48523.1.
RefSeqiNP_031508.1. NM_007482.3.
UniGeneiMm.154144.

Genome annotation databases

EnsembliENSMUST00000020161; ENSMUSP00000020161; ENSMUSG00000019987.
GeneIDi11846.
KEGGimmu:11846.
UCSCiuc007erg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48523.1.
RefSeqiNP_031508.1. NM_007482.3.
UniGeneiMm.154144.

3D structure databases

ProteinModelPortaliQ61176.
SMRiQ61176. Positions 6-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198190. 1 interaction.
IntActiQ61176. 4 interactions.
MINTiMINT-1854942.

PTM databases

PhosphoSiteiQ61176.

2D gel databases

SWISS-2DPAGEQ61176.

Proteomic databases

MaxQBiQ61176.
PaxDbiQ61176.
PRIDEiQ61176.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020161; ENSMUSP00000020161; ENSMUSG00000019987.
GeneIDi11846.
KEGGimmu:11846.
UCSCiuc007erg.2. mouse.

Organism-specific databases

CTDi383.
MGIiMGI:88070. Arg1.

Phylogenomic databases

eggNOGiCOG0010.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
InParanoidiQ61176.
KOiK01476.
OMAiDYGDLPF.
OrthoDBiEOG747PJ5.
PhylomeDBiQ61176.
TreeFamiTF300034.

Enzyme and pathway databases

UniPathwayiUPA00158; UER00270.
BRENDAi3.5.3.1. 3474.
ReactomeiREACT_315699. Urea cycle.
SABIO-RKQ61176.

Miscellaneous databases

ChiTaRSiArg1. mouse.
NextBioi279807.
PROiQ61176.
SOURCEiSearch...

Gene expression databases

BgeeiQ61176.
CleanExiMM_ARG1.
GenevestigatoriQ61176.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01229. rocF_arginase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver and Mammary gland.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-72 AND THR-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiARGI1_MOUSE
AccessioniPrimary (citable) accession number: Q61176
Secondary accession number(s): Q3TB74
, Q3UEL0, Q4FK78, Q80VI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 1, 2015
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.