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Q61176

- ARGI1_MOUSE

UniProt

Q61176 - ARGI1_MOUSE

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Protein

Arginase-1

Gene

Arg1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

ReactomeiREACT_246679. 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: Chromosome 10

Organism-specific databases

MGIiMGI:88070. Arg1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. neuronal cell body Source: Ensembl
  5. neuron projection Source: Ensembl
  6. nucleus Source: Ensembl
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 residuei72 – 721Phosphoserine1 Publication
Modified residuei75 – 751N6-succinyllysine1 Publication
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.
OMAiKEQECDV.
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. 1 PublicationCurated

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 .
CCDSi CCDS48523.1.
RefSeqi NP_031508.1. NM_007482.3.
UniGenei Mm.154144.

3D structure databases

ProteinModelPortali Q61176.
SMRi Q61176. Positions 6-313.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198190. 1 interaction.
IntActi Q61176. 4 interactions.
MINTi MINT-1854942.

PTM databases

PhosphoSitei Q61176.

2D gel databases

SWISS-2DPAGE Q61176.

Proteomic databases

MaxQBi Q61176.
PaxDbi Q61176.
PRIDEi Q61176.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020161 ; ENSMUSP00000020161 ; ENSMUSG00000019987 .
GeneIDi 11846.
KEGGi mmu:11846.
UCSCi uc007erg.2. mouse.

Organism-specific databases

CTDi 383.
MGIi MGI:88070. Arg1.

Phylogenomic databases

eggNOGi COG0010.
GeneTreei ENSGT00530000063082.
HOGENOMi HOG000204319.
HOVERGENi HBG003030.
InParanoidi Q61176.
KOi K01476.
OMAi KEQECDV.
OrthoDBi EOG747PJ5.
PhylomeDBi Q61176.
TreeFami TF300034.

Enzyme and pathway databases

UniPathwayi UPA00158 ; UER00270 .
Reactomei REACT_246679. Urea cycle.
SABIO-RK Q61176.

Miscellaneous databases

ChiTaRSi Arg1. mouse.
NextBioi 279807.
PROi Q61176.
SOURCEi Search...

Gene expression databases

Bgeei Q61176.
CleanExi MM_ARG1.
Genevestigatori Q61176.

Family and domain databases

Gene3Di 3.40.800.10. 1 hit.
InterProi IPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view ]
PANTHERi PTHR11358. PTHR11358. 1 hit.
Pfami PF00491. Arginase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036979. Arginase. 1 hit.
PRINTSi PR00116. ARGINASE.
TIGRFAMsi TIGR01229. rocF_arginase. 1 hit.
PROSITEi PS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 123 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