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P07824

- ARGI1_RAT

UniProt

P07824 - ARGI1_RAT

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Protein

Arginase-1

Gene

Arg1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 2 manganese ions per subunit.2 PublicationsPROSITE-ProRule annotation

Enzyme regulationi

Inactivated by diethyl pyrocarbonate (DEPC).

Kineticsi

  1. KM=1.4 mM for arginine2 Publications

Pathwayi

Sites

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

GO - Molecular functioni

  1. arginase activity Source: RGD
  2. manganese ion binding Source: RGD

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arginine metabolism, Urea cycle

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_216480. Urea cycle.
SABIO-RKP07824.
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi2150. Arg1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. extracellular space Source: RGD
  3. extracellular vesicular exosome Source: Ensembl
  4. mitochondrial outer membrane Source: RGD
  5. neuronal cell body Source: RGD
  6. neuron projection Source: RGD
  7. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011H → E: Reduced catalytic activity. No effect on manganese binding. 1 Publication
Mutagenesisi128 – 1281D → E or N: Reduced manganese binding and strongly reduced catalytic activity. 1 Publication
Mutagenesisi141 – 1411H → A, C or D: Strongly reduced catalytic activity. Minor effect on affinity for arginine. 1 Publication
Mutagenesisi141 – 1411H → N: Reduced affinity for arginine and reduced catalytic activity. 1 Publication
Mutagenesisi232 – 2321D → A: Loss of one manganese ion and strongly reduced catalytic activity. 1 Publication
Mutagenesisi232 – 2321D → C: Reduced manganese binding and strongly reduced catalytic activity. 1 Publication
Mutagenesisi234 – 2341D → A, E or H: Reduced manganese binding and strongly reduced catalytic activity. 1 Publication
Mutagenesisi235 – 2351G → A: 56% of wild-type activity. 1 Publication
Mutagenesisi235 – 2351G → R: Loss of manganese-binding and activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Arginase-1PRO_0000173697Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171N6-succinyllysineBy similarity
Modified residuei72 – 721PhosphoserineBy similarity
Modified residuei75 – 751N6-succinyllysineBy similarity
Modified residuei281 – 2811PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP07824.
PRIDEiP07824.

PTM databases

PhosphoSiteiP07824.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Inductioni

By arginine or homoarginine.

Gene expression databases

GenevestigatoriP07824.

Interactioni

Subunit structurei

Homotrimer.2 Publications

Protein-protein interaction databases

BioGridi247899. 1 interaction.
IntActiP07824. 1 interaction.
MINTiMINT-4567374.
STRINGi10116.ENSRNOP00000017911.

Structurei

Secondary structure

1
323
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125
Beta strandi19 – 213
Helixi22 – 265
Helixi27 – 337
Helixi36 – 405
Beta strandi43 – 453
Beta strandi47 – 526
Beta strandi64 – 663
Beta strandi67 – 693
Helixi70 – 8920
Beta strandi93 – 975
Helixi101 – 1033
Helixi104 – 11411
Beta strandi119 – 1268
Turni132 – 1343
Beta strandi136 – 1383
Helixi140 – 1423
Helixi144 – 1485
Helixi150 – 1523
Beta strandi153 – 1564
Turni160 – 1645
Helixi171 – 1733
Beta strandi174 – 1796
Helixi184 – 19310
Beta strandi196 – 1994
Helixi200 – 2067
Helixi208 – 22013
Beta strandi221 – 2233
Beta strandi227 – 2326
Helixi233 – 2353
Turni238 – 2403
Beta strandi244 – 2463
Helixi254 – 26714
Beta strandi270 – 2767
Helixi280 – 2823
Beta strandi283 – 2853
Helixi286 – 30318

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D3VX-ray1.70A/B1-323[»]
1HQ5X-ray2.30A/B1-323[»]
1HQFX-ray2.90A/B/C1-323[»]
1HQGX-ray2.00A/B/C1-323[»]
1HQHX-ray2.80A/B/C1-323[»]
1HQXX-ray3.00A/B/C1-323[»]
1P8MX-ray2.84A/B/C6-319[»]
1P8NX-ray2.90A/B/C6-319[»]
1P8OX-ray2.96A/B/C6-319[»]
1P8PX-ray2.50A/B/C6-319[»]
1P8QX-ray2.95A/B/C6-319[»]
1P8RX-ray2.50A/B6-313[»]
1P8SX-ray3.20A/B/C6-319[»]
1R1OX-ray2.80A/B/C1-323[»]
1RLAX-ray2.10A/B/C1-323[»]
1T4PX-ray2.60A/B/C6-319[»]
1T4RX-ray2.60A/B/C6-319[»]
1T4SX-ray2.80A/B/C6-319[»]
1T4TX-ray2.20A/B/C6-319[»]
1T5FX-ray2.20A/B/C6-319[»]
1T5GX-ray2.40A/B/C6-319[»]
1TA1X-ray2.50A/B/C6-319[»]
1TBHX-ray2.70A/B/C6-319[»]
1TBJX-ray2.80A/B/C6-319[»]
1TBLX-ray3.10A/B/C6-319[»]
1ZPEX-ray1.70A/B/C6-319[»]
1ZPGX-ray1.90A/B/C6-319[»]
2RLAX-ray3.00A/B/C1-323[»]
3E8QX-ray2.90A/B/C1-323[»]
3E8ZX-ray2.00A/B/C1-323[»]
3E9BX-ray2.15A/B/C1-323[»]
3RLAX-ray2.54A/B/C1-323[»]
4RLAX-ray2.94A/B/C1-323[»]
5RLAX-ray2.74A/B/C1-323[»]
ProteinModelPortaliP07824.
SMRiP07824. Positions 6-319.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07824.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the arginase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0010.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204319.
HOVERGENiHBG003030.
InParanoidiP07824.
KOiK01476.
OMAiFLIRIEV.
OrthoDBiEOG747PJ5.
PhylomeDBiP07824.
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.

P07824-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSKPKPIEI IGAPFSKGQP RGGVEKGPAA LRKAGLVEKL KETEYNVRDH
60 70 80 90 100
GDLAFVDVPN DSPFQIVKNP RSVGKANEQL AAVVAETQKN GTISVVLGGD
110 120 130 140 150
HSMAIGSISG HARVHPDLCV IWVDAHTDIN TPLTTSSGNL HGQPVAFLLK
160 170 180 190 200
ELKGKFPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYII KTLGIKYFSM
210 220 230 240 250
TEVDKLGIGK VMEETFSYLL GRKKRPIHLS FDVDGLDPVF TPATGTPVVG
260 270 280 290 300
GLSYREGLYI TEEIYKTGLL SGLDIMEVNP TLGKTPEEVT RTVNTAVALT
310 320
LSCFGTKREG NHKPETDYLK PPK
Length:323
Mass (Da):34,973
Last modified:April 1, 1990 - v2
Checksum:i5A92CB0931F9A053
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti298 – 2981A → P in AAA40761. (PubMed:3571256)Curated
Sequence conflicti298 – 2981A → P in AAA40760. (PubMed:3571256)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02720 mRNA. Translation: AAA40761.1.
M17931
, M17924, M17925, M17926, M17927, M17928, M17929, M17930 Genomic DNA. Translation: AAA40760.1.
BC091158 mRNA. Translation: AAH91158.1.
PIRiA26702.
RefSeqiNP_058830.2. NM_017134.3.
UniGeneiRn.9857.

Genome annotation databases

EnsembliENSRNOT00000017911; ENSRNOP00000017911; ENSRNOG00000013304.
GeneIDi29221.
KEGGirno:29221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02720 mRNA. Translation: AAA40761.1 .
M17931
, M17924 , M17925 , M17926 , M17927 , M17928 , M17929 , M17930 Genomic DNA. Translation: AAA40760.1 .
BC091158 mRNA. Translation: AAH91158.1 .
PIRi A26702.
RefSeqi NP_058830.2. NM_017134.3.
UniGenei Rn.9857.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D3V X-ray 1.70 A/B 1-323 [» ]
1HQ5 X-ray 2.30 A/B 1-323 [» ]
1HQF X-ray 2.90 A/B/C 1-323 [» ]
1HQG X-ray 2.00 A/B/C 1-323 [» ]
1HQH X-ray 2.80 A/B/C 1-323 [» ]
1HQX X-ray 3.00 A/B/C 1-323 [» ]
1P8M X-ray 2.84 A/B/C 6-319 [» ]
1P8N X-ray 2.90 A/B/C 6-319 [» ]
1P8O X-ray 2.96 A/B/C 6-319 [» ]
1P8P X-ray 2.50 A/B/C 6-319 [» ]
1P8Q X-ray 2.95 A/B/C 6-319 [» ]
1P8R X-ray 2.50 A/B 6-313 [» ]
1P8S X-ray 3.20 A/B/C 6-319 [» ]
1R1O X-ray 2.80 A/B/C 1-323 [» ]
1RLA X-ray 2.10 A/B/C 1-323 [» ]
1T4P X-ray 2.60 A/B/C 6-319 [» ]
1T4R X-ray 2.60 A/B/C 6-319 [» ]
1T4S X-ray 2.80 A/B/C 6-319 [» ]
1T4T X-ray 2.20 A/B/C 6-319 [» ]
1T5F X-ray 2.20 A/B/C 6-319 [» ]
1T5G X-ray 2.40 A/B/C 6-319 [» ]
1TA1 X-ray 2.50 A/B/C 6-319 [» ]
1TBH X-ray 2.70 A/B/C 6-319 [» ]
1TBJ X-ray 2.80 A/B/C 6-319 [» ]
1TBL X-ray 3.10 A/B/C 6-319 [» ]
1ZPE X-ray 1.70 A/B/C 6-319 [» ]
1ZPG X-ray 1.90 A/B/C 6-319 [» ]
2RLA X-ray 3.00 A/B/C 1-323 [» ]
3E8Q X-ray 2.90 A/B/C 1-323 [» ]
3E8Z X-ray 2.00 A/B/C 1-323 [» ]
3E9B X-ray 2.15 A/B/C 1-323 [» ]
3RLA X-ray 2.54 A/B/C 1-323 [» ]
4RLA X-ray 2.94 A/B/C 1-323 [» ]
5RLA X-ray 2.74 A/B/C 1-323 [» ]
ProteinModelPortali P07824.
SMRi P07824. Positions 6-319.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247899. 1 interaction.
IntActi P07824. 1 interaction.
MINTi MINT-4567374.
STRINGi 10116.ENSRNOP00000017911.

PTM databases

PhosphoSitei P07824.

Proteomic databases

PaxDbi P07824.
PRIDEi P07824.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000017911 ; ENSRNOP00000017911 ; ENSRNOG00000013304 .
GeneIDi 29221.
KEGGi rno:29221.

Organism-specific databases

CTDi 383.
RGDi 2150. Arg1.

Phylogenomic databases

eggNOGi COG0010.
GeneTreei ENSGT00530000063082.
HOGENOMi HOG000204319.
HOVERGENi HBG003030.
InParanoidi P07824.
KOi K01476.
OMAi FLIRIEV.
OrthoDBi EOG747PJ5.
PhylomeDBi P07824.
TreeFami TF300034.

Enzyme and pathway databases

UniPathwayi UPA00158 ; UER00270 .
Reactomei REACT_216480. Urea cycle.
SABIO-RK P07824.

Miscellaneous databases

EvolutionaryTracei P07824.
NextBioi 608419.
PROi P07824.

Gene expression databases

Genevestigatori P07824.

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. "Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver arginase."
    Kawamoto S., Amaya Y., Murakami K., Tokunaga F., Iwanaga S., Kobayashi K., Saheki T., Kimura S., Mori M.
    J. Biol. Chem. 262:6280-6283(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Structural organization of the gene for rat liver-type arginase."
    Ohtake A., Takiguchi M., Shigeto Y., Amaya Y., Kawamoto S., Mori M.
    J. Biol. Chem. 263:2245-2249(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  3. "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].
    Tissue: Liver.
  4. "Functional consequences of the G235R mutation in liver arginase leading to hyperargininemia."
    Lavulo L.T., Emig F.A., Ash D.E.
    Arch. Biochem. Biophys. 399:49-55(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-235.
  5. "Structure of a unique binuclear manganese cluster in arginase."
    Kanyo Z.F., Scolnick L.R., Ash D.E., Christianson D.W.
    Nature 383:554-557(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  6. "Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function."
    Scolnick L.R., Kanyo Z.F., Cavalli R.C., Ash D.E., Christianson D.W.
    Biochemistry 36:10558-10565(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  7. "Arginase-boronic acid complex highlights a physiological role in erectile function."
    Cox J.D., Kim N.N., Traish A.M., Christianson D.W.
    Nat. Struct. Biol. 6:1043-1047(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
  8. "Structural and functional importance of first-shell metal ligands in the binuclear manganese cluster of arginase I."
    Cama E., Emig F.A., Ash D.E., Christianson D.W.
    Biochemistry 42:7748-7758(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 6-319 OF MUTANTS ASN-101; GLU-101; ASN-128; GLU-128; ALA-232; CYS-232 AND GLU-234 IN COMPLEXES WITH MANGANESE IONS, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-101; ASP-128; ASP-232 AND ASP-234.
  9. "Design of amino acid aldehydes as transition-state analogue inhibitors of arginase."
    Shin H., Cama E., Christianson D.W.
    J. Am. Chem. Soc. 126:10278-10284(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 6-319 IN COMPLEX WITH MANGANESE IONS AND THE SYNTHETIC INHIBITOR (S)-2-AMINO-7-OXOHEPTANOIC ACID.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 6-319 OF MUTANTS ALA-141; ASN-141; ASP-141 AND CYS-141 IN COMPLEX WITH MANGANESE IONS, COFACTOR, MUTAGENESIS OF HIS-141, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.

Entry informationi

Entry nameiARGI1_RAT
AccessioniPrimary (citable) accession number: P07824
Secondary accession number(s): Q5BK93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3