ARGI1_MOUSE
ID ARGI1_MOUSE Reviewed; 323 AA.
AC Q61176; Q3TB74; Q3UEL0; Q4FK78; Q80VI4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Arginase-1;
DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
DE AltName: Full=Liver-type arginase;
DE AltName: Full=Type I arginase;
GN Name=Arg1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RA Chieko H.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION IN ALTERNATIVELY ACTIVATED MACROPHAGES, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=7537672; DOI=10.1002/eji.1830250436;
RA Modolell M., Corraliza I.M., Link F., Soler G., Eichmann K.;
RT "Reciprocal regulation of the nitric oxide synthase/arginase balance in
RT mouse bone marrow-derived macrophages by TH1 and TH2 cytokines.";
RL Eur. J. Immunol. 25:1101-1104(1995).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12193690; DOI=10.4049/jimmunol.169.5.2253;
RA Lang R., Patel D., Morris J.J., Rutschman R.L., Murray P.J.;
RT "Shaping gene expression in activated and resting primary macrophages by
RT IL-10.";
RL J. Immunol. 169:2253-2263(2002).
RN [7]
RP FUNCTION IN MYELOID-DERIVED SUPPRESSOR CELLS, AND TISSUE SPECIFICITY.
RX PubMed=15313928; DOI=10.1158/0008-5472.can-04-0465;
RA Rodriguez P.C., Quiceno D.G., Zabaleta J., Ortiz B., Zea A.H.,
RA Piazuelo M.B., Delgado A., Correa P., Brayer J., Sotomayor E.M.,
RA Antonia S., Ochoa J.B., Ochoa A.C.;
RT "Arginase I production in the tumor microenvironment by mature myeloid
RT cells inhibits T-cell receptor expression and antigen-specific T-cell
RT responses.";
RL Cancer Res. 64:5839-5849(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-72 AND THR-281, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP FUNCTION IN TUMOR-INFILTRATING DENDRITIC CELLS, INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19414774; DOI=10.4049/jimmunol.0803926;
RA Liu Q., Zhang C., Sun A., Zheng Y., Wang L., Cao X.;
RT "Tumor-educated CD11bhighIalow regulatory dendritic cells suppress T cell
RT response through arginase I.";
RL J. Immunol. 182:6207-6216(2009).
RN [10]
RP FUNCTION IN ALTERNATIVELY ACTIVATED MACROPHAGES, AND TISSUE SPECIFICITY.
RX PubMed=19360123; DOI=10.1371/journal.ppat.1000371;
RA Pesce J.T., Ramalingam T.R., Mentink-Kane M.M., Wilson M.S., El Kasmi K.C.,
RA Smith A.M., Thompson R.W., Cheever A.W., Murray P.J., Wynn T.A.;
RT "Arginase-1-expressing macrophages suppress Th2 cytokine-driven
RT inflammation and fibrosis.";
RL PLoS Pathog. 5:E1000371-E1000371(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-163 AND THR-281, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP FUNCTION IN ALTERNATIVELY ACTIVATED MACROPHAGES.
RX PubMed=20483789; DOI=10.4049/jimmunol.0902009;
RA Herbert D.R., Orekov T., Roloson A., Ilies M., Perkins C., O'Brien W.,
RA Cederbaum S., Christianson D.W., Zimmermann N., Rothenberg M.E.,
RA Finkelman F.D.;
RT "Arginase I suppresses IL-12/IL-23p40-driven intestinal inflammation during
RT acute schistosomiasis.";
RL J. Immunol. 184:6438-6446(2010).
RN [13]
RP FUNCTION IN TUMOR-INFILTRATING DENDRITIC CELLS.
RX PubMed=23248265; DOI=10.4049/jimmunol.1103797;
RA Narita Y., Kitamura H., Wakita D., Sumida K., Masuko K., Terada S.,
RA Nakano K., Nishimura T.;
RT "The key role of IL-6-arginase cascade for inducing dendritic cell-
RT dependent CD4(+) T cell dysfunction in tumor-bearing mice.";
RL J. Immunol. 190:812-820(2013).
RN [14]
RP FUNCTION IN WOUND HEALING.
RX PubMed=23552798; DOI=10.1038/jid.2013.164;
RA Campbell L., Saville C.R., Murray P.J., Cruickshank S.M., Hardman M.J.;
RT "Local arginase 1 activity is required for cutaneous wound healing.";
RL J. Invest. Dermatol. 133:2461-2470(2013).
RN [15]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-75, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [16]
RP FUNCTION IN ALTERNATIVELY ACTIVATED MACROPHAGES.
RX PubMed=23637937; DOI=10.1371/journal.pone.0061961;
RA Barron L., Smith A.M., El Kasmi K.C., Qualls J.E., Huang X., Cheever A.,
RA Borthwick L.A., Wilson M.S., Murray P.J., Wynn T.A.;
RT "Role of arginase 1 from myeloid cells in th2-dominated lung
RT inflammation.";
RL PLoS ONE 8:E61961-E61961(2013).
RN [17]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=27043409; DOI=10.1038/ni.3421;
RA Monticelli L.A., Buck M.D., Flamar A.L., Saenz S.A., Tait Wojno E.D.,
RA Yudanin N.A., Osborne L.C., Hepworth M.R., Tran S.V., Rodewald H.R.,
RA Shah H., Cross J.R., Diamond J.M., Cantu E., Christie J.D., Pearce E.L.,
RA Artis D.;
RT "Arginase 1 is an innate lymphoid-cell-intrinsic metabolic checkpoint
RT controlling type 2 inflammation.";
RL Nat. Immunol. 17:656-665(2016).
CC -!- FUNCTION: Key element of the urea cycle converting L-arginine to urea
CC and L-ornithine, which is further metabolized into metabolites proline
CC and polyamides that drive collagen synthesis and bioenergetic pathways
CC critical for cell proliferation, respectively; the urea cycle takes
CC place primarily in the liver and, to a lesser extent, in the kidneys.
CC {ECO:0000305}.
CC -!- FUNCTION: Functions in L-arginine homeostasis in nonhepatic tissues
CC characterized by the competition between nitric oxide synthase (NOS)
CC and arginase for the available intracellular substrate arginine.
CC Arginine metabolism is a critical regulator of innate and adaptive
CC immune responses. Involved in an antimicrobial effector pathway in
CC polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated
CC from the phagolysosome and depletes arginine in the microenvironment
CC leading to suppressed T cell and natural killer (NK) cell proliferation
CC and cytokine secretion (By similarity). In group 2 innate lymphoid
CC cells (ILC2s) promotes acute type 2 inflammation in the lung and is
CC involved in optimal ILC2 proliferation but not survival
CC (PubMed:27043409). Plays a role in the immune response of alternatively
CC activated or M2 macrophages in processes such as wound healing and
CC tissue regeneration, immune defense against multicellular pathogens and
CC parasites, and immune suppression and allergic inflammation; the
CC regulatory outcome seems to be organ specific (PubMed:7537672,
CC PubMed:19360123, PubMed:20483789, PubMed:23552798, PubMed:23637937). In
CC tumor-infiltrating dendritic cells (DCs) and myeloid-derived suppressor
CC cells (MDSCs) plays a role in suppression of T cell-mediated antitumor
CC immunity (PubMed:19414774, PubMed:23248265).
CC {ECO:0000250|UniProtKB:P05089, ECO:0000269|PubMed:15313928,
CC ECO:0000269|PubMed:19360123, ECO:0000269|PubMed:19414774,
CC ECO:0000269|PubMed:20483789, ECO:0000269|PubMed:23248265,
CC ECO:0000269|PubMed:23552798, ECO:0000269|PubMed:23637937,
CC ECO:0000269|PubMed:27043409, ECO:0000269|PubMed:7537672}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:46911; EC=3.5.3.1;
CC Evidence={ECO:0000250|UniProtKB:P05089};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00742};
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}.
CC -!- SUBUNIT: Homotrimer (By similarity). Interacts with CMTM6 (By
CC similarity). {ECO:0000250|UniProtKB:P05089}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05089}.
CC Cytoplasmic granule {ECO:0000250|UniProtKB:P05089}.
CC -!- TISSUE SPECIFICITY: Expressed in macrophages (PubMed:7537672,
CC PubMed:12193690, PubMed:19360123). Expressed in precursor and mature
CC group 2 innate lymphoid cells (ILC2s) (PubMed:27043409). Expressed in
CC lung tumor-associated myeloid cells (PubMed:15313928). Expressed in
CC lung tumor-infiltrating dendritic cells (PubMed:19414774).
CC {ECO:0000269|PubMed:12193690, ECO:0000269|PubMed:19360123,
CC ECO:0000269|PubMed:19414774, ECO:0000269|PubMed:27043409,
CC ECO:0000269|PubMed:7537672}.
CC -!- INDUCTION: By T helper 2 (Th2) cytokines such as IL-4, IL-13 and IL-10.
CC In tumor-infiltrating dendritic cells by prostaglandin E2.
CC {ECO:0000269|PubMed:12193690, ECO:0000269|PubMed:19414774,
CC ECO:0000269|PubMed:7537672}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE28901.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U51805; AAA98611.1; -; mRNA.
DR EMBL; AK149471; BAE28901.1; ALT_INIT; mRNA.
DR EMBL; AK171417; BAE42440.1; -; mRNA.
DR EMBL; CT010173; CAJ18381.1; -; mRNA.
DR EMBL; BC013341; AAH13341.1; -; mRNA.
DR EMBL; BC050005; AAH50005.2; -; mRNA.
DR CCDS; CCDS48523.1; -.
DR RefSeq; NP_031508.1; NM_007482.3.
DR AlphaFoldDB; Q61176; -.
DR SMR; Q61176; -.
DR BioGRID; 198190; 12.
DR IntAct; Q61176; 2.
DR MINT; Q61176; -.
DR STRING; 10090.ENSMUSP00000020161; -.
DR BindingDB; Q61176; -.
DR ChEMBL; CHEMBL4630836; -.
DR CarbonylDB; Q61176; -.
DR iPTMnet; Q61176; -.
DR PhosphoSitePlus; Q61176; -.
DR SwissPalm; Q61176; -.
DR SWISS-2DPAGE; Q61176; -.
DR CPTAC; non-CPTAC-3893; -.
DR jPOST; Q61176; -.
DR MaxQB; Q61176; -.
DR PaxDb; Q61176; -.
DR PeptideAtlas; Q61176; -.
DR PRIDE; Q61176; -.
DR ProteomicsDB; 283262; -.
DR Antibodypedia; 779; 1296 antibodies from 50 providers.
DR DNASU; 11846; -.
DR Ensembl; ENSMUST00000020161; ENSMUSP00000020161; ENSMUSG00000019987.
DR GeneID; 11846; -.
DR KEGG; mmu:11846; -.
DR UCSC; uc007erg.2; mouse.
DR CTD; 383; -.
DR MGI; MGI:88070; Arg1.
DR VEuPathDB; HostDB:ENSMUSG00000019987; -.
DR eggNOG; KOG2965; Eukaryota.
DR GeneTree; ENSGT00950000183195; -.
DR HOGENOM; CLU_039478_6_1_1; -.
DR InParanoid; Q61176; -.
DR OMA; DTPFQIV; -.
DR OrthoDB; 1179130at2759; -.
DR PhylomeDB; Q61176; -.
DR TreeFam; TF300034; -.
DR BRENDA; 3.5.3.1; 3474.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-70635; Urea cycle.
DR SABIO-RK; Q61176; -.
DR UniPathway; UPA00158; UER00270.
DR BioGRID-ORCS; 11846; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Arg1; mouse.
DR PRO; PR:Q61176; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q61176; protein.
DR Bgee; ENSMUSG00000019987; Expressed in left lobe of liver and 153 other tissues.
DR Genevisible; Q61176; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0004053; F:arginase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030145; F:manganese ion binding; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; ISO:MGI.
DR GO; GO:0006525; P:arginine metabolic process; ISO:MGI.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; IEA:Ensembl.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0032964; P:collagen biosynthetic process; ISO:MGI.
DR GO; GO:0042832; P:defense response to protozoan; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0060056; P:mammary gland involution; IEA:Ensembl.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IMP:UniProtKB.
DR GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; ISO:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI.
DR GO; GO:2000552; P:negative regulation of T-helper 2 cell cytokine production; IMP:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0070965; P:positive regulation of neutrophil mediated killing of fungus; ISO:MGI.
DR GO; GO:1905541; P:regulation of L-arginine import across plasma membrane; ISO:MGI.
DR GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR GO; GO:0009635; P:response to herbicide; IEA:Ensembl.
DR GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
DR GO; GO:0051597; P:response to methylmercury; IEA:Ensembl.
DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
DR GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
DR GO; GO:0000050; P:urea cycle; ISO:MGI.
DR InterPro; IPR014033; Arginase.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR43782; PTHR43782; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01229; rocF_arginase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Arginine metabolism; Cytoplasm; Hydrolase; Immunity;
KW Innate immunity; Manganese; Metal-binding; Phosphoprotein;
KW Reference proteome; Urea cycle.
FT CHAIN 1..323
FT /note="Arginase-1"
FT /id="PRO_0000173694"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 126..130
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 137..139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 232
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 232
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P78540"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 17
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 75
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT MOD_RES 281
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 109
FT /note="S -> T (in Ref. 2; BAE28901)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="T -> A (in Ref. 3; CAJ18381)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 34808 MW; 6D0231978AC1B977 CRC64;
MSSKPKSLEI IGAPFSKGQP RGGVEKGPAA LRKAGLLEKL KETEYDVRDH GDLAFVDVPN
DSSFQIVKNP RSVGKANEEL AGVVAEVQKN GRVSVVLGGD HSLAVGSISG HARVHPDLCV
IWVDAHTDIN TPLTTSSGNL HGQPVSFLLK ELKGKFPDVP GFSWVTPCIS AKDIVYIGLR
DVDPGEHYII KTLGIKYFSM TEVDKLGIGK VMEETFSYLL GRKKRPIHLS FDVDGLDPAF
TPATGTPVLG GLSYREGLYI TEEIYKTGLL SGLDIMEVNP TLGKTAEEVK STVNTAVALT
LACFGTQREG NHKPGTDYLK PPK
