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   24-JAN-2024, entry version 184.
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; Evidence={ECO:0000255|PROSITE-
CC         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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   CPTAC; non-CPTAC-3893; -.
DR   jPOST; Q61176; -.
DR   MaxQB; Q61176; -.
DR   PaxDb; 10090-ENSMUSP00000020161; -.
DR   PeptideAtlas; Q61176; -.
DR   ProteomicsDB; 283262; -.
DR   Pumba; Q61176; -.
DR   Antibodypedia; 779; 1479 antibodies from 50 providers.
DR   DNASU; 11846; -.
DR   Ensembl; ENSMUST00000020161.10; ENSMUSP00000020161.9; ENSMUSG00000019987.10.
DR   GeneID; 11846; -.
DR   KEGG; mmu:11846; -.
DR   UCSC; uc007erg.2; mouse.
DR   AGR; MGI:88070; -.
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; YAMDSID; -.
DR   OrthoDB; 161483at2759; -.
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 77 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 157 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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:0019547; P:arginine catabolic process to ornithine; ISO:MGI.
DR   GO; GO:0006525; P:arginine metabolic process; ISO:MGI.
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:0046007; P:negative regulation of activated T cell proliferation; IMP:UniProtKB.
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:0060336; P:negative regulation of type II interferon-mediated signaling pathway; ISO:MGI.
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:0000050; P:urea cycle; ISO:MGI.
DR   CDD; cd11587; Arginase-like; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR014033; Arginase.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   NCBIfam; TIGR01229; rocF_arginase; 1.
DR   PANTHER; PTHR43782; ARGINASE; 1.
DR   PANTHER; PTHR43782:SF2; ARGINASE-1; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
DR   PRINTS; PR00116; ARGINASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   PROSITE; PS01053; ARGINASE_1; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
DR   SWISS-2DPAGE; Q61176; -.
DR   Genevisible; Q61176; MM.
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
//