ARGI1_HUMAN
ID ARGI1_HUMAN Reviewed; 322 AA.
AC P05089; A6NEA0; Q5JWT5; Q5JWT6; Q8TE72; Q9BS50;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 238.
DE RecName: Full=Arginase-1;
DE EC=3.5.3.1 {ECO:0000269|PubMed:16141327, ECO:0000269|PubMed:17562323};
DE AltName: Full=Liver-type arginase;
DE AltName: Full=Type I arginase;
GN Name=ARG1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=3540966; DOI=10.1073/pnas.84.2.412;
RA Haraguchi Y., Takiguchi M., Amaya Y., Kawamoto S., Matsuda I., Mori M.;
RT "Molecular cloning and nucleotide sequence of cDNA for human liver
RT arginase.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:412-415(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=3174433; DOI=10.1093/nar/16.18.8789;
RA Takiguchi M., Haraguchi Y., Mori M.;
RT "Human liver-type arginase gene: structure of the gene and analysis of the
RT promoter region.";
RL Nucleic Acids Res. 16:8789-8802(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Erythroblast;
RA Lee Y.T., Miller J.L.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Liver, and Skeletal muscle;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-13, AND SUBUNIT.
RC TISSUE=Liver;
RX PubMed=2241902; DOI=10.1042/bj2700697;
RA Ikemoto M., Tabata M., Miyake T., Kono T., Mori M., Totani M., Murachi T.;
RT "Expression of human liver arginase in Escherichia coli. Purification and
RT properties of the product.";
RL Biochem. J. 270:697-703(1990).
RN [8]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION IN ANTIMICROBIAL
RP RESPONSE.
RX PubMed=15546957; DOI=10.1182/blood-2004-07-2521;
RA Munder M., Mollinedo F., Calafat J., Canchado J., Gil-Lamaignere C.,
RA Fuentes J.M., Luckner C., Doschko G., Soler G., Eichmann K., Mueller F.M.,
RA Ho A.D., Goerner M., Modolell M.;
RT "Arginase I is constitutively expressed in human granulocytes and
RT participates in fungicidal activity.";
RL Blood 105:2549-2556(2005).
RN [9]
RP FUNCTION IN ANTIMICROBIAL RESPONSE.
RX PubMed=16709924; DOI=10.1182/blood-2006-11-010389;
RA Munder M., Schneider H., Luckner C., Giese T., Langhans C.D., Fuentes J.M.,
RA Kropf P., Mueller I., Kolb A., Modolell M., Ho A.D.;
RT "Suppression of T-cell functions by human granulocyte arginase.";
RL Blood 108:1627-1634(2006).
RN [10]
RP FUNCTION.
RX PubMed=19380772; DOI=10.4049/jimmunol.0803523;
RA Oberlies J., Watzl C., Giese T., Luckner C., Kropf P., Mueller I., Ho A.D.,
RA Munder M.;
RT "Regulation of NK cell function by human granulocyte arginase.";
RL J. Immunol. 182:5259-5267(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=23749634; DOI=10.4049/jimmunol.1300113;
RA Mattila J.T., Ojo O.O., Kepka-Lenhart D., Marino S., Kim J.H., Eum S.Y.,
RA Via L.E., Barry C.E. III, Klein E., Kirschner D.E., Morris S.M. Jr.,
RA Lin P.L., Flynn J.L.;
RT "Microenvironments in tuberculous granulomas are delineated by distinct
RT populations of macrophage subsets and expression of nitric oxide synthase
RT and arginase isoforms.";
RL J. Immunol. 191:773-784(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-163 AND SER-217, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP 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).
RN [15]
RP INTERACTION WITH CMTM6, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28813417; DOI=10.1038/nature23643;
RA Burr M.L., Sparbier C.E., Chan Y.C., Williamson J.C., Woods K.,
RA Beavis P.A., Lam E.Y.N., Henderson M.A., Bell C.C., Stolzenburg S.,
RA Gilan O., Bloor S., Noori T., Morgens D.W., Bassik M.C., Neeson P.J.,
RA Behren A., Darcy P.K., Dawson S.J., Voskoboinik I., Trapani J.A., Cebon J.,
RA Lehner P.J., Dawson M.A.;
RT "CMTM6 maintains the expression of PD-L1 and regulates anti-tumour
RT immunity.";
RL Nature 549:101-105(2017).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.29 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND
RP THE SYNTHETIC INHIBITOR 2(S)-AMINO-6-BORONOHEXANOIC ACID, SUBCELLULAR
RP LOCATION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=16141327; DOI=10.1073/pnas.0504027102;
RA Di Costanzo L., Sabio G., Mora A., Rodriguez P.C., Ochoa A.C., Centeno F.,
RA Christianson D.W.;
RT "Crystal structure of human arginase I at 1.29-A resolution and exploration
RT of inhibition in the immune response.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13058-13063(2005).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND
RP THE SYNTHETIC INHIBITOR 2(S)-AMINO-6-BORONOHEXANOIC ACID, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND CATALYTIC ACTIVITY.
RX PubMed=17562323; DOI=10.1016/j.abb.2007.04.036;
RA Di Costanzo L., Moulin M., Haertlein M., Meilleur F., Christianson D.W.;
RT "Expression, purification, assay, and crystal structure of perdeuterated
RT human arginase I.";
RL Arch. Biochem. Biophys. 465:82-89(2007).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND
RP THIOSEMICARBAZIDE, AND SUBUNIT.
RX PubMed=17469833; DOI=10.1021/ja071567j;
RA Di Costanzo L., Pique M.E., Christianson D.W.;
RT "Crystal structure of human arginase I complexed with thiosemicarbazide
RT reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear
RT manganese cluster.";
RL J. Am. Chem. Soc. 129:6388-6389(2007).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND
RP THE SYNTHETIC INHIBITOR (2S)-2-AMINO-7,8-EPOXYOCTANOIC ACID.
RX PubMed=18802628; DOI=10.1039/b811797g;
RA Zakharian T.Y., Di Costanzo L., Christianson D.W.;
RT "Synthesis of (2S)-2-amino-7,8-epoxyoctanoic acid and structure of its
RT metal-bridging complex with human arginase I.";
RL Org. Biomol. Chem. 6:3240-3243(2008).
RN [20]
RP VARIANT ARGIN ARG-235.
RX PubMed=1463019;
RA Uchino T., Haraguchi Y., Aparicio J.M., Mizutani N., Higashikawa M.,
RA Naitoh H., Mori M., Matsuda I.;
RT "Three novel mutations in the liver-type arginase gene in three unrelated
RT Japanese patients with argininemia.";
RL Am. J. Hum. Genet. 51:1406-1412(1992).
RN [21]
RP VARIANT SER-290.
RX PubMed=1598908;
RA Grody W.W., Klein D., Dodson A.E., Kern R.M., Wissmann P.B., Goodman B.K.,
RA Bassand P., Marescau B., Kang S.-S., Leonard J.V., Cederbaum S.D.;
RT "Molecular genetic study of human arginase deficiency.";
RL Am. J. Hum. Genet. 50:1281-1290(1992).
RN [22]
RP VARIANTS ARGIN THR-11 AND VAL-138.
RX PubMed=7649538; DOI=10.1007/bf00210403;
RA Uchino T., Snyderman S.E., Lambert M., Qureshi I.A., Shapira S.K.,
RA Sansaricq C., Smit L.M.E., Jakobs C., Matsuda I.;
RT "Molecular basis of phenotypic variation in patients with argininemia.";
RL Hum. Genet. 96:255-260(1995).
RN [23]
RP VARIANTS ARGIN THR-11; ASP-27; VAL-74; ILE-134 AND GLN-308.
RX PubMed=22959135; DOI=10.1016/j.gene.2012.08.003;
RA Carvalho D.R., Brand G.D., Brum J.M., Takata R.I., Speck-Martins C.E.,
RA Pratesi R.;
RT "Analysis of novel ARG1 mutations causing hyperargininemia and correlation
RT with arginase I activity in erythrocytes.";
RL Gene 509:124-130(2012).
RN [24]
RP VARIANTS ARGIN VAL-125; THR-180 AND ARG-235.
RX PubMed=23859858; DOI=10.1016/j.pediatrneurol.2013.04.026;
RA Wu T.F., Liu Y.P., Li X.Y., Wang Q., Ding Y., Ma Y.Y., Song J.Q.,
RA Yang Y.L.;
RT "Five novel mutations in ARG1 gene in Chinese patients of argininemia.";
RL Pediatr. Neurol. 49:119-123(2013).
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 (PubMed:15546957, PubMed:16709924,
CC PubMed:19380772). In group 2 innate lymphoid cells (ILC2s) promotes
CC acute type 2 inflammation in the lung and is involved in optimal ILC2
CC proliferation but not survival (By similarity). In humans, the
CC immunological role in the monocytic/macrophage/dendritic cell (DC)
CC lineage is unsure. {ECO:0000250|UniProtKB:Q61176,
CC ECO:0000269|PubMed:15546957, ECO:0000269|PubMed:16709924,
CC ECO:0000269|PubMed:19380772}.
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; Evidence={ECO:0000269|PubMed:16141327,
CC ECO:0000269|PubMed:17562323};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16141327, ECO:0000269|PubMed:17469833,
CC ECO:0000269|PubMed:17562323, ECO:0000269|PubMed:18802628};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:16141327,
CC ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323,
CC ECO:0000269|PubMed:18802628};
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC arginine: step 1/1. {ECO:0000305|PubMed:16141327}.
CC -!- SUBUNIT: Homotrimer (PubMed:16141327, PubMed:17469833, PubMed:17562323,
CC PubMed:18802628, PubMed:2241902). Interacts with CMTM6
CC (PubMed:28813417). {ECO:0000269|PubMed:16141327,
CC ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323,
CC ECO:0000269|PubMed:18802628, ECO:0000269|PubMed:2241902,
CC ECO:0000269|PubMed:28813417}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16141327}.
CC Cytoplasmic granule {ECO:0000269|PubMed:15546957}. Note=Localized in
CC azurophil granules of neutrophils (PubMed:15546957).
CC {ECO:0000269|PubMed:15546957}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P05089-1; Sequence=Displayed;
CC Name=2; Synonyms=Erythroid variant;
CC IsoId=P05089-2; Sequence=VSP_009330;
CC Name=3;
CC IsoId=P05089-3; Sequence=VSP_009331;
CC -!- TISSUE SPECIFICITY: Within the immune system initially reported to be
CC selectively expressed in granulocytes (polymorphonuclear leukocytes
CC [PMNs]) (PubMed:15546957). Also detected in macrophages mycobacterial
CC granulomas (PubMed:23749634). Expressed in group2 innate lymphoid cells
CC (ILC2s) during lung disease (PubMed:27043409).
CC {ECO:0000269|PubMed:15546957, ECO:0000269|PubMed:23749634}.
CC -!- INDUCTION: By arginine or homoarginine.
CC -!- DISEASE: Argininemia (ARGIN) [MIM:207800]: A rare autosomal recessive
CC disorder of the urea cycle. Arginine is elevated in the blood and
CC cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical
CC manifestations include developmental delay, seizures, intellectual
CC disability, hypotonia, ataxia and progressive spastic quadriplegia.
CC {ECO:0000269|PubMed:1463019, ECO:0000269|PubMed:22959135,
CC ECO:0000269|PubMed:23859858, ECO:0000269|PubMed:7649538}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Arginase entry;
CC URL="https://en.wikipedia.org/wiki/Arginase";
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DR EMBL; M14502; AAA51776.1; -; mRNA.
DR EMBL; X12662; CAA31188.1; -; Genomic_DNA.
DR EMBL; X12663; CAA31188.1; JOINED; Genomic_DNA.
DR EMBL; X12664; CAA31188.1; JOINED; Genomic_DNA.
DR EMBL; X12665; CAA31188.1; JOINED; Genomic_DNA.
DR EMBL; X12666; CAA31188.1; JOINED; Genomic_DNA.
DR EMBL; X12667; CAA31188.1; JOINED; Genomic_DNA.
DR EMBL; X12668; CAA31188.1; JOINED; Genomic_DNA.
DR EMBL; X12669; CAA31188.1; JOINED; Genomic_DNA.
DR EMBL; AY074488; AAL71547.1; -; mRNA.
DR EMBL; BT006741; AAP35387.1; -; mRNA.
DR EMBL; AL121575; CAB92071.1; -; Genomic_DNA.
DR EMBL; AL121575; CAI23317.1; -; Genomic_DNA.
DR EMBL; AL121575; CAI23318.1; -; Genomic_DNA.
DR EMBL; BC005321; AAH05321.1; -; mRNA.
DR EMBL; BC020653; AAH20653.1; -; mRNA.
DR CCDS; CCDS5145.1; -. [P05089-1]
DR CCDS; CCDS59038.1; -. [P05089-2]
DR PIR; S02132; A26370.
DR RefSeq; NP_000036.2; NM_000045.3. [P05089-1]
DR RefSeq; NP_001231367.1; NM_001244438.1. [P05089-2]
DR PDB; 1WVA; X-ray; 1.94 A; A/B=1-322.
DR PDB; 1WVB; X-ray; 2.30 A; A/B=1-322.
DR PDB; 2AEB; X-ray; 1.29 A; A/B=1-322.
DR PDB; 2PHA; X-ray; 1.90 A; A/B=1-322.
DR PDB; 2PHO; X-ray; 1.95 A; A/B=1-322.
DR PDB; 2PLL; X-ray; 1.90 A; A/B=1-322.
DR PDB; 2ZAV; X-ray; 1.70 A; A/B=1-322.
DR PDB; 3DJ8; X-ray; 1.51 A; A/B=1-322.
DR PDB; 3E6K; X-ray; 2.10 A; A/B=1-322.
DR PDB; 3E6V; X-ray; 1.72 A; A/B=1-322.
DR PDB; 3F80; X-ray; 1.60 A; A/B=1-322.
DR PDB; 3GMZ; X-ray; 1.43 A; A/B=1-322.
DR PDB; 3GN0; X-ray; 1.70 A; A/B=1-322.
DR PDB; 3KV2; X-ray; 1.55 A; A/B=1-322.
DR PDB; 3LP4; X-ray; 1.90 A; A/B=1-322.
DR PDB; 3LP7; X-ray; 2.04 A; A/B=1-322.
DR PDB; 3MFV; X-ray; 1.90 A; A/B=1-322.
DR PDB; 3MFW; X-ray; 1.47 A; A/B=1-322.
DR PDB; 3MJL; X-ray; 1.90 A; A/B=1-322.
DR PDB; 3SJT; X-ray; 1.60 A; A/B=1-322.
DR PDB; 3SKK; X-ray; 1.70 A; A/B=1-322.
DR PDB; 3TF3; X-ray; 1.64 A; A/B=1-322.
DR PDB; 3TH7; X-ray; 2.10 A; A/B=1-322.
DR PDB; 3THE; X-ray; 1.97 A; A/B=1-322.
DR PDB; 3THH; X-ray; 1.85 A; A/B=1-322.
DR PDB; 3THJ; X-ray; 1.50 A; A/B=1-322.
DR PDB; 4FCI; X-ray; 1.82 A; A/B=1-322.
DR PDB; 4FCK; X-ray; 1.90 A; A/B=1-322.
DR PDB; 4GSM; X-ray; 1.70 A; A/B=1-322.
DR PDB; 4GSV; X-ray; 1.48 A; A/B=1-322.
DR PDB; 4GSZ; X-ray; 2.20 A; A/B=1-322.
DR PDB; 4GWC; X-ray; 1.90 A; A/B=1-322.
DR PDB; 4GWD; X-ray; 1.53 A; A/B=1-322.
DR PDB; 4HWW; X-ray; 1.30 A; A/B=5-318.
DR PDB; 4HXQ; X-ray; 1.45 A; A/B=5-318.
DR PDB; 4IE1; X-ray; 2.00 A; A/B=5-318.
DR PDB; 6Q92; X-ray; 1.50 A; A/B=1-322.
DR PDB; 6Q9P; X-ray; 1.66 A; A/B=1-322.
DR PDB; 6QAF; X-ray; 1.61 A; A/B=1-322.
DR PDB; 6V7C; X-ray; 1.80 A; A/B/C/D/E/F=1-322.
DR PDB; 6V7D; X-ray; 1.82 A; A/B/C/D/E/F=1-322.
DR PDB; 6V7E; X-ray; 1.99 A; A/B/C/D/E/F=1-322.
DR PDB; 6V7F; X-ray; 2.02 A; A/B/C/D/E/F=1-322.
DR PDB; 7K4G; X-ray; 1.80 A; A/B/C/D/E/F=1-322.
DR PDB; 7K4H; X-ray; 1.65 A; A/B/C/D/E/F=1-322.
DR PDB; 7K4I; X-ray; 1.98 A; A/B/C/D/E/F=1-322.
DR PDB; 7K4J; X-ray; 1.94 A; A/B/C/D/E/F=1-322.
DR PDB; 7K4K; X-ray; 2.27 A; A/B/C/D/E/F=1-322.
DR PDB; 7KLK; X-ray; 1.80 A; A/B/C/D/E/F=1-322.
DR PDB; 7KLL; X-ray; 2.22 A; A/B/C/D/E/F=1-322.
DR PDB; 7KLM; X-ray; 2.27 A; A/B/C/D/E/F=1-322.
DR PDB; 7LEX; EM; 3.60 A; A/B/C/J/M/N=1-322.
DR PDB; 7LEY; EM; 3.05 A; A/B/C=1-322.
DR PDB; 7LEZ; EM; 4.15 A; A/B/C/J/M/N=1-322.
DR PDB; 7LF0; EM; 3.68 A; A/B/C/J/M/N=1-322.
DR PDB; 7LF1; EM; 4.04 A; A/B/C/J/M/N=1-322.
DR PDB; 7LF2; EM; 3.72 A; A/B/C/J/Q/R=1-322.
DR PDBsum; 1WVA; -.
DR PDBsum; 1WVB; -.
DR PDBsum; 2AEB; -.
DR PDBsum; 2PHA; -.
DR PDBsum; 2PHO; -.
DR PDBsum; 2PLL; -.
DR PDBsum; 2ZAV; -.
DR PDBsum; 3DJ8; -.
DR PDBsum; 3E6K; -.
DR PDBsum; 3E6V; -.
DR PDBsum; 3F80; -.
DR PDBsum; 3GMZ; -.
DR PDBsum; 3GN0; -.
DR PDBsum; 3KV2; -.
DR PDBsum; 3LP4; -.
DR PDBsum; 3LP7; -.
DR PDBsum; 3MFV; -.
DR PDBsum; 3MFW; -.
DR PDBsum; 3MJL; -.
DR PDBsum; 3SJT; -.
DR PDBsum; 3SKK; -.
DR PDBsum; 3TF3; -.
DR PDBsum; 3TH7; -.
DR PDBsum; 3THE; -.
DR PDBsum; 3THH; -.
DR PDBsum; 3THJ; -.
DR PDBsum; 4FCI; -.
DR PDBsum; 4FCK; -.
DR PDBsum; 4GSM; -.
DR PDBsum; 4GSV; -.
DR PDBsum; 4GSZ; -.
DR PDBsum; 4GWC; -.
DR PDBsum; 4GWD; -.
DR PDBsum; 4HWW; -.
DR PDBsum; 4HXQ; -.
DR PDBsum; 4IE1; -.
DR PDBsum; 6Q92; -.
DR PDBsum; 6Q9P; -.
DR PDBsum; 6QAF; -.
DR PDBsum; 6V7C; -.
DR PDBsum; 6V7D; -.
DR PDBsum; 6V7E; -.
DR PDBsum; 6V7F; -.
DR PDBsum; 7K4G; -.
DR PDBsum; 7K4H; -.
DR PDBsum; 7K4I; -.
DR PDBsum; 7K4J; -.
DR PDBsum; 7K4K; -.
DR PDBsum; 7KLK; -.
DR PDBsum; 7KLL; -.
DR PDBsum; 7KLM; -.
DR PDBsum; 7LEX; -.
DR PDBsum; 7LEY; -.
DR PDBsum; 7LEZ; -.
DR PDBsum; 7LF0; -.
DR PDBsum; 7LF1; -.
DR PDBsum; 7LF2; -.
DR AlphaFoldDB; P05089; -.
DR SMR; P05089; -.
DR BioGRID; 106878; 126.
DR IntAct; P05089; 36.
DR MINT; P05089; -.
DR STRING; 9606.ENSP00000349446; -.
DR BindingDB; P05089; -.
DR ChEMBL; CHEMBL1075097; -.
DR DrugBank; DB01983; 2(S)-Amino-6-Boronohexanoic Acid.
DR DrugBank; DB04585; DEHYDRO-2(S)-AMINO-6-BORONOHEXANOIC ACID.
DR DrugBank; DB04197; Descarboxy-nor-N(Omega)-Hydroxy-L-Arginine.
DR DrugBank; DB02499; Dinor-N(Omega)-Hydroxy-L-Arginine.
DR DrugBank; DB06757; Manganese.
DR DrugBank; DB03144; N(5)-[(hydroxyamino)(imino)methyl]-L-ornithine.
DR DrugBank; DB02381; nor-NOHA.
DR DrugBank; DB00129; Ornithine.
DR DrugBank; DB04530; S,S-(2-Hydroxyethyl)Thiocysteine.
DR DrugBank; DB03731; S-2-(Boronoethyl)-L-Cysteine.
DR DrugBank; DB04648; S-propylamine-L-cysteine.
DR DrugBank; DB02689; S-{2-[Amino(Dihydroxy)-Lambda~4~-Sulfanyl]Ethyl}-D-Cysteine.
DR DrugBank; DB03904; Urea.
DR GuidetoPHARMACOLOGY; 1244; -.
DR GlyGen; P05089; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P05089; -.
DR PhosphoSitePlus; P05089; -.
DR BioMuta; ARG1; -.
DR DMDM; 12230985; -.
DR EPD; P05089; -.
DR jPOST; P05089; -.
DR MassIVE; P05089; -.
DR MaxQB; P05089; -.
DR PaxDb; P05089; -.
DR PeptideAtlas; P05089; -.
DR PRIDE; P05089; -.
DR ProteomicsDB; 51784; -. [P05089-1]
DR ProteomicsDB; 51785; -. [P05089-2]
DR ProteomicsDB; 51786; -. [P05089-3]
DR ABCD; P05089; 4 sequenced antibodies.
DR Antibodypedia; 779; 1296 antibodies from 50 providers.
DR CPTC; P05089; 1 antibody.
DR DNASU; 383; -.
DR Ensembl; ENST00000356962.2; ENSP00000349446.2; ENSG00000118520.15. [P05089-2]
DR Ensembl; ENST00000368087.8; ENSP00000357066.3; ENSG00000118520.15. [P05089-1]
DR Ensembl; ENST00000640973.1; ENSP00000492623.1; ENSG00000118520.15. [P05089-3]
DR GeneID; 383; -.
DR KEGG; hsa:383; -.
DR MANE-Select; ENST00000368087.8; ENSP00000357066.3; NM_000045.4; NP_000036.2.
DR UCSC; uc003qcp.3; human. [P05089-1]
DR CTD; 383; -.
DR DisGeNET; 383; -.
DR GeneCards; ARG1; -.
DR GeneReviews; ARG1; -.
DR HGNC; HGNC:663; ARG1.
DR HPA; ENSG00000118520; Tissue enriched (liver).
DR MalaCards; ARG1; -.
DR MIM; 207800; phenotype.
DR MIM; 608313; gene.
DR neXtProt; NX_P05089; -.
DR OpenTargets; ENSG00000118520; -.
DR Orphanet; 90; Argininemia.
DR PharmGKB; PA24947; -.
DR VEuPathDB; HostDB:ENSG00000118520; -.
DR eggNOG; KOG2965; Eukaryota.
DR GeneTree; ENSGT00950000183195; -.
DR HOGENOM; CLU_039478_6_1_1; -.
DR InParanoid; P05089; -.
DR OMA; DTPFQIV; -.
DR OrthoDB; 1179130at2759; -.
DR PhylomeDB; P05089; -.
DR TreeFam; TF300034; -.
DR BioCyc; MetaCyc:HS04231-MON; -.
DR BRENDA; 3.5.3.1; 2681.
DR PathwayCommons; P05089; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-70635; Urea cycle.
DR SABIO-RK; P05089; -.
DR SignaLink; P05089; -.
DR SIGNOR; P05089; -.
DR UniPathway; UPA00158; UER00270.
DR BioGRID-ORCS; 383; 14 hits in 1067 CRISPR screens.
DR ChiTaRS; ARG1; human.
DR EvolutionaryTrace; P05089; -.
DR GenomeRNAi; 383; -.
DR Pharos; P05089; Tchem.
DR PRO; PR:P05089; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P05089; protein.
DR Bgee; ENSG00000118520; Expressed in right lobe of liver and 121 other tissues.
DR ExpressionAtlas; P05089; baseline and differential.
DR Genevisible; P05089; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:0004053; F:arginase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0006527; P:arginine catabolic process; TAS:ProtInc.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:UniProtKB.
DR GO; GO:2000552; P:negative regulation of T-helper 2 cell cytokine production; IEA:Ensembl.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0070965; P:positive regulation of neutrophil mediated killing of fungus; IMP:UniProtKB.
DR GO; GO:1905541; P:regulation of L-arginine import across plasma membrane; IEA:Ensembl.
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; IEA:UniProtKB-UniPathway.
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 3D-structure; Adaptive immunity; Alternative splicing; Arginine metabolism;
KW Cytoplasm; Disease variant; Hydrolase; Immunity; Innate immunity;
KW Manganese; Metal-binding; Phosphoprotein; Reference proteome; Urea cycle.
FT CHAIN 1..322
FT /note="Arginase-1"
FT /id="PRO_0000173693"
FT BINDING 101
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16141327,
FT ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323,
FT ECO:0000269|PubMed:18802628, ECO:0007744|PDB:1WVA,
FT ECO:0007744|PDB:1WVB, ECO:0007744|PDB:2AEB,
FT ECO:0007744|PDB:2PHA, ECO:0007744|PDB:2PHO,
FT ECO:0007744|PDB:2PLL, ECO:0007744|PDB:2ZAV,
FT ECO:0007744|PDB:3DJ8, ECO:0007744|PDB:3E6K,
FT ECO:0007744|PDB:3E6V, ECO:0007744|PDB:3F80,
FT ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0,
FT ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP4,
FT ECO:0007744|PDB:3LP7, ECO:0007744|PDB:3MFV,
FT ECO:0007744|PDB:3MFW, ECO:0007744|PDB:3MJL,
FT ECO:0007744|PDB:3SJT, ECO:0007744|PDB:3SKK,
FT ECO:0007744|PDB:4FCI, ECO:0007744|PDB:4GSZ,
FT ECO:0007744|PDB:4GWC, ECO:0007744|PDB:4GWD,
FT ECO:0007744|PDB:4HWW, ECO:0007744|PDB:4HXQ,
FT ECO:0007744|PDB:4IE1"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16141327,
FT ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323,
FT ECO:0000269|PubMed:18802628, ECO:0007744|PDB:1WVA,
FT ECO:0007744|PDB:1WVB, ECO:0007744|PDB:2AEB,
FT ECO:0007744|PDB:2PHA, ECO:0007744|PDB:2PHO,
FT ECO:0007744|PDB:2PLL, ECO:0007744|PDB:2ZAV,
FT ECO:0007744|PDB:3DJ8, ECO:0007744|PDB:3E6K,
FT ECO:0007744|PDB:3E6V, ECO:0007744|PDB:3F80,
FT ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0,
FT ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP4,
FT ECO:0007744|PDB:3LP7, ECO:0007744|PDB:3MFV,
FT ECO:0007744|PDB:3MFW, ECO:0007744|PDB:3MJL,
FT ECO:0007744|PDB:3SJT, ECO:0007744|PDB:3SKK,
FT ECO:0007744|PDB:4FCI, ECO:0007744|PDB:4GSZ,
FT ECO:0007744|PDB:4GWC, ECO:0007744|PDB:4GWD,
FT ECO:0007744|PDB:4HWW, ECO:0007744|PDB:4HXQ,
FT ECO:0007744|PDB:4IE1"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16141327,
FT ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323,
FT ECO:0000269|PubMed:18802628, ECO:0007744|PDB:1WVA,
FT ECO:0007744|PDB:1WVB, ECO:0007744|PDB:2AEB,
FT ECO:0007744|PDB:2PHA, ECO:0007744|PDB:2PHO,
FT ECO:0007744|PDB:2PLL, ECO:0007744|PDB:2ZAV,
FT ECO:0007744|PDB:3DJ8, ECO:0007744|PDB:3E6K,
FT ECO:0007744|PDB:3E6V, ECO:0007744|PDB:3F80,
FT ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0,
FT ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP4,
FT ECO:0007744|PDB:3LP7, ECO:0007744|PDB:3MFV,
FT ECO:0007744|PDB:3MFW, ECO:0007744|PDB:3MJL,
FT ECO:0007744|PDB:3SJT, ECO:0007744|PDB:3SKK,
FT ECO:0007744|PDB:4FCI, ECO:0007744|PDB:4GSZ,
FT ECO:0007744|PDB:4GWC, ECO:0007744|PDB:4GWD,
FT ECO:0007744|PDB:4HWW, ECO:0007744|PDB:4HXQ,
FT ECO:0007744|PDB:4IE1"
FT BINDING 126..130
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0,
FT ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP7,
FT ECO:0007744|PDB:3THJ"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16141327,
FT ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323,
FT ECO:0000269|PubMed:18802628, ECO:0007744|PDB:1WVA,
FT ECO:0007744|PDB:1WVB, ECO:0007744|PDB:2AEB,
FT ECO:0007744|PDB:2PHA, ECO:0007744|PDB:2PHO,
FT ECO:0007744|PDB:2PLL, ECO:0007744|PDB:2ZAV,
FT ECO:0007744|PDB:3DJ8, ECO:0007744|PDB:3E6K,
FT ECO:0007744|PDB:3E6V, ECO:0007744|PDB:3F80,
FT ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0,
FT ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP4,
FT ECO:0007744|PDB:3LP7, ECO:0007744|PDB:3MFV,
FT ECO:0007744|PDB:3MFW, ECO:0007744|PDB:3MJL,
FT ECO:0007744|PDB:3SJT, ECO:0007744|PDB:3SKK,
FT ECO:0007744|PDB:4FCI, ECO:0007744|PDB:4GSZ,
FT ECO:0007744|PDB:4GWC, ECO:0007744|PDB:4GWD,
FT ECO:0007744|PDB:4HWW, ECO:0007744|PDB:4HXQ,
FT ECO:0007744|PDB:4IE1"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16141327,
FT ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323,
FT ECO:0000269|PubMed:18802628, ECO:0007744|PDB:1WVA,
FT ECO:0007744|PDB:1WVB, ECO:0007744|PDB:2AEB,
FT ECO:0007744|PDB:2PHA, ECO:0007744|PDB:2PHO,
FT ECO:0007744|PDB:2PLL, ECO:0007744|PDB:2ZAV,
FT ECO:0007744|PDB:3DJ8, ECO:0007744|PDB:3E6K,
FT ECO:0007744|PDB:3E6V, ECO:0007744|PDB:3F80,
FT ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0,
FT ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP4,
FT ECO:0007744|PDB:3LP7, ECO:0007744|PDB:3MFV,
FT ECO:0007744|PDB:3MFW, ECO:0007744|PDB:3MJL,
FT ECO:0007744|PDB:3SJT, ECO:0007744|PDB:3SKK,
FT ECO:0007744|PDB:4FCI, ECO:0007744|PDB:4GSZ,
FT ECO:0007744|PDB:4GWC, ECO:0007744|PDB:4GWD,
FT ECO:0007744|PDB:4HWW, ECO:0007744|PDB:4HXQ,
FT ECO:0007744|PDB:4IE1"
FT BINDING 137..139
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0,
FT ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP7,
FT ECO:0007744|PDB:3THJ"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0,
FT ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP7,
FT ECO:0007744|PDB:3THJ"
FT BINDING 232
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16141327,
FT ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323,
FT ECO:0000269|PubMed:18802628, ECO:0007744|PDB:1WVA,
FT ECO:0007744|PDB:1WVB, ECO:0007744|PDB:2AEB,
FT ECO:0007744|PDB:2PHA, ECO:0007744|PDB:2PHO,
FT ECO:0007744|PDB:2PLL, ECO:0007744|PDB:2ZAV,
FT ECO:0007744|PDB:3DJ8, ECO:0007744|PDB:3E6K,
FT ECO:0007744|PDB:3E6V, ECO:0007744|PDB:3F80,
FT ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0,
FT ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP4,
FT ECO:0007744|PDB:3LP7, ECO:0007744|PDB:3MFV,
FT ECO:0007744|PDB:3MFW, ECO:0007744|PDB:3MJL,
FT ECO:0007744|PDB:3SJT, ECO:0007744|PDB:3SKK,
FT ECO:0007744|PDB:4FCI, ECO:0007744|PDB:4GSZ,
FT ECO:0007744|PDB:4GWC, ECO:0007744|PDB:4GWD,
FT ECO:0007744|PDB:4HWW, ECO:0007744|PDB:4HXQ,
FT ECO:0007744|PDB:4IE1"
FT BINDING 232
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16141327,
FT ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323,
FT ECO:0000269|PubMed:18802628, ECO:0007744|PDB:1WVA,
FT ECO:0007744|PDB:1WVB, ECO:0007744|PDB:2AEB,
FT ECO:0007744|PDB:2PHA, ECO:0007744|PDB:2PHO,
FT ECO:0007744|PDB:2PLL, ECO:0007744|PDB:2ZAV,
FT ECO:0007744|PDB:3DJ8, ECO:0007744|PDB:3E6K,
FT ECO:0007744|PDB:3E6V, ECO:0007744|PDB:3F80,
FT ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0,
FT ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP4,
FT ECO:0007744|PDB:3LP7, ECO:0007744|PDB:3MFV,
FT ECO:0007744|PDB:3MFW, ECO:0007744|PDB:3MJL,
FT ECO:0007744|PDB:3SJT, ECO:0007744|PDB:3SKK,
FT ECO:0007744|PDB:4FCI, ECO:0007744|PDB:4GSZ,
FT ECO:0007744|PDB:4GWC, ECO:0007744|PDB:4GWD,
FT ECO:0007744|PDB:4HWW, ECO:0007744|PDB:4HXQ,
FT ECO:0007744|PDB:4IE1"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16141327,
FT ECO:0000269|PubMed:17469833, ECO:0000269|PubMed:17562323,
FT ECO:0000269|PubMed:18802628, ECO:0007744|PDB:1WVA,
FT ECO:0007744|PDB:1WVB, ECO:0007744|PDB:2AEB,
FT ECO:0007744|PDB:2PHA, ECO:0007744|PDB:2PHO,
FT ECO:0007744|PDB:2PLL, ECO:0007744|PDB:2ZAV,
FT ECO:0007744|PDB:3DJ8, ECO:0007744|PDB:3E6K,
FT ECO:0007744|PDB:3E6V, ECO:0007744|PDB:3F80,
FT ECO:0007744|PDB:3GMZ, ECO:0007744|PDB:3GN0,
FT ECO:0007744|PDB:3KV2, ECO:0007744|PDB:3LP4,
FT ECO:0007744|PDB:3LP7, ECO:0007744|PDB:3MFV,
FT ECO:0007744|PDB:3MFW, ECO:0007744|PDB:3MJL,
FT ECO:0007744|PDB:3SJT, ECO:0007744|PDB:3SKK,
FT ECO:0007744|PDB:4FCI, ECO:0007744|PDB:4GSZ,
FT ECO:0007744|PDB:4GWC, ECO:0007744|PDB:4GWD,
FT ECO:0007744|PDB:4HWW, ECO:0007744|PDB:4HXQ,
FT ECO:0007744|PDB:4IE1"
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 17
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61176"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61176"
FT MOD_RES 75
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61176"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 43
FT /note="Q -> QVTQNFLIL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_009330"
FT VAR_SEQ 204..289
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_009331"
FT VARIANT 11
FT /note="I -> T (in ARGIN; 12% of wild-type activity;
FT dbSNP:rs28941474)"
FT /evidence="ECO:0000269|PubMed:22959135,
FT ECO:0000269|PubMed:7649538"
FT /id="VAR_015594"
FT VARIANT 27
FT /note="G -> D (in ARGIN; 5.2% of wild-type activity;
FT dbSNP:rs1326930389)"
FT /evidence="ECO:0000269|PubMed:22959135"
FT /id="VAR_072164"
FT VARIANT 74
FT /note="G -> V (in ARGIN; 9.3% of wild-type activity)"
FT /evidence="ECO:0000269|PubMed:22959135"
FT /id="VAR_072165"
FT VARIANT 125
FT /note="A -> V (in ARGIN; decreases erythrocyte arginase
FT activity)"
FT /evidence="ECO:0000269|PubMed:23859858"
FT /id="VAR_072166"
FT VARIANT 134
FT /note="T -> I (in ARGIN; 9.3% of wild-type activity)"
FT /evidence="ECO:0000269|PubMed:22959135"
FT /id="VAR_072167"
FT VARIANT 138
FT /note="G -> V (in ARGIN; dbSNP:rs104893943)"
FT /evidence="ECO:0000269|PubMed:7649538"
FT /id="VAR_015595"
FT VARIANT 180
FT /note="R -> T (in ARGIN; decreases erythrocyte arginase
FT activity)"
FT /evidence="ECO:0000269|PubMed:23859858"
FT /id="VAR_072168"
FT VARIANT 235
FT /note="G -> R (in ARGIN; decreases erythrocyte arginase
FT activity; dbSNP:rs104893948)"
FT /evidence="ECO:0000269|PubMed:1463019,
FT ECO:0000269|PubMed:23859858"
FT /id="VAR_000674"
FT VARIANT 290
FT /note="T -> S (in dbSNP:rs104893942)"
FT /evidence="ECO:0000269|PubMed:1598908"
FT /id="VAR_000675"
FT VARIANT 308
FT /note="R -> Q (in ARGIN; 20.8% of wild-type activity;
FT dbSNP:rs377280518)"
FT /evidence="ECO:0000269|PubMed:22959135"
FT /id="VAR_072169"
FT CONFLICT 48
FT /note="K -> E (in Ref. 3; AAL71547)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="E -> Q (in Ref. 1; AAA51776)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="E -> K (in Ref. 3; AAL71547)"
FT /evidence="ECO:0000305"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:6Q92"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:2AEB"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:7KLK"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:2AEB"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:2AEB"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:7LEY"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3TH7"
FT HELIX 70..89
FT /evidence="ECO:0007829|PDB:2AEB"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:2AEB"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:2AEB"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2AEB"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2AEB"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:2AEB"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 208..220
FT /evidence="ECO:0007829|PDB:2AEB"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:2AEB"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:2AEB"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:2AEB"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 254..267
FT /evidence="ECO:0007829|PDB:2AEB"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:2AEB"
FT HELIX 286..303
FT /evidence="ECO:0007829|PDB:2AEB"
SQ SEQUENCE 322 AA; 34735 MW; 8F3BE2652243F622 CRC64;
MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQECDVKDY GDLPFADIPN
DSPFQIVKNP RSVGKASEQL AGKVAEVKKN GRISLVLGGD HSLAIGSISG HARVHPDLGV
IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR
DVDPGEHYIL KTLGIKYFSM TEVDRLGIGK VMEETLSYLL GRKKRPIHLS FDVDGLDPSF
TPATGTPVVG GLTYREGLYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVAIT
LACFGLAREG NHKPIDYLNP PK
