ARGI2_HUMAN
ID ARGI2_HUMAN Reviewed; 354 AA.
AC P78540; B2R690; Q6FHY8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Arginase-2, mitochondrial;
DE EC=3.5.3.1 {ECO:0000269|PubMed:12859189};
DE AltName: Full=Arginase II;
DE AltName: Full=Kidney-type arginase;
DE AltName: Full=Non-hepatic arginase;
DE AltName: Full=Type II arginase;
DE Flags: Precursor;
GN Name=ARG2;
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], AND SUBCELLULAR LOCATION.
RX PubMed=8898077; DOI=10.1016/0014-5793(96)01015-0;
RA Gotoh T., Sonoki T., Nagasaki A., Terada K., Takiguchi M., Mori M.;
RT "Molecular cloning of cDNA for nonhepatic mitochondrial arginase (arginase
RT II) and comparison of its induction with nitric oxide synthase in a murine
RT macrophage-like cell line.";
RL FEBS Lett. 395:119-122(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8954792; DOI=10.1006/geno.1996.0606;
RA Vockley J.G., Jenkinson C.P., Shukla H., Kern R.M., Grody W.W.,
RA Cederbaum S.D.;
RT "Cloning and characterization of the human type II arginase gene.";
RL Genomics 38:118-123(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=9256072; DOI=10.1016/s0378-1119(97)00099-1;
RA Morris S.M. Jr., Bhamidipati D., Kepka-Lenhart D.;
RT "Human type II arginase: sequence analysis and tissue-specific
RT expression.";
RL Gene 193:157-161(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Erythroblast;
RA Lee Y.T., Miller J.L.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, Muscle, Prostate, and Testis;
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 [9]
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 [10]
RP FUNCTION.
RX PubMed=22928666; DOI=10.1111/acel.12001;
RA Yepuri G., Velagapudi S., Xiong Y., Rajapakse A.G., Montani J.P.,
RA Ming X.F., Yang Z.;
RT "Positive crosstalk between arginase-II and S6K1 in vascular endothelial
RT inflammation and aging.";
RL Aging Cell 11:1005-1016(2012).
RN [11]
RP FUNCTION.
RX PubMed=23832324; DOI=10.1161/jaha.113.000096;
RA Xiong Y., Yu Y., Montani J.P., Yang Z., Ming X.F.;
RT "Arginase-II induces vascular smooth muscle cell senescence and apoptosis
RT through p66Shc and p53 independently of its l-arginine ureahydrolase
RT activity: implications for atherosclerotic plaque vulnerability.";
RL J. Am. Heart Assoc. 2:E000096-E000096(2013).
RN [12]
RP FUNCTION.
RX PubMed=25484082; DOI=10.4161/15548627.2014.981789;
RA Xiong Y., Yepuri G., Forbiteh M., Yu Y., Montani J.P., Yang Z., Ming X.F.;
RT "ARG2 impairs endothelial autophagy through regulation of MTOR and
RT PRKAA/AMPK signaling in advanced atherosclerosis.";
RL Autophagy 10:2223-2238(2014).
RN [13]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=27745970; DOI=10.1016/j.cell.2016.09.031;
RA Geiger R., Rieckmann J.C., Wolf T., Basso C., Feng Y., Fuhrer T.,
RA Kogadeeva M., Picotti P., Meissner F., Mann M., Zamboni N., Sallusto F.,
RA Lanzavecchia A.;
RT "L-arginine modulates T cell metabolism and enhances survival and anti-
RT tumor activity.";
RL Cell 167:829-842(2016).
RN [14]
RP FUNCTION.
RX PubMed=27214549; DOI=10.1172/jci82925;
RA Xu W., Ghosh S., Comhair S.A., Asosingh K., Janocha A.J., Mavrakis D.A.,
RA Bennett C.D., Gruca L.L., Graham B.B., Queisser K.A., Kao C.C., Wedes S.H.,
RA Petrich J.M., Tuder R.M., Kalhan S.C., Erzurum S.C.;
RT "Increased mitochondrial arginine metabolism supports bioenergetics in
RT asthma.";
RL J. Clin. Invest. 126:2465-2481(2016).
RN [15]
RP FUNCTION.
RX PubMed=28614294; DOI=10.1038/nature22795;
RA McGovern N., Shin A., Low G., Low D., Duan K., Yao L.J., Msallam R.,
RA Low I., Shadan N.B., Sumatoh H.R., Soon E., Lum J., Mok E., Hubert S.,
RA See P., Kunxiang E.H., Lee Y.H., Janela B., Choolani M., Mattar C.N.Z.,
RA Fan Y., Lim T.K.H., Chan D.K.H., Tan K.K., Tam J.K.C., Schuster C.,
RA Elbe-Buerger A., Wang X.N., Bigley V., Collin M., Haniffa M., Schlitzer A.,
RA Poidinger M., Albani S., Larbi A., Newell E.W., Chan J.K.Y., Ginhoux F.;
RT "Human fetal dendritic cells promote prenatal T-cell immune suppression
RT through arginase-2.";
RL Nature 546:662-666(2017).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 24-329 IN COMPLEX WITH MANGANESE
RP IONS AND S-2-(BORONOETHYL)-L-CYSTEINE, COFACTOR, SUBUNIT, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=12859189; DOI=10.1021/bi034340j;
RA Cama E., Colleluori D.M., Emig F.A., Shin H., Kim S.W., Kim N.N.,
RA Traish A.M., Ash D.E., Christianson D.W.;
RT "Human arginase II: crystal structure and physiological role in male and
RT female sexual arousal.";
RL Biochemistry 42:8445-8451(2003).
CC -!- FUNCTION: May play a role in the regulation of extra-urea cycle
CC arginine metabolism and also in down-regulation of nitric oxide
CC synthesis. Extrahepatic arginase functions to regulate L-arginine
CC bioavailability to nitric oxid synthase (NOS). Arginine metabolism is a
CC critical regulator of innate and adaptive immune responses. Seems to be
CC involved in negative regulation of the survival capacity of activated
CC CD4(+) and CD8(+) T cells (PubMed:27745970). May suppress inflammation-
CC related signaling in asthmatic airway epithelium (PubMed:27214549). May
CC contribute to the immune evasion of H.pylori by restricting M1
CC macrophage activation and polyamine metabolism (By similarity). In
CC fetal dendritic cells may play a role in promoting immune suppression
CC and T cell TNF-alpha production during gestation (PubMed:28614294).
CC Regulates RPS6KB1 signaling, which promotes endothelial cell senescence
CC and inflammation and implicates NOS3/eNOS dysfunction
CC (PubMed:22928666). Can inhibit endothelial autophagy independently of
CC its enzymatic activity implicating mTORC2 signaling (PubMed:25484082).
CC Involved in vascular smooth muscle cell senescence and apoptosis
CC independently of its enzymatic activity (PubMed:23832324). Since NOS is
CC found in the penile corpus cavernosum smooth muscle, the clitoral
CC corpus cavernosum and the vagina, arginase-2 plays a role in both male
CC and female sexual arousal (PubMed:12859189).
CC {ECO:0000250|UniProtKB:O08691, ECO:0000269|PubMed:12859189,
CC ECO:0000269|PubMed:22928666, ECO:0000269|PubMed:23832324,
CC ECO:0000269|PubMed:25484082, ECO:0000269|PubMed:27214549,
CC ECO:0000269|PubMed:27745970}.
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:0000269|PubMed:12859189};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742,
CC ECO:0000269|PubMed:12859189};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00742, ECO:0000269|PubMed:12859189};
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12859189}.
CC -!- INTERACTION:
CC P78540; Q3SYB3: FOXD4L6; NbExp=3; IntAct=EBI-9056613, EBI-6425864;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:8898077}.
CC -!- TISSUE SPECIFICITY: Expressed most strongly in kidney and prostate,
CC much less strongly in the brain, skeletal muscle, placenta, lung,
CC mammary gland, macrophage, uterus, testis and gut, but apparently not
CC in the liver, heart and pancreas. Expressed in activated T cells
CC (PubMed:27745970). {ECO:0000269|PubMed:27745970}.
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; D86724; BAA13158.1; -; mRNA.
DR EMBL; U75667; AAB39855.1; -; mRNA.
DR EMBL; U82256; AAC51664.1; -; mRNA.
DR EMBL; AY074489; AAL71548.1; -; mRNA.
DR EMBL; CR536550; CAG38787.1; -; mRNA.
DR EMBL; AK312484; BAG35387.1; -; mRNA.
DR EMBL; CH471061; EAW80943.1; -; Genomic_DNA.
DR EMBL; BC001350; AAH01350.1; -; mRNA.
DR EMBL; BC008464; AAH08464.1; -; mRNA.
DR EMBL; BC029050; AAH29050.1; -; mRNA.
DR CCDS; CCDS9785.1; -.
DR RefSeq; NP_001163.1; NM_001172.3.
DR PDB; 1PQ3; X-ray; 2.70 A; A/B/C/D/E/F=24-329.
DR PDB; 4HZE; X-ray; 1.60 A; A/B/C=24-329.
DR PDB; 4I06; X-ray; 1.80 A; A/B/C=24-329.
DR PDB; 4IE2; X-ray; 2.21 A; A/B/C=24-329.
DR PDB; 4IE3; X-ray; 2.35 A; A/B/C=24-329.
DR PDB; 4IXU; X-ray; 1.90 A; A/B/C=24-329.
DR PDB; 4IXV; X-ray; 2.30 A; A/B/C=24-329.
DR PDB; 6Q37; X-ray; 2.21 A; A/B/C=24-329.
DR PDB; 6Q39; X-ray; 2.21 A; A/B/C=24-329.
DR PDB; 6SS2; X-ray; 2.40 A; AAA=23-354.
DR PDB; 6SS4; X-ray; 2.90 A; AAA=23-354.
DR PDB; 6SS6; X-ray; 3.25 A; AAA/BBB/CCC=23-354.
DR PDBsum; 1PQ3; -.
DR PDBsum; 4HZE; -.
DR PDBsum; 4I06; -.
DR PDBsum; 4IE2; -.
DR PDBsum; 4IE3; -.
DR PDBsum; 4IXU; -.
DR PDBsum; 4IXV; -.
DR PDBsum; 6Q37; -.
DR PDBsum; 6Q39; -.
DR PDBsum; 6SS2; -.
DR PDBsum; 6SS4; -.
DR PDBsum; 6SS6; -.
DR AlphaFoldDB; P78540; -.
DR SMR; P78540; -.
DR BioGRID; 106879; 15.
DR IntAct; P78540; 6.
DR MINT; P78540; -.
DR STRING; 9606.ENSP00000261783; -.
DR BindingDB; P78540; -.
DR ChEMBL; CHEMBL1795148; -.
DR DrugBank; DB00125; Arginine.
DR DrugBank; DB00129; Ornithine.
DR DrugBank; DB03731; S-2-(Boronoethyl)-L-Cysteine.
DR GuidetoPHARMACOLOGY; 1245; -.
DR iPTMnet; P78540; -.
DR PhosphoSitePlus; P78540; -.
DR BioMuta; ARG2; -.
DR DMDM; 2492935; -.
DR EPD; P78540; -.
DR jPOST; P78540; -.
DR MassIVE; P78540; -.
DR MaxQB; P78540; -.
DR PaxDb; P78540; -.
DR PeptideAtlas; P78540; -.
DR PRIDE; P78540; -.
DR ProteomicsDB; 57644; -.
DR ABCD; P78540; 8 sequenced antibodies.
DR Antibodypedia; 1; 438 antibodies from 36 providers.
DR CPTC; P78540; 1 antibody.
DR DNASU; 384; -.
DR Ensembl; ENST00000261783.4; ENSP00000261783.3; ENSG00000081181.8.
DR GeneID; 384; -.
DR KEGG; hsa:384; -.
DR MANE-Select; ENST00000261783.4; ENSP00000261783.3; NM_001172.4; NP_001163.1.
DR UCSC; uc001xjs.4; human.
DR CTD; 384; -.
DR DisGeNET; 384; -.
DR GeneCards; ARG2; -.
DR HGNC; HGNC:664; ARG2.
DR HPA; ENSG00000081181; Tissue enhanced (parathyroid gland, prostate, thyroid gland).
DR MIM; 107830; gene.
DR neXtProt; NX_P78540; -.
DR OpenTargets; ENSG00000081181; -.
DR PharmGKB; PA24948; -.
DR VEuPathDB; HostDB:ENSG00000081181; -.
DR eggNOG; KOG2965; Eukaryota.
DR GeneTree; ENSGT00950000183195; -.
DR HOGENOM; CLU_039478_6_0_1; -.
DR InParanoid; P78540; -.
DR OMA; IATCFGQ; -.
DR OrthoDB; 1179130at2759; -.
DR PhylomeDB; P78540; -.
DR TreeFam; TF300034; -.
DR BioCyc; MetaCyc:HS01388-MON; -.
DR BRENDA; 3.5.3.1; 2681.
DR PathwayCommons; P78540; -.
DR Reactome; R-HSA-70635; Urea cycle.
DR SABIO-RK; P78540; -.
DR SignaLink; P78540; -.
DR SIGNOR; P78540; -.
DR UniPathway; UPA00158; UER00270.
DR BioGRID-ORCS; 384; 15 hits in 1090 CRISPR screens.
DR ChiTaRS; ARG2; human.
DR EvolutionaryTrace; P78540; -.
DR GenomeRNAi; 384; -.
DR Pharos; P78540; Tchem.
DR PRO; PR:P78540; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P78540; protein.
DR Bgee; ENSG00000081181; Expressed in tendon of biceps brachii and 186 other tissues.
DR ExpressionAtlas; P78540; baseline and differential.
DR Genevisible; P78540; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004053; F:arginase activity; IMP:CACAO.
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:0019547; P:arginine catabolic process to ornithine; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1905403; P:negative regulation of activated CD8-positive, alpha-beta T cell apoptotic process; IEA:Ensembl.
DR GO; GO:2000562; P:negative regulation of CD4-positive, alpha-beta T cell proliferation; IEA:Ensembl.
DR GO; GO:0071644; P:negative regulation of chemokine (C-C motif) ligand 4 production; IEA:Ensembl.
DR GO; GO:0071650; P:negative regulation of chemokine (C-C motif) ligand 5 production; IEA:Ensembl.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; IEA:Ensembl.
DR GO; GO:0032696; P:negative regulation of interleukin-13 production; IEA:Ensembl.
DR GO; GO:0032700; P:negative regulation of interleukin-17 production; IEA:Ensembl.
DR GO; GO:0071641; P:negative regulation of macrophage inflammatory protein 1 alpha production; IEA:Ensembl.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB.
DR GO; GO:0002829; P:negative regulation of type 2 immune response; IEA:Ensembl.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; TAS:ProtInc.
DR GO; GO:2000774; P:positive regulation of cellular senescence; IDA:UniProtKB.
DR GO; GO:0032651; P:regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR GO; GO:0006941; P:striated muscle contraction; IEA:Ensembl.
DR GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR CDD; cd09989; Arginase; 1.
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; Arginine metabolism; Hydrolase; Immunity;
KW Innate immunity; Manganese; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide; Urea cycle.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..354
FT /note="Arginase-2, mitochondrial"
FT /id="PRO_0000002084"
FT REGION 334..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12859189,
FT ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE,
FT ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2,
FT ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU,
FT ECO:0007744|PDB:4IXV"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12859189,
FT ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE,
FT ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2,
FT ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU,
FT ECO:0007744|PDB:4IXV"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12859189,
FT ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE,
FT ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2,
FT ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU,
FT ECO:0007744|PDB:4IXV"
FT BINDING 145..149
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12859189,
FT ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE,
FT ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2,
FT ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU,
FT ECO:0007744|PDB:4IXV"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12859189,
FT ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE,
FT ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2,
FT ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU,
FT ECO:0007744|PDB:4IXV"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12859189,
FT ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE,
FT ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2,
FT ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU,
FT ECO:0007744|PDB:4IXV"
FT BINDING 156..158
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12859189,
FT ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE,
FT ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2,
FT ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU,
FT ECO:0007744|PDB:4IXV"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12859189,
FT ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE,
FT ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2,
FT ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU,
FT ECO:0007744|PDB:4IXV"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12859189,
FT ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE,
FT ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2,
FT ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU,
FT ECO:0007744|PDB:4IXV"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12859189,
FT ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE,
FT ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2,
FT ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU,
FT ECO:0007744|PDB:4IXV"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12859189,
FT ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE,
FT ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2,
FT ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU,
FT ECO:0007744|PDB:4IXV"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12859189,
FT ECO:0007744|PDB:1PQ3, ECO:0007744|PDB:4HZE,
FT ECO:0007744|PDB:4I06, ECO:0007744|PDB:4IE2,
FT ECO:0007744|PDB:4IE3, ECO:0007744|PDB:4IXU,
FT ECO:0007744|PDB:4IXV"
FT VARIANT 240
FT /note="G -> R (in dbSNP:rs17104534)"
FT /id="VAR_033520"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:4HZE"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:4HZE"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 89..108
FT /evidence="ECO:0007829|PDB:4HZE"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:4HZE"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:4HZE"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:4HZE"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:4HZE"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:4HZE"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:4HZE"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4HZE"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:4HZE"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 273..285
FT /evidence="ECO:0007829|PDB:4HZE"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:4HZE"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:4HZE"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1PQ3"
FT HELIX 305..322
FT /evidence="ECO:0007829|PDB:4HZE"
SQ SEQUENCE 354 AA; 38578 MW; 1624FAC7D515C68B CRC64;
MSLRGSLSRL LQTRVHSILK KSVHSVAVIG APFSQGQKRK GVEHGPAAIR EAGLMKRLSS
LGCHLKDFGD LSFTPVPKDD LYNNLIVNPR SVGLANQELA EVVSRAVSDG YSCVTLGGDH
SLAIGTISGH ARHCPDLCVV WVDAHADINT PLTTSSGNLH GQPVSFLLRE LQDKVPQLPG
FSWIKPCISS ASIVYIGLRD VDPPEHFILK NYDIQYFSMR DIDRLGIQKV MERTFDLLIG
KRQRPIHLSF DIDAFDPTLA PATGTPVVGG LTYREGMYIA EEIHNTGLLS ALDLVEVNPQ
LATSEEEAKT TANLAVDVIA SSFGQTREGG HIVYDQLPTP SSPDESENQA RVRI
