ARGI2_BOVIN
ID ARGI2_BOVIN Reviewed; 354 AA.
AC Q58DL1; A2VEA1;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Arginase-2, mitochondrial;
DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
DE AltName: Full=Arginase II;
DE AltName: Full=Type II arginase;
DE Flags: Precursor;
GN Name=ARG2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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 T
CC cells. May suppress inflammation-related signaling in asthmatic airway
CC epithelium. May play a role in promoting prenatal immune suppression.
CC Regulates RPS6KB1 signaling, which promotes endothelial cell senescence
CC and inflammation and implicates NOS3/eNOS dysfunction. Can inhibit
CC endothelial autophagy independently of its enzymatic activity
CC implicating mTORC2 signaling. Involved in vascular smooth muscle cell
CC senescence and apoptosis independently of its enzymatic activity.
CC {ECO:0000250|UniProtKB:O08691, ECO:0000250|UniProtKB:P78540}.
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. {ECO:0000250|UniProtKB:P78540}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O08691,
CC ECO:0000250|UniProtKB:P78540}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; BT021586; AAX46433.1; -; mRNA.
DR EMBL; BC133643; AAI33644.1; -; mRNA.
DR RefSeq; NP_001017942.1; NM_001017942.1.
DR STRING; 9913.ENSBTAP00000002529; -.
DR PaxDb; Q58DL1; -.
DR PRIDE; Q58DL1; -.
DR GeneID; 518752; -.
DR KEGG; bta:518752; -.
DR CTD; 384; -.
DR eggNOG; KOG2965; Eukaryota.
DR InParanoid; Q58DL1; -.
DR OrthoDB; 1179130at2759; -.
DR SABIO-RK; Q58DL1; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004053; F:arginase activity; IBA:GO_Central.
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:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW 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_0000041752"
FT REGION 330..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:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 145..149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 156..158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P78540"
FT CONFLICT 276
FT /note="G -> D (in Ref. 2; AAI33644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 38616 MW; E6DFBC08F32EEA04 CRC64;
MSLRSHLSRL LRTQVHSVRK KSVHSVAVIG APFSQGQKRK GVEYGPAAVR XAGLMKRLSD
LGCHLKDFGD LNFTPVPKDD LYNNLIVNPR SVGLANQELA EVVSRAVSGG YSCVTVGGDH
SLAIGTISGH ARHCPDLGVI WVDAHADINT PLTTSSGNLH GQPVSFLLRE LQDKVPQLPG
FSWIKPCISS PSIVYIGLRD VDPPEHFILK NYDIQYFSMR DIDRLGIQKV MEQTFDLLIG
KRQRPIHLSF DIDAFDPTLA PATGTPVVGG LTYREGIYIT EEIHSTGLLS ALDLVEVNPR
LAVSEEEAKA TASLAVDVIA SSFGQTREGG HIVYDQLPTP SSPDESESEE RVRI
