ARGI2_RABIT
ID ARGI2_RABIT Reviewed; 354 AA.
AC Q4VK78;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ah-Ra K., Yun Hyun H., Jang-Soo C.;
RT "Chondrocyte phenotype-specific gene.";
RL Submitted (DEC-2004) 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}.
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; AY864853; AAX58119.1; -; mRNA.
DR RefSeq; NP_001075650.1; NM_001082181.1.
DR AlphaFoldDB; Q4VK78; -.
DR SMR; Q4VK78; -.
DR STRING; 9986.ENSOCUP00000000507; -.
DR PRIDE; Q4VK78; -.
DR GeneID; 100008967; -.
DR KEGG; ocu:100008967; -.
DR CTD; 384; -.
DR eggNOG; KOG2965; Eukaryota.
DR InParanoid; Q4VK78; -.
DR OrthoDB; 1179130at2759; -.
DR BRENDA; 3.5.3.1; 1749.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004053; F:arginase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
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_0000044614"
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"
SQ SEQUENCE 354 AA; 38393 MW; 23313E232A8B6E8E CRC64;
MSYGSCVSRL LRTRVQSVLK KSVHSVAVIG APFSQGQKRK GVECGPAAIR DAGLVKRLSD
LGCRLKDYGD LSFTPVPKDD LYNNLIVNPR SVGLANQELA EVVNRAVSGG YSCVTVGGDH
SLAIGTISGH ARHCPDLCVV WVDAHADINT PLTTSSGNLH GQPVSFLLRE LQDKVPQLPG
FSWIKPCISS PSIVYIGLRD VDPPEHFILK KYDIQYFSMR DIDRLGIQKV MEQTFDLLIG
KKQRPIHLSF DIDAFDPTLA PATGTPGCGG ADLSRRMYIS EEIHNTGLLS ALDLVEVNPR
LAASDEEAKA TASLAVDVIA SSFGQTREGG HTVYEQLPPP SSPHESENAE RVRI
