ARGI1_BOVIN
ID ARGI1_BOVIN Reviewed; 322 AA.
AC Q2KJ64;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
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 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].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Interacts with CMTM6 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P05089}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; BC105497; AAI05498.1; -; mRNA.
DR RefSeq; NP_001039619.1; NM_001046154.1.
DR RefSeq; XP_005210981.1; XM_005210924.3.
DR RefSeq; XP_010806852.1; XM_010808550.2.
DR AlphaFoldDB; Q2KJ64; -.
DR SMR; Q2KJ64; -.
DR STRING; 9913.ENSBTAP00000016461; -.
DR BindingDB; Q2KJ64; -.
DR ChEMBL; CHEMBL1075060; -.
DR PaxDb; Q2KJ64; -.
DR PeptideAtlas; Q2KJ64; -.
DR PRIDE; Q2KJ64; -.
DR Ensembl; ENSBTAT00000016461; ENSBTAP00000016461; ENSBTAG00000012403.
DR GeneID; 513608; -.
DR KEGG; bta:513608; -.
DR CTD; 383; -.
DR VEuPathDB; HostDB:ENSBTAG00000012403; -.
DR VGNC; VGNC:26070; ARG1.
DR eggNOG; KOG2965; Eukaryota.
DR GeneTree; ENSGT00950000183195; -.
DR HOGENOM; CLU_039478_6_1_1; -.
DR InParanoid; Q2KJ64; -.
DR OMA; DTPFQIV; -.
DR OrthoDB; 1179130at2759; -.
DR TreeFam; TF300034; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-70635; Urea cycle.
DR SABIO-RK; Q2KJ64; -.
DR UniPathway; UPA00158; UER00270.
DR PRO; PR:Q2KJ64; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000012403; Expressed in liver and 30 other 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; IEA:Ensembl.
DR GO; GO:0004053; F:arginase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IBA:GO_Central.
DR GO; GO:0042832; P:defense response to protozoan; 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; IEA:Ensembl.
DR GO; GO:2000552; P:negative regulation of T-helper 2 cell cytokine production; IEA:Ensembl.
DR GO; GO:0070965; P:positive regulation of neutrophil mediated killing of fungus; 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 2: Evidence at transcript level;
KW Arginine metabolism; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Phosphoprotein; Reference proteome; Urea cycle.
FT CHAIN 1..322
FT /note="Arginase-1"
FT /id="PRO_0000240339"
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:0000250|UniProtKB:Q61176"
FT MOD_RES 17
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61176"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT MOD_RES 75
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61176"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05089"
SQ SEQUENCE 322 AA; 35009 MW; B71BE758F1AB83CA CRC64;
MSSKPQSIGV IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KELECDVKDY GDLSFADNLD
DSPFQIVKNP RCVGKASEKL ADVVAEVKKT GRISLVLGGD HSLAIGSISG HARVHPDLCV
IWVDAHTDIN TPLTTKTGNL HGQPVSFLLK ELKEKMPEVP GFYWVAPCIS AKDIVYIGLR
DVDPGEHYIL KTLGIKYFSM TEVDKLGIGK VMEETFSYLL GRKKRPIHLS FDVDGLDPSF
TPATGTPVQG GLTYREGLYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTTVAIT
MACFGVAREG NHKPIDYLSP PK
