ARGI1_RABIT
ID ARGI1_RABIT Reviewed; 322 AA.
AC Q95KM0;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 109.
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 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].
RC TISSUE=Liver;
RA Teupser D., Burkhardt R., Wilfert W., Thiery J.;
RT "Oryctolagus cuniculus arginase 1, liver (Arg1) mRNA.";
RL Submitted (JAN-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.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; AF365403; AAK52824.2; -; mRNA.
DR RefSeq; NP_001075577.1; NM_001082108.1.
DR AlphaFoldDB; Q95KM0; -.
DR SMR; Q95KM0; -.
DR STRING; 9986.ENSOCUP00000001559; -.
DR GeneID; 100008814; -.
DR KEGG; ocu:100008814; -.
DR CTD; 383; -.
DR eggNOG; KOG2965; Eukaryota.
DR InParanoid; Q95KM0; -.
DR OrthoDB; 1179130at2759; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; 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:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
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_0000173696"
FT REGION 1..26
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 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05089"
SQ SEQUENCE 322 AA; 34448 MW; FCE8DEE779C035D8 CRC64;
MSSKSKSIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQEHDVTDY GDLSFADVPN
DSPFHIVKNP RAVGRANEQL AGAVAEIKKN GRISLVLGGD HSLAIGSISG HASVCPDLAV
IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR
DVDPGEHYIV KTLGIKYFSM TEVDKLGIGK VMEETLCYLL GRKKRPIHLS FDVDGLDPSF
TPATGTPVAG GLSYREGIYI TEAIHKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVALT
LASFGVAREG NHKPIDYLHP PK
