ARGI1_PIG
ID ARGI1_PIG Reviewed; 322 AA.
AC Q95JC8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kepka-Lenhart D., Morris S.M. Jr.;
RT "Sequence of pig arginase I.";
RL Submitted (JUN-2001) 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; AY039112; AAK91874.1; -; mRNA.
DR RefSeq; NP_999213.1; NM_214048.2.
DR RefSeq; XP_005659247.1; XM_005659190.2.
DR AlphaFoldDB; Q95JC8; -.
DR SMR; Q95JC8; -.
DR STRING; 9823.ENSSSCP00000004530; -.
DR PaxDb; Q95JC8; -.
DR PeptideAtlas; Q95JC8; -.
DR Ensembl; ENSSSCT00000004636; ENSSSCP00000004530; ENSSSCG00000004195.
DR Ensembl; ENSSSCT00005044893; ENSSSCP00005027488; ENSSSCG00005028353.
DR Ensembl; ENSSSCT00005044916; ENSSSCP00005027506; ENSSSCG00005028353.
DR Ensembl; ENSSSCT00005044927; ENSSSCP00005027514; ENSSSCG00005028353.
DR Ensembl; ENSSSCT00015077075; ENSSSCP00015031012; ENSSSCG00015057664.
DR Ensembl; ENSSSCT00025000287; ENSSSCP00025000095; ENSSSCG00025000224.
DR Ensembl; ENSSSCT00035071810; ENSSSCP00035029140; ENSSSCG00035053824.
DR Ensembl; ENSSSCT00045012908; ENSSSCP00045008882; ENSSSCG00045007689.
DR Ensembl; ENSSSCT00055027949; ENSSSCP00055022261; ENSSSCG00055014125.
DR Ensembl; ENSSSCT00065085231; ENSSSCP00065037231; ENSSSCG00065062146.
DR Ensembl; ENSSSCT00070039531; ENSSSCP00070033112; ENSSSCG00070019904.
DR Ensembl; ENSSSCT00070039536; ENSSSCP00070033115; ENSSSCG00070019904.
DR GeneID; 397115; -.
DR KEGG; ssc:397115; -.
DR CTD; 383; -.
DR VGNC; VGNC:85454; ARG1.
DR eggNOG; KOG2965; Eukaryota.
DR GeneTree; ENSGT00950000183195; -.
DR HOGENOM; CLU_039478_6_1_1; -.
DR InParanoid; Q95JC8; -.
DR OMA; DTPFQIV; -.
DR OrthoDB; 1179130at2759; -.
DR TreeFam; TF300034; -.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Reactome; R-SSC-70635; Urea cycle.
DR SABIO-RK; Q95JC8; -.
DR UniPathway; UPA00158; UER00270.
DR ChiTaRS; ARG1; pig.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Chromosome 1.
DR Bgee; ENSSSCG00000004195; Expressed in liver and 23 other tissues.
DR ExpressionAtlas; Q95JC8; baseline and differential.
DR Genevisible; Q95JC8; SS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; 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:0019547; P:arginine catabolic process to ornithine; IBA:GO_Central.
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_0000173695"
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 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61176"
FT MOD_RES 75
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61176"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05089"
SQ SEQUENCE 322 AA; 35018 MW; D99FB071CE916B2F CRC64;
MSFKSQSIGI IGAPFSKGQP RGGVEEGPTA LRKAGLLEKL KEQECDVKDY GDLCFADVPN
DTPFQIVKNP RSVGKANQQL ADVVAEIKKN GRTSLVLGGD HSMAIGSISG HARVHPDLCV
IWVDAHTDIN TPLTTTTGNL HGQPVSFLLK ELKEKIPEVP GLSWVTPCLS AKDIVYIGLR
DVDPAEHYIL KTLGIKYFSM IEVDKLGIGK VMEEAFSYLL GRKKRPIHLS FDVDGLDPFF
TPATGTPVHG GLSYREGIYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVALV
LACFGVAREG NHKPIDYLKP PK
