ARGI1_XENLA
ID ARGI1_XENLA Reviewed; 316 AA.
AC P30759;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Arginase-1;
DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
DE AltName: Full=Arginase, hepatic;
DE AltName: Full=Type I arginase;
GN Name=arg1; Synonyms=argl;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7916684; DOI=10.1111/j.1432-1033.1993.tb17622.x;
RA Xu Q., Baker B.S., Tata J.R.;
RT "Developmental and hormonal regulation of the Xenopus liver-type arginase
RT gene.";
RL Eur. J. Biochem. 211:891-898(1993).
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=7929226; DOI=10.1016/s0021-9258(18)47251-1;
RA Patterton D., Shi Y.-B.;
RT "Thyroid hormone-dependent differential regulation of multiple arginase
RT genes during amphibian metamorphosis.";
RL J. Biol. Chem. 269:25328-25334(1994).
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.
CC -!- TISSUE SPECIFICITY: Strongest expression in liver.
CC -!- DEVELOPMENTAL STAGE: First expressed at stage 10/11 of gastrulation.
CC Higher levels found at stages 23/24 and 60-62. In the intestine,
CC expression increased during metamorphosis (stage 62/64) and then,
CC decreased. In the tail region, highest levels were found at the time of
CC tail resorption. Activated, but at low levels, at stages 56-58 of
CC hindlimb development. {ECO:0000269|PubMed:7929226}.
CC -!- INDUCTION: Slow-response activation by thyroid hormone (T3).
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; X69820; CAA49474.1; -; mRNA.
DR PIR; S29394; S29394.
DR RefSeq; NP_001095269.1; NM_001101799.1.
DR AlphaFoldDB; P30759; -.
DR SMR; P30759; -.
DR BioGRID; 607768; 1.
DR PRIDE; P30759; -.
DR GeneID; 779061; -.
DR CTD; 383; -.
DR SABIO-RK; P30759; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000186698; Genome assembly.
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 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 Arginine metabolism; Hydrolase; Manganese; Metal-binding;
KW Reference proteome; Urea cycle.
FT CHAIN 1..316
FT /note="Arginase-1"
FT /id="PRO_0000173698"
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"
SQ SEQUENCE 316 AA; 34566 MW; 8E6D08B20BF915ED CRC64;
MAKERHSVGV IGAPFSKGQP RRGVEEGPKY LREAGLIEKL REFGNDVRDC GDLDFPDVPN
DTPFNNVKNP RTVGKATEIL ANAVTAVKKA DKTCQSIGGD HSLAVGTIAG HAAVHPNLCV
VWVDAHADIN TPSTSPCGNL HGQPLSFLMK ELKAKMPAVP GFEWVKPCLR SKDIVYIGLR
DVDPGEHYIL KTLGIKYLSM IEVDYLKDDK VMEETLEYLV GKHKRPIHLS FDIDGLDPSI
APATGTPCPG GRTYREGRIL HEQLHKTGLL SGVDTIWMES TSRGETKRDV EVTVKTALDM
TLSCFGKARE GFHAST
