ARGN3_XENLA
ID ARGN3_XENLA Reviewed; 360 AA.
AC Q91555; Q52L42;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Arginase, non-hepatic 3;
DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
GN Name=arg2-c; Synonyms=arg3;
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=Intestine;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-360.
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: As well as its role in the urea cycle, may be involved in
CC tissue remodeling.
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}.
CC -!- TISSUE SPECIFICITY: Expressed at differing tadpole stages in tail,
CC intestine, hindlimb and trunk region. Strongest in tadpole tail.
CC -!- DEVELOPMENTAL STAGE: First detected in early tailbud (stage 23/24).
CC Highest levels in whole tadpole found around stage 47/48. In the
CC intestine, increased levels are found during metamorphosis (stages 58-
CC 64) and in the hindlimb, expressed at low levels during metamorphosis
CC until stage 66 when levels dramatically increase. In the tail, a
CC constant high level of expression is found throughout metamorphosis.
CC -!- INDUCTION: By thyroid hormone (T3).
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; U08408; AAA56893.1; -; mRNA.
DR EMBL; BC094076; AAH94076.1; -; mRNA.
DR PIR; I51665; I51665.
DR AlphaFoldDB; Q91555; -.
DR SMR; Q91555; -.
DR OMA; KFGIRYY; -.
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..360
FT /note="Arginase, non-hepatic 3"
FT /id="PRO_0000173701"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
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..151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 158..160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P05089"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
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 255
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P78540"
SQ SEQUENCE 360 AA; 39238 MW; F1515DED32514662 CRC64;
MSIRSNFVRL LKKQVNIIKL QKKCSHSVAV IGAPFSKGQK RRGVEHGPAA IRSAGLIDRL
SNLGCNVCDF GDLHFSQVPN DEQYNSIVKH PRTVGLACKV LAKEVGKAVG AGHTCVTLGG
DHSLAFGSIT GHAQQCPDLC VIWVDAHADI NTPLTTPSGN LHGQPVSFLL RELQDKIPPI
PGFSWAKPCL SKSDIVYIGL RDLDPAEQFI LKNYNISYYS MRHIDCMGIR KVMEKTFDQL
LGRRDRPIHL SFDIDAFDPA LAPATGTPVI GGLTYREGVY ITEEIHNTGM LSALDLVEVN
PVLATTSEEV KATANLAVDV IASCFGQTRE GAHTRADTII DVLPTPSTSY ESDNEEQVRI
