ARGN2_XENLA
ID ARGN2_XENLA Reviewed; 360 AA.
AC Q91554;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Arginase, non-hepatic 2;
DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
GN Name=arg2-b; Synonyms=arg2;
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).
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 neurula (stage 16/17). Highest
CC levels in whole tadpole found around stage 47/48. In the intestine,
CC increased levels are found during metamorphosis (stages 58-64) and in
CC the hindlimb, expressed at low levels during metamorphosis until stage
CC 66 when levels dramatically increase. In the tail, a constant high
CC 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; U08407; AAA56892.1; -; mRNA.
DR PIR; I51664; I51664.
DR RefSeq; NP_001079511.1; NM_001086042.1.
DR AlphaFoldDB; Q91554; -.
DR SMR; Q91554; -.
DR DNASU; 379198; -.
DR GeneID; 379198; -.
DR KEGG; xla:379198; -.
DR CTD; 379198; -.
DR Xenbase; XB-GENE-6251613; arg2.S.
DR OrthoDB; 1179130at2759; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 379198; Expressed in muscle tissue and 14 other tissues.
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 2"
FT /id="PRO_0000173700"
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; 39155 MW; 44A4E61915DD0833 CRC64;
MSIRSNFVRL LKKQVSIIKL QKKCSHSVAV IGAPFSKGQK RRGVEHGPAA IRSAGLIERL
SNLGCNVCDF GDLHFSKVPN DELYNSIVKH PRTVGLACKV LAEEVSKAVG AGHTCVTLGG
DHSLAFGSIT GHAQQCPDLC VIWVDAHADI NTPLTTPSGN LHGQPVSFLL RELQDKVPPI
PGFSWAKPCL SKSDIVYIGL RDLDPAEQFI LKNYNISYYS MRHIDCMGIK KVMEKTFDQL
LGRRDRPIHL SFDIDAFDPA LAPATGTPVI GGLTYREGVY ITEEIHNTGM LSAVDLVEVN
PVLAATSEEV KATANLAVDV IASCFGQTRE GAHTRADTII DVLPTPSTSY ESDNEEQVRI
