RIDA_MOUSE
ID RIDA_MOUSE Reviewed; 135 AA.
AC P52760; Q569N4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=2-iminobutanoate/2-iminopropanoate deaminase {ECO:0000250|UniProtKB:P52758};
DE EC=3.5.99.10 {ECO:0000250|UniProtKB:P52758};
DE AltName: Full=Heat-responsive protein 12 {ECO:0000303|PubMed:9141440};
DE AltName: Full=Reactive intermediate imine deaminase A homolog {ECO:0000312|MGI:MGI:1095401};
DE AltName: Full=Translation inhibitor L-PSP ribonuclease {ECO:0000250|UniProtKB:P52759};
GN Name=Rida {ECO:0000312|MGI:MGI:1095401};
GN Synonyms=Hrp12 {ECO:0000303|PubMed:9141440};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=9141440; DOI=10.1002/hep.510250525;
RA Samuel S.J., Tzung S.P., Cohen S.A.;
RT "Hrp12, a novel heat-responsive, tissue-specific, phosphorylated protein
RT isolated from mouse liver.";
RL Hepatology 25:1213-1222(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-60; LYS-67 AND LYS-134,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of enamine/imine
CC intermediates that form during the course of normal metabolism. May
CC facilitate the release of ammonia from these potentially toxic reactive
CC metabolites, reducing their impact on cellular components. It may act
CC on enamine/imine intermediates formed by several types of pyridoxal-5'-
CC phosphate-dependent dehydratases including L-threonine dehydratase.
CC {ECO:0000250|UniProtKB:P52758}.
CC -!- FUNCTION: Also promotes endoribonucleolytic cleavage of some
CC transcripts by promoting recruitment of the ribonuclease P/MRP complex.
CC Acts by bridging YTHDF2 and the ribonuclease P/MRP complex. RIDA/HRSP12
CC binds to N6-methyladenosine (m6A)-containing mRNAs containing a 5'-
CC GGUUC-3' motif: cooperative binding of RIDA/HRSP12 and YTHDF2 to such
CC transcripts lead to recruitment of the ribonuclease P/MRP complex and
CC subsequent endoribonucleolytic cleavage.
CC {ECO:0000250|UniProtKB:P52758}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-iminobutanoate + H2O = 2-oxobutanoate + NH4(+);
CC Xref=Rhea:RHEA:39975, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:76545; EC=3.5.99.10;
CC Evidence={ECO:0000250|UniProtKB:P52758};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-iminopropanoate + H2O = NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:40671, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:44400; EC=3.5.99.10;
CC Evidence={ECO:0000250|UniProtKB:P52758};
CC -!- SUBUNIT: Homotrimer. Interacts with YTHDF2.
CC {ECO:0000250|UniProtKB:P52758}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52758}. Nucleus
CC {ECO:0000250|UniProtKB:P52758}. Peroxisome
CC {ECO:0000250|UniProtKB:P52759}. Mitochondrion
CC {ECO:0000250|UniProtKB:P52759}. Note=Mostly cytoplasmic but, in less
CC differentiated cells occasionally nuclear.
CC {ECO:0000250|UniProtKB:P52758}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in liver and kidney. Lower
CC levels in lung and brain. {ECO:0000269|PubMed:9141440}.
CC -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA96033.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U50631; AAA96033.1; ALT_INIT; mRNA.
DR EMBL; BC092375; AAH92375.1; -; mRNA.
DR EMBL; BC125590; AAI25591.1; -; mRNA.
DR EMBL; BC125592; AAI25593.1; -; mRNA.
DR CCDS; CCDS27418.1; -.
DR RefSeq; NP_032313.2; NM_008287.3.
DR AlphaFoldDB; P52760; -.
DR SMR; P52760; -.
DR IntAct; P52760; 2.
DR MINT; P52760; -.
DR STRING; 10090.ENSMUSP00000022946; -.
DR iPTMnet; P52760; -.
DR PhosphoSitePlus; P52760; -.
DR SwissPalm; P52760; -.
DR SWISS-2DPAGE; P52760; -.
DR CPTAC; non-CPTAC-3491; -.
DR EPD; P52760; -.
DR jPOST; P52760; -.
DR MaxQB; P52760; -.
DR PaxDb; P52760; -.
DR PeptideAtlas; P52760; -.
DR PRIDE; P52760; -.
DR ProteomicsDB; 253241; -.
DR TopDownProteomics; P52760; -.
DR Antibodypedia; 13021; 164 antibodies from 24 providers.
DR DNASU; 15473; -.
DR Ensembl; ENSMUST00000022946; ENSMUSP00000022946; ENSMUSG00000022323.
DR GeneID; 15473; -.
DR KEGG; mmu:15473; -.
DR UCSC; uc007vlt.2; mouse.
DR CTD; 10247; -.
DR MGI; MGI:1095401; Rida.
DR VEuPathDB; HostDB:ENSMUSG00000022323; -.
DR eggNOG; KOG2317; Eukaryota.
DR GeneTree; ENSGT00420000029792; -.
DR HOGENOM; CLU_100715_7_1_1; -.
DR InParanoid; P52760; -.
DR OMA; GSYFKEP; -.
DR OrthoDB; 1435276at2759; -.
DR PhylomeDB; P52760; -.
DR TreeFam; TF105775; -.
DR Reactome; R-MMU-8849175; Threonine catabolism.
DR BioGRID-ORCS; 15473; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rida; mouse.
DR PRO; PR:P52760; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P52760; protein.
DR Bgee; ENSMUSG00000022323; Expressed in right kidney and 261 other tissues.
DR Genevisible; P52760; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0120242; F:2-iminobutanoate deaminase activity; ISS:UniProtKB.
DR GO; GO:0120243; F:2-iminopropanoate deaminase activity; IEA:RHEA.
DR GO; GO:0019239; F:deaminase activity; IBA:GO_Central.
DR GO; GO:0016892; F:endoribonuclease activity, producing 3'-phosphomonoesters; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043167; F:ion binding; ISO:MGI.
DR GO; GO:0036041; F:long-chain fatty acid binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0046914; F:transition metal ion binding; ISO:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0061157; P:mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:1901565; P:organonitrogen compound catabolic process; ISS:UniProtKB.
DR Gene3D; 3.30.1330.40; -; 1.
DR InterPro; IPR006056; RidA.
DR InterPro; IPR019897; RidA_CS.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR006175; YjgF/YER057c/UK114.
DR PANTHER; PTHR11803; PTHR11803; 1.
DR Pfam; PF01042; Ribonuc_L-PSP; 1.
DR SUPFAM; SSF55298; SSF55298; 1.
DR TIGRFAMs; TIGR00004; TIGR00004; 1.
DR PROSITE; PS01094; UPF0076; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Lipid metabolism; Mitochondrion;
KW Nucleus; Peroxisome; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P80601"
FT CHAIN 2..135
FT /note="2-iminobutanoate/2-iminopropanoate deaminase"
FT /id="PRO_0000170309"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P80601"
FT MOD_RES 13
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 60
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 67
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 134
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 135 AA; 14255 MW; DDECBFD7E03D7E25 CRC64;
MSSIIRKVIS TTKAPAAIGP YSQAVQVDRT IYISGQVGLD PSSGQLVPGG VVEEAKQALK
NLGEILKAAG CDFNNVVKTT VLLADMNDFG TVNEIYKTYF QGSLPARAAY QVAALPRGSR
VEIEAIAVQG PFIKA
