RIDA_HUMAN
ID RIDA_HUMAN Reviewed; 137 AA.
AC P52758; Q6FHU9; Q6IBG0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=2-iminobutanoate/2-iminopropanoate deaminase {ECO:0000305|PubMed:22094463};
DE EC=3.5.99.10 {ECO:0000269|PubMed:22094463};
DE AltName: Full=14.5 kDa translational inhibitor protein {ECO:0000303|PubMed:8973653};
DE Short=hp14.5 {ECO:0000303|PubMed:14997576};
DE Short=p14.5 {ECO:0000303|PubMed:8973653};
DE AltName: Full=Heat-responsive protein 12 {ECO:0000312|HGNC:HGNC:16897};
DE AltName: Full=Reactive intermediate imine deaminase A homolog {ECO:0000312|HGNC:HGNC:16897};
DE AltName: Full=Translation inhibitor L-PSP ribonuclease {ECO:0000250|UniProtKB:P52759};
DE AltName: Full=UK114 antigen homolog {ECO:0000305|PubMed:20817725};
GN Name=RIDA {ECO:0000312|HGNC:HGNC:16897};
GN Synonyms=HRSP12 {ECO:0000312|HGNC:HGNC:16897};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 14-28; 30-43; 68-78 AND
RP 98-113, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Liver;
RX PubMed=8973653; DOI=10.1111/j.1432-1033.1996.0339r.x;
RA Schmiedeknecht G., Kerkhoff C., Orso E., Stoehr J., Aslanidis C.,
RA Nagy G.M., Knuechel R., Schmitz G.;
RT "Isolation and characterization of a 14.5-kDa trichloroacetic-acid-soluble
RT translational inhibitor protein from human monocytes that is upregulated
RT upon cellular differentiation.";
RL Eur. J. Biochem. 242:339-351(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Pozdniakovaite N., Popendikyte V., Naktinis V.;
RT "Genomic structure of the human translational inhibitor protein p14.5.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Cervix, and Skin;
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 [6]
RP TISSUE SPECIFICITY.
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 [7]
RP FUNCTION.
RX PubMed=20817725; DOI=10.1074/jbc.m110.160515;
RA Lambrecht J.A., Browne B.A., Downs D.M.;
RT "Members of the YjgF/YER057c/UK114 family of proteins inhibit
RT phosphoribosylamine synthesis in vitro.";
RL J. Biol. Chem. 285:34401-34407(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22094463; DOI=10.1074/jbc.m111.304477;
RA Lambrecht J.A., Flynn J.M., Downs D.M.;
RT "The conserved YjgF protein family deaminates enamine/imine intermediates
RT of pyridoxal-5'-phosphate (PLP)-dependent enzyme reactions.";
RL J. Biol. Chem. 287:3454-3461(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74 AND SER-136, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP FUNCTION, AND INTERACTION WITH YTHDF2.
RX PubMed=30930054; DOI=10.1016/j.molcel.2019.02.034;
RA Park O.H., Ha H., Lee Y., Boo S.H., Kwon D.H., Song H.K., Kim Y.K.;
RT "Endoribonucleolytic cleavage of m6A-containing RNAs by RNase P/MRP
RT complex.";
RL Mol. Cell 74:494-507(2019).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT.
RX PubMed=14997576; DOI=10.1002/prot.10619;
RA Manjasetty B.A., Delbruck H., Pham D.-T., Mueller U., Fieber-Erdmann M.,
RA Scheich C., Sievert V., Buessow K., Neisen F.H., Weihofen W., Loll B.,
RA Saenger W., Heinemann U.;
RT "Crystal structure of Homo sapiens protein hp14.5.";
RL Proteins 54:797-800(2004).
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:0000269|PubMed:20817725, ECO:0000269|PubMed:22094463}.
CC -!- FUNCTION: Also promotes endoribonucleolytic cleavage of some
CC transcripts by promoting recruitment of the ribonuclease P/MRP complex
CC (PubMed:8973653, PubMed:30930054). Acts by bridging YTHDF2 and the
CC ribonuclease P/MRP complex (PubMed:30930054). RIDA/HRSP12 binds to N6-
CC methyladenosine (m6A)-containing mRNAs containing a 5'-GGUUC-3' motif:
CC cooperative binding of RIDA/HRSP12 and YTHDF2 to such transcripts lead
CC to recruitment of the ribonuclease P/MRP complex and subsequent
CC endoribonucleolytic cleavage (PubMed:30930054).
CC {ECO:0000269|PubMed:30930054, ECO:0000269|PubMed:8973653}.
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:0000269|PubMed:22094463};
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:0000269|PubMed:22094463};
CC -!- SUBUNIT: Homotrimer (PubMed:14997576). Interacts with YTHDF2
CC (PubMed:30930054). {ECO:0000269|PubMed:14997576,
CC ECO:0000269|PubMed:30930054}.
CC -!- INTERACTION:
CC P52758; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-1045080, EBI-11524452;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8973653}. Nucleus
CC {ECO:0000269|PubMed:8973653}. 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:0000269|PubMed:8973653}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in liver and kidney. Lower
CC levels in lung and brain. {ECO:0000269|PubMed:8973653,
CC ECO:0000269|PubMed:9141440}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during cellular differentiation.
CC {ECO:0000269|PubMed:8973653}.
CC -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
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DR EMBL; X95384; CAA64670.1; -; mRNA.
DR EMBL; AY026764; AAK01939.1; -; Genomic_DNA.
DR EMBL; CR456844; CAG33125.1; -; mRNA.
DR EMBL; CR541652; CAG46453.1; -; mRNA.
DR EMBL; CH471060; EAW91774.1; -; Genomic_DNA.
DR EMBL; BC010280; AAH10280.1; -; mRNA.
DR EMBL; BC012592; AAH12592.1; -; mRNA.
DR EMBL; BC093059; AAH93059.1; -; mRNA.
DR CCDS; CCDS6276.1; -.
DR RefSeq; NP_005827.1; NM_005836.2.
DR PDB; 1ONI; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I=2-137.
DR PDBsum; 1ONI; -.
DR AlphaFoldDB; P52758; -.
DR SMR; P52758; -.
DR BioGRID; 115541; 29.
DR IntAct; P52758; 16.
DR STRING; 9606.ENSP00000254878; -.
DR iPTMnet; P52758; -.
DR PhosphoSitePlus; P52758; -.
DR BioMuta; RIDA; -.
DR DMDM; 1717975; -.
DR UCD-2DPAGE; P52758; -.
DR CPTAC; CPTAC-387; -.
DR CPTAC; CPTAC-388; -.
DR EPD; P52758; -.
DR jPOST; P52758; -.
DR MassIVE; P52758; -.
DR PaxDb; P52758; -.
DR PeptideAtlas; P52758; -.
DR PRIDE; P52758; -.
DR ProteomicsDB; 56530; -.
DR TopDownProteomics; P52758; -.
DR Antibodypedia; 13021; 164 antibodies from 24 providers.
DR DNASU; 10247; -.
DR Ensembl; ENST00000254878.8; ENSP00000254878.3; ENSG00000132541.11.
DR GeneID; 10247; -.
DR KEGG; hsa:10247; -.
DR MANE-Select; ENST00000254878.8; ENSP00000254878.3; NM_005836.3; NP_005827.1.
DR UCSC; uc003yii.2; human.
DR CTD; 10247; -.
DR DisGeNET; 10247; -.
DR GeneCards; RIDA; -.
DR HGNC; HGNC:16897; RIDA.
DR HPA; ENSG00000132541; Group enriched (kidney, liver).
DR MIM; 602487; gene.
DR neXtProt; NX_P52758; -.
DR OpenTargets; ENSG00000132541; -.
DR PharmGKB; PA134890258; -.
DR VEuPathDB; HostDB:ENSG00000132541; -.
DR eggNOG; KOG2317; Eukaryota.
DR GeneTree; ENSGT00420000029792; -.
DR HOGENOM; CLU_100715_7_1_1; -.
DR InParanoid; P52758; -.
DR OMA; GSYFKEP; -.
DR OrthoDB; 1435276at2759; -.
DR PhylomeDB; P52758; -.
DR TreeFam; TF105775; -.
DR PathwayCommons; P52758; -.
DR Reactome; R-HSA-8849175; Threonine catabolism.
DR SignaLink; P52758; -.
DR BioGRID-ORCS; 10247; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; RIDA; human.
DR EvolutionaryTrace; P52758; -.
DR GeneWiki; Heat-responsive_protein_12; -.
DR GenomeRNAi; 10247; -.
DR Pharos; P52758; Tbio.
DR PRO; PR:P52758; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P52758; protein.
DR Bgee; ENSG00000132541; Expressed in right lobe of liver and 185 other tissues.
DR ExpressionAtlas; P52758; baseline and differential.
DR Genevisible; P52758; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0120242; F:2-iminobutanoate deaminase activity; IDA: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; IEA:Ensembl.
DR GO; GO:0036041; F:long-chain fatty acid binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0046914; F:transition metal ion binding; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0070314; P:G1 to G0 transition; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0019518; P:L-threonine catabolic process to glycine; TAS:Reactome.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0061157; P:mRNA destabilization; IDA:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:1901565; P:organonitrogen compound catabolic process; IDA:UniProtKB.
DR GO; GO:0033993; P:response to lipid; IEA:Ensembl.
DR GO; GO:1902074; P:response to salt; IEA:Ensembl.
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 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Lipid metabolism; Mitochondrion; Nucleus; Peroxisome; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..137
FT /note="2-iminobutanoate/2-iminopropanoate deaminase"
FT /id="PRO_0000170308"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 13
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52760"
FT MOD_RES 60
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52760"
FT MOD_RES 67
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52760"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CONFLICT 84
FT /note="A -> V (in Ref. 3; CAG46453)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1ONI"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1ONI"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:1ONI"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1ONI"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1ONI"
FT HELIX 51..68
FT /evidence="ECO:0007829|PDB:1ONI"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1ONI"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:1ONI"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1ONI"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:1ONI"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1ONI"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1ONI"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:1ONI"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1ONI"
SQ SEQUENCE 137 AA; 14494 MW; DD0740621E8BE6AD CRC64;
MSSLIRRVIS TAKAPGAIGP YSQAVLVDRT IYISGQIGMD PSSGQLVSGG VAEEAKQALK
NMGEILKAAG CDFTNVVKTT VLLADINDFN TVNEIYKQYF KSNFPARAAY QVAALPKGSR
IEIEAVAIQG PLTTASL
