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Protein

2-iminobutanoate/2-iminopropanoate deaminase

Gene

Rida

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase.By similarity
May also function as an endoribonuclease, cleaving mRNA phosphodiester bonds of single-stranded RNA (By similarity). Thereby, may inhibit protein translation (By similarity).By similarity

Catalytic activityi

2-iminobutanoate + H2O = 2-oxobutanoate + NH3.By similarity
2-iminopropanoate + H2O = pyruvate + NH3.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
2-iminobutanoate/2-iminopropanoate deaminaseBy similarity (EC:3.5.99.10By similarity)
Alternative name(s):
Heat-responsive protein 121 Publication
Reactive intermediate imine deaminase A homologImported
Translation inhibitor L-PSP ribonucleaseBy similarity (EC:3.1.-.-By similarity)
Gene namesi
Name:RidaImported
Synonyms:Hrp121 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1095401. Rida.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001703092 – 1352-iminobutanoate/2-iminopropanoate deaminaseAdd BLAST134

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei13N6-succinyllysineCombined sources1
Modified residuei60N6-succinyllysineCombined sources1
Modified residuei67N6-succinyllysineCombined sources1
Modified residuei134N6-succinyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP52760.
MaxQBiP52760.
PaxDbiP52760.
PeptideAtlasiP52760.
PRIDEiP52760.
TopDownProteomicsiP52760.

2D gel databases

SWISS-2DPAGEiP52760.

PTM databases

iPTMnetiP52760.
PhosphoSitePlusiP52760.

Expressioni

Tissue specificityi

Expressed predominantly in liver and kidney. Lower levels in lung and brain.1 Publication

Gene expression databases

BgeeiENSMUSG00000022323.
CleanExiMM_HRSP12.
GenevisibleiP52760. MM.

Interactioni

Subunit structurei

Homotrimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP52760. 6 interactors.
MINTiMINT-1869903.
STRINGi10090.ENSMUSP00000022946.

Structurei

3D structure databases

ProteinModelPortaliP52760.
SMRiP52760.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RutC family.Curated

Phylogenomic databases

eggNOGiKOG2317. Eukaryota.
COG0251. LUCA.
GeneTreeiENSGT00420000029792.
HOGENOMiHOG000267215.
HOVERGENiHBG003597.
InParanoidiP52760.
OMAiGSYFKEP.
OrthoDBiEOG091G0VJN.
PhylomeDBiP52760.
TreeFamiTF105775.

Family and domain databases

Gene3Di3.30.1330.40. 1 hit.
InterProiView protein in InterPro
IPR013813. Endoribo_LPSP/chorism_mut-like.
IPR006056. RidA.
IPR019897. RidA_CS.
IPR006175. YjgF/YER057c/UK114.
PANTHERiPTHR11803. PTHR11803. 1 hit.
PfamiView protein in Pfam
PF01042. Ribonuc_L-PSP. 1 hit.
SUPFAMiSSF55298. SSF55298. 1 hit.
TIGRFAMsiTIGR00004. TIGR00004. 1 hit.
PROSITEiView protein in PROSITE
PS01094. UPF0076. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52760-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSIIRKVIS TTKAPAAIGP YSQAVQVDRT IYISGQVGLD PSSGQLVPGG
60 70 80 90 100
VVEEAKQALK NLGEILKAAG CDFNNVVKTT VLLADMNDFG TVNEIYKTYF
110 120 130
QGSLPARAAY QVAALPRGSR VEIEAIAVQG PFIKA
Length:135
Mass (Da):14,255
Last modified:January 23, 2007 - v3
Checksum:iDDECBFD7E03D7E25
GO

Sequence cautioni

The sequence AAA96033 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50631 mRNA. Translation: AAA96033.1. Different initiation.
BC092375 mRNA. Translation: AAH92375.1.
BC125590 mRNA. Translation: AAI25591.1.
BC125592 mRNA. Translation: AAI25593.1.
CCDSiCCDS27418.1.
RefSeqiNP_032313.2. NM_008287.3.
UniGeneiMm.491154.

Genome annotation databases

EnsembliENSMUST00000022946; ENSMUSP00000022946; ENSMUSG00000022323.
GeneIDi15473.
KEGGimmu:15473.
UCSCiuc007vlt.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiRIDA_MOUSE
AccessioniPrimary (citable) accession number: P52760
Secondary accession number(s): Q569N4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 125 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families