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Protein

Ribonuclease inhibitor

Gene

Rnh1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis.1 Publication

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease inhibitor
Alternative name(s):
Ribonuclease/angiogenin inhibitor 1
Gene namesi
Name:Rnh1
Synonyms:Rnh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621398. Rnh1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000973471 – 456Ribonuclease inhibitorAdd BLAST456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei86PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP29315.
PRIDEiP29315.

PTM databases

iPTMnetiP29315.
PhosphoSitePlusiP29315.

Expressioni

Tissue specificityi

Brain, heart, lung, liver, spleen, testes and kidney; highest in the lung and lowest in the heart.1 Publication

Interactioni

Subunit structurei

Forms high-affinity heterodimers with RNASE1, ANG and RNASE2.1 Publication

Protein-protein interaction databases

IntActiP29315. 1 interactor.
STRINGi10116.ENSRNOP00000022241.

Structurei

3D structure databases

ProteinModelPortaliP29315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati15 – 43LRR 1Add BLAST29
Repeati44 – 71LRR 2Add BLAST28
Repeati72 – 100LRR 3Add BLAST29
Repeati101 – 128LRR 4Add BLAST28
Repeati129 – 157LRR 5Add BLAST29
Repeati158 – 185LRR 6Add BLAST28
Repeati186 – 214LRR 7Add BLAST29
Repeati215 – 242LRR 8Add BLAST28
Repeati243 – 271LRR 9Add BLAST29
Repeati272 – 299LRR 10Add BLAST28
Repeati300 – 328LRR 11Add BLAST29
Repeati329 – 356LRR 12Add BLAST28
Repeati357 – 385LRR 13Add BLAST29
Repeati386 – 413LRR 14Add BLAST28
Repeati414 – 442LRR 15Add BLAST29

Domaini

The LRR domain forms a horseshoe-shaped structure that interacts tightly with target RNases via a large protein interaction surface on its interior side.By similarity

Sequence similaritiesi

Contains 15 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG4308. Eukaryota.
ENOG410ZBX3. LUCA.
HOGENOMiHOG000140402.
HOVERGENiHBG001059.
InParanoidiP29315.
KOiK16634.
PhylomeDBiP29315.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
PfamiPF13516. LRR_6. 7 hits.
[Graphical view]
PROSITEiPS51450. LRR. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29315-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLDIQCEQL SDARWTELLP LIQQYQVVRL DDCGLTEVRC KDIRSAIQAN
60 70 80 90 100
PALTELSLRT NELGDAGVGL VLQGLQNPTC KIQKLSLQNC SLTEAGCGVL
110 120 130 140 150
PDVLRSLSTL RELHLNDNPL GDEGLKLLCE GLRDPQCRLE KLQLEYCNLT
160 170 180 190 200
ATSCEPLASV LRVKPDFKEL VLSNNDFHEA GIHTLCQGLK DSACQLESLK
210 220 230 240 250
LENCGITSAN CKDLCDVVAS KASLQELDLG SNKLGNTGIA ALCSGLLLPS
260 270 280 290 300
CRLRTLWLWD CDVTAEGCKD LCRVLRAKQS LKELSLAGNE LKDEGAQLLC
310 320 330 340 350
ESLLEPGCQL ESLWVKTCSL TAASCPHFCS VLTKNRSLFE LQMSSNPLGD
360 370 380 390 400
SGVVELCKAL GYPDTVLRVL WLGDCDVTDS GCSSLATVLL ANRSLRELDL
410 420 430 440 450
SNNCMGDNGV LQLLESLKQP SCILQQLVLY DIYWTDEVED QLRALEEERP

SLRIIS
Length:456
Mass (Da):49,974
Last modified:October 11, 2005 - v2
Checksum:i85A8E4B1F09E5898
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti336R → S in CAA44388 (PubMed:1536887).Curated1
Sequence conflicti408N → T in AAH70501 (PubMed:15489334).Curated1
Sequence conflicti423I → A in AAH70501 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62528 mRNA. Translation: CAA44388.1.
BC070501 mRNA. Translation: AAH70501.1.
PIRiS20597.
RefSeqiNP_001257691.1. NM_001270762.1.
NP_001257692.1. NM_001270763.1.
NP_620805.2. NM_139105.3.
UniGeneiRn.3756.

Genome annotation databases

GeneIDi100360501.
KEGGirno:100360501.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62528 mRNA. Translation: CAA44388.1.
BC070501 mRNA. Translation: AAH70501.1.
PIRiS20597.
RefSeqiNP_001257691.1. NM_001270762.1.
NP_001257692.1. NM_001270763.1.
NP_620805.2. NM_139105.3.
UniGeneiRn.3756.

3D structure databases

ProteinModelPortaliP29315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP29315. 1 interactor.
STRINGi10116.ENSRNOP00000022241.

PTM databases

iPTMnetiP29315.
PhosphoSitePlusiP29315.

Proteomic databases

PaxDbiP29315.
PRIDEiP29315.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100360501.
KEGGirno:100360501.

Organism-specific databases

CTDi6050.
RGDi621398. Rnh1.

Phylogenomic databases

eggNOGiKOG4308. Eukaryota.
ENOG410ZBX3. LUCA.
HOGENOMiHOG000140402.
HOVERGENiHBG001059.
InParanoidiP29315.
KOiK16634.
PhylomeDBiP29315.

Miscellaneous databases

PROiP29315.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
PfamiPF13516. LRR_6. 7 hits.
[Graphical view]
PROSITEiPS51450. LRR. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRINI_RAT
AccessioniPrimary (citable) accession number: P29315
Secondary accession number(s): Q6IRS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 11, 2005
Last modified: November 2, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.