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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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Ribonuclease inhibitorPRO_0000097347Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei86 – 861PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP29315.
PRIDEiP29315.

PTM databases

iPTMnetiP29315.
PhosphoSiteiP29315.

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 interaction.
STRINGi10116.ENSRNOP00000022241.

Structurei

3D structure databases

ProteinModelPortaliP29315.
SMRiP29315. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati15 – 4329LRR 1Add
BLAST
Repeati44 – 7128LRR 2Add
BLAST
Repeati72 – 10029LRR 3Add
BLAST
Repeati101 – 12828LRR 4Add
BLAST
Repeati129 – 15729LRR 5Add
BLAST
Repeati158 – 18528LRR 6Add
BLAST
Repeati186 – 21429LRR 7Add
BLAST
Repeati215 – 24228LRR 8Add
BLAST
Repeati243 – 27129LRR 9Add
BLAST
Repeati272 – 29928LRR 10Add
BLAST
Repeati300 – 32829LRR 11Add
BLAST
Repeati329 – 35628LRR 12Add
BLAST
Repeati357 – 38529LRR 13Add
BLAST
Repeati386 – 41328LRR 14Add
BLAST
Repeati414 – 44229LRR 15Add
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti336 – 3361R → S in CAA44388 (PubMed:1536887).Curated
Sequence conflicti408 – 4081N → T in AAH70501 (PubMed:15489334).Curated
Sequence conflicti423 – 4231I → A in AAH70501 (PubMed:15489334).Curated

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.
XP_008758192.1. XM_008759970.1.
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.
XP_008758192.1. XM_008759970.1.
UniGeneiRn.3756.

3D structure databases

ProteinModelPortaliP29315.
SMRiP29315. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP29315. 1 interaction.
STRINGi10116.ENSRNOP00000022241.

PTM databases

iPTMnetiP29315.
PhosphoSiteiP29315.

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...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and sequence of rat ribonuclease inhibitor, and tissue distribution of the mRNA."
    Kawanomoto M., Motojima K., Sasaki M., Hattori H., Goto S.
    Biochim. Biophys. Acta 1129:335-338(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-64; 66-78; 169-190; 293-309 AND 335-349, FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
    Tissue: Lung.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.

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: June 8, 2016
This is version 114 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.