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Protein

Ribonuclease inhibitor

Gene

Rnh1

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease inhibitor
Alternative name(s):
Ribonuclease/angiogenin inhibitor 1
Gene namesi
Name:Rnh1
Synonyms:Rnh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1195456. 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_0000097344Add
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

EPDiQ91VI7.
MaxQBiQ91VI7.
PaxDbiQ91VI7.
PRIDEiQ91VI7.

2D gel databases

UCD-2DPAGEQ91VI7.

PTM databases

iPTMnetiQ91VI7.
PhosphoSiteiQ91VI7.
SwissPalmiQ91VI7.

Expressioni

Gene expression databases

BgeeiQ91VI7.
CleanExiMM_RNH1.
GenevisibleiQ91VI7. MM.

Interactioni

Subunit structurei

Forms high-affinity heterodimers with RNASE1, ANG and RNASE2.By similarity

Protein-protein interaction databases

BioGridi223500. 5 interactions.
IntActiQ91VI7. 3 interactions.
MINTiMINT-1868853.
STRINGi10090.ENSMUSP00000101651.

Structurei

Secondary structure

456
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 77Combined sources
Helixi12 – 2211Combined sources
Beta strandi26 – 338Combined sources
Helixi37 – 393Combined sources
Helixi40 – 489Combined sources
Beta strandi55 – 573Combined sources
Helixi64 – 7411Combined sources
Beta strandi84 – 863Combined sources
Helixi94 – 996Combined sources
Helixi100 – 1067Combined sources
Beta strandi112 – 1143Combined sources
Helixi121 – 13212Combined sources
Beta strandi140 – 1434Combined sources
Helixi151 – 1533Combined sources
Helixi154 – 16310Combined sources
Beta strandi169 – 1713Combined sources
Helixi178 – 19114Combined sources
Beta strandi198 – 2003Combined sources
Helixi208 – 2103Combined sources
Helixi211 – 22010Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi231 – 2333Combined sources
Helixi235 – 24612Combined sources
Beta strandi255 – 2573Combined sources
Helixi265 – 27713Combined sources
Beta strandi283 – 2853Combined sources
Helixi292 – 30312Combined sources
Beta strandi312 – 3143Combined sources
Helixi322 – 3243Combined sources
Helixi325 – 33410Combined sources
Beta strandi340 – 3423Combined sources
Helixi349 – 36012Combined sources
Beta strandi369 – 3713Combined sources
Helixi379 – 3813Combined sources
Helixi382 – 39110Combined sources
Beta strandi397 – 3993Combined sources
Helixi407 – 41711Combined sources
Beta strandi426 – 4283Combined sources
Helixi436 – 44813Combined sources
Beta strandi453 – 4553Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TSRX-ray2.20E/F/G/H1-456[»]
ProteinModelPortaliQ91VI7.
SMRiQ91VI7. 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.
GeneTreeiENSGT00840000129796.
HOGENOMiHOG000140402.
HOVERGENiHBG001059.
InParanoidiQ91VI7.
KOiK16634.
OMAiCRDLCSI.
OrthoDBiEOG7P5T07.
PhylomeDBiQ91VI7.

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]

Sequencei

Sequence statusi: Complete.

Q91VI7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLDIQCEQL SDARWTELLP LIQQYEVVRL DDCGLTEVRC KDISSAVQAN
60 70 80 90 100
PALTELSLRT NELGDGGVGL VLQGLQNPTC KIQKLSLQNC GLTEAGCGIL
110 120 130 140 150
PGMLRSLSTL RELHLNDNPM GDAGLKLLCE GLQDPQCRLE KLQLEYCNLT
160 170 180 190 200
ATSCEPLASV LRVKADFKEL VLSNNDLHEP GVRILCQGLK DSACQLESLK
210 220 230 240 250
LENCGITAAN CKDLCDVVAS KASLQELDLS SNKLGNAGIA ALCPGLLLPS
260 270 280 290 300
CKLRTLWLWE CDITAEGCKD LCRVLRAKQS LKELSLASNE LKDEGARLLC
310 320 330 340 350
ESLLEPGCQL ESLWIKTCSL TAASCPYFCS VLTKSRSLLE LQMSSNPLGD
360 370 380 390 400
EGVQELCKAL SQPDTVLREL WLGDCDVTNS GCSSLANVLL ANRSLRELDL
410 420 430 440 450
SNNCMGGPGV LQLLESLKQP SCTLQQLVLY DIYWTNEVEE QLRALEEERP

SLRIIS
Length:456
Mass (Da):49,816
Last modified:December 1, 2001 - v1
Checksum:i007B782F05A357E8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111S → G in AAK68859 (Ref. 1) Curated
Sequence conflicti68 – 681V → A in AAK68859 (Ref. 1) Curated
Sequence conflicti254 – 2541R → G in AAK68859 (Ref. 1) Curated
Sequence conflicti278 – 2781K → N in AAK68859 (Ref. 1) Curated
Sequence conflicti448 – 4481E → G in AAK68859 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071546 mRNA. Translation: AAK68859.1.
AK133822 mRNA. Translation: BAE21862.1.
AK141351 mRNA. Translation: BAE24659.1.
AK147059 mRNA. Translation: BAE27643.1.
BC010331 mRNA. Translation: AAH10331.1.
CCDSiCCDS22002.1.
RefSeqiNP_001165571.1. NM_001172100.1.
NP_001165572.1. NM_001172101.1.
NP_660117.2. NM_145135.3.
UniGeneiMm.197493.
Mm.279485.

Genome annotation databases

EnsembliENSMUST00000106033; ENSMUSP00000101651; ENSMUSG00000038650.
ENSMUST00000167493; ENSMUSP00000133061; ENSMUSG00000038650.
GeneIDi107702.
KEGGimmu:107702.
UCSCiuc009kjs.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071546 mRNA. Translation: AAK68859.1.
AK133822 mRNA. Translation: BAE21862.1.
AK141351 mRNA. Translation: BAE24659.1.
AK147059 mRNA. Translation: BAE27643.1.
BC010331 mRNA. Translation: AAH10331.1.
CCDSiCCDS22002.1.
RefSeqiNP_001165571.1. NM_001172100.1.
NP_001165572.1. NM_001172101.1.
NP_660117.2. NM_145135.3.
UniGeneiMm.197493.
Mm.279485.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TSRX-ray2.20E/F/G/H1-456[»]
ProteinModelPortaliQ91VI7.
SMRiQ91VI7. Positions 1-456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223500. 5 interactions.
IntActiQ91VI7. 3 interactions.
MINTiMINT-1868853.
STRINGi10090.ENSMUSP00000101651.

PTM databases

iPTMnetiQ91VI7.
PhosphoSiteiQ91VI7.
SwissPalmiQ91VI7.

2D gel databases

UCD-2DPAGEQ91VI7.

Proteomic databases

EPDiQ91VI7.
MaxQBiQ91VI7.
PaxDbiQ91VI7.
PRIDEiQ91VI7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000106033; ENSMUSP00000101651; ENSMUSG00000038650.
ENSMUST00000167493; ENSMUSP00000133061; ENSMUSG00000038650.
GeneIDi107702.
KEGGimmu:107702.
UCSCiuc009kjs.2. mouse.

Organism-specific databases

CTDi6050.
MGIiMGI:1195456. Rnh1.

Phylogenomic databases

eggNOGiKOG4308. Eukaryota.
ENOG410ZBX3. LUCA.
GeneTreeiENSGT00840000129796.
HOGENOMiHOG000140402.
HOVERGENiHBG001059.
InParanoidiQ91VI7.
KOiK16634.
OMAiCRDLCSI.
OrthoDBiEOG7P5T07.
PhylomeDBiQ91VI7.

Miscellaneous databases

ChiTaRSiRnh1. mouse.
NextBioi359282.
PROiQ91VI7.
SOURCEiSearch...

Gene expression databases

BgeeiQ91VI7.
CleanExiMM_RNH1.
GenevisibleiQ91VI7. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse homolog of ribonuclease/angiogenesis inhibitor."
    Melnick M.B., Comb M.J.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  3. "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].
    Strain: NMRI.
    Tissue: Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRINI_MOUSE
AccessioniPrimary (citable) accession number: Q91VI7
Secondary accession number(s): Q924P4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.