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P10775 (RINI_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease inhibitor
Alternative name(s):
Ribonuclease/angiogenin inhibitor 1
Gene names
Name:RNH1
Synonyms:RI, RNH
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play role in redox homeostasis. Ref.2

Subunit structure

Forms high-affinity heterodimers with RNASE1, ANG and RNASE2. Ref.2

Subcellular location

Cytoplasm.

Domain

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 similarities

Contains 15 LRR (leucine-rich) repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainLeucine-rich repeat
Repeat
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Ribonuclease inhibitor
PRO_0000097346

Regions

Repeat15 – 4329LRR 1
Repeat44 – 7128LRR 2
Repeat72 – 10029LRR 3
Repeat101 – 12828LRR 4
Repeat129 – 15729LRR 5
Repeat158 – 18528LRR 6
Repeat186 – 21429LRR 7
Repeat215 – 24228LRR 8
Repeat243 – 27129LRR 9
Repeat272 – 29928LRR 10
Repeat300 – 32829LRR 11
Repeat329 – 35628LRR 12
Repeat357 – 38529LRR 13
Repeat386 – 41328LRR 14
Repeat414 – 44229LRR 15

Amino acid modifications

Modified residue11N-acetylmethionine
Modified residue861Phosphoserine By similarity

Secondary structure

............................................................................ 456
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10775 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 01DA0A529CDC763E

FASTA45649,023
        10         20         30         40         50         60 
MNLDIHCEQL SDARWTELLP LLQQYEVVRL DDCGLTEEHC KDIGSALRAN PSLTELCLRT 

        70         80         90        100        110        120 
NELGDAGVHL VLQGLQSPTC KIQKLSLQNC SLTEAGCGVL PSTLRSLPTL RELHLSDNPL 

       130        140        150        160        170        180 
GDAGLRLLCE GLLDPQCHLE KLQLEYCRLT AASCEPLASV LRATRALKEL TVSNNDIGEA 

       190        200        210        220        230        240 
GARVLGQGLA DSACQLETLR LENCGLTPAN CKDLCGIVAS QASLRELDLG SNGLGDAGIA 

       250        260        270        280        290        300 
ELCPGLLSPA SRLKTLWLWE CDITASGCRD LCRVLQAKET LKELSLAGNK LGDEGARLLC 

       310        320        330        340        350        360 
ESLLQPGCQL ESLWVKSCSL TAACCQHVSL MLTQNKHLLE LQLSSNKLGD SGIQELCQAL 

       370        380        390        400        410        420 
SQPGTTLRVL CLGDCEVTNS GCSSLASLLL ANRSLRELDL SNNCVGDPGV LQLLGSLEQP 

       430        440        450 
GCALEQLVLY DTYWTEEVED RLQALEGSKP GLRVIS 

« Hide

References

[1]"Amino acid sequence of the ribonuclease inhibitor from porcine liver reveals the presence of leucine-rich repeats."
Hofsteenge J., Kieffer B., Matthies R., Hemmings B.A., Stone S.R.
Biochemistry 27:8537-8544(1988) [PubMed: 3219361] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Protein chemical and kinetic characterization of recombinant porcine ribonuclease inhibitor expressed in Saccharomyces cerevisiae."
Vicentini A.M., Kieffer B., Matthies R., Meyhack B., Hemmings B.A., Stone S.R., Hofsteenge J.
Biochemistry 29:8827-8834(1990) [PubMed: 2271559] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 82-456, FUNCTION, SUBUNIT.
Tissue: Kidney.
[3]"Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats."
Kobe B., Deisenhofer J.
Nature 366:751-756(1993) [PubMed: 8264799] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[4]"A structural basis of the interactions between leucine-rich repeats and protein ligands."
Kobe B., Deisenhofer J.
Nature 374:183-186(1995) [PubMed: 7877692] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58700 mRNA. Translation: AAA63448.1.
PIRA31857.
UniGeneSsc.6413.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DFJX-ray2.50I1-456[»]
2BNHX-ray2.30A1-456[»]
ProteinModelPortalP10775.
SMRP10775. Positions 1-456.
ModBaseSearch...

Protein-protein interaction databases

IntActP10775. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG001059.

Family and domain databases

InterProIPR001611. Leu-rich_rpt.
IPR003590. Leu-rich_rpt_RNase_inh_sub-typ.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
[Graphical view]
SMARTSM00368. LRR_RI. 2 hits.
[Graphical view]
PROSITEPS51450. LRR. 6 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRINI_PIG
AccessionPrimary (citable) accession number: P10775
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 21, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families