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Protein

Ribonuclease inhibitor

Gene

RNH1

Organism
Sus scrofa (Pig)
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:RI, RNH
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000973461 – 456Ribonuclease inhibitorAdd BLAST456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei86PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PeptideAtlasiP10775.
PRIDEiP10775.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP10775. 1 interactor.
MINTiMINT-1510428.

Structurei

Secondary structure

1456
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 7Combined sources3
Helixi12 – 22Combined sources11
Beta strandi26 – 31Combined sources6
Helixi37 – 47Combined sources11
Beta strandi55 – 57Combined sources3
Helixi64 – 75Combined sources12
Beta strandi84 – 86Combined sources3
Helixi94 – 98Combined sources5
Helixi100 – 106Combined sources7
Beta strandi112 – 114Combined sources3
Helixi121 – 133Combined sources13
Beta strandi141 – 143Combined sources3
Helixi151 – 163Combined sources13
Beta strandi169 – 171Combined sources3
Helixi178 – 190Combined sources13
Beta strandi198 – 200Combined sources3
Helixi208 – 220Combined sources13
Beta strandi226 – 228Combined sources3
Helixi235 – 246Combined sources12
Beta strandi255 – 257Combined sources3
Helixi265 – 277Combined sources13
Beta strandi283 – 285Combined sources3
Helixi292 – 303Combined sources12
Beta strandi312 – 314Combined sources3
Helixi322 – 324Combined sources3
Helixi325 – 334Combined sources10
Beta strandi340 – 342Combined sources3
Beta strandi345 – 347Combined sources3
Helixi349 – 359Combined sources11
Beta strandi362 – 364Combined sources3
Beta strandi369 – 371Combined sources3
Helixi379 – 391Combined sources13
Beta strandi397 – 399Combined sources3
Beta strandi402 – 404Combined sources3
Helixi407 – 417Combined sources11
Beta strandi419 – 421Combined sources3
Beta strandi426 – 428Combined sources3
Helixi436 – 448Combined sources13
Beta strandi453 – 455Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DFJX-ray2.50I1-456[»]
2BNHX-ray2.30A1-456[»]
ProteinModelPortaliP10775.
SMRiP10775.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10775.

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

HOVERGENiHBG001059.
InParanoidiP10775.
KOiK16634.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
[Graphical view]
PfamiPF13516. LRR_6. 8 hits.
[Graphical view]
SMARTiSM00367. LRR_CC. 6 hits.
[Graphical view]
PROSITEiPS51450. LRR. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10775-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLDIHCEQL SDARWTELLP LLQQYEVVRL DDCGLTEEHC KDIGSALRAN
60 70 80 90 100
PSLTELCLRT NELGDAGVHL VLQGLQSPTC KIQKLSLQNC SLTEAGCGVL
110 120 130 140 150
PSTLRSLPTL RELHLSDNPL GDAGLRLLCE GLLDPQCHLE KLQLEYCRLT
160 170 180 190 200
AASCEPLASV LRATRALKEL TVSNNDIGEA GARVLGQGLA DSACQLETLR
210 220 230 240 250
LENCGLTPAN CKDLCGIVAS QASLRELDLG SNGLGDAGIA ELCPGLLSPA
260 270 280 290 300
SRLKTLWLWE CDITASGCRD LCRVLQAKET LKELSLAGNK LGDEGARLLC
310 320 330 340 350
ESLLQPGCQL ESLWVKSCSL TAACCQHVSL MLTQNKHLLE LQLSSNKLGD
360 370 380 390 400
SGIQELCQAL SQPGTTLRVL CLGDCEVTNS GCSSLASLLL ANRSLRELDL
410 420 430 440 450
SNNCVGDPGV LQLLGSLEQP GCALEQLVLY DTYWTEEVED RLQALEGSKP

GLRVIS
Length:456
Mass (Da):49,023
Last modified:July 1, 1989 - v1
Checksum:i01DA0A529CDC763E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58700 mRNA. Translation: AAA63448.1.
PIRiA31857.
RefSeqiXP_013847653.1. XM_013992199.1.
UniGeneiSsc.6413.

Genome annotation databases

GeneIDi445517.
KEGGissc:445517.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58700 mRNA. Translation: AAA63448.1.
PIRiA31857.
RefSeqiXP_013847653.1. XM_013992199.1.
UniGeneiSsc.6413.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DFJX-ray2.50I1-456[»]
2BNHX-ray2.30A1-456[»]
ProteinModelPortaliP10775.
SMRiP10775.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP10775. 1 interactor.
MINTiMINT-1510428.

Proteomic databases

PeptideAtlasiP10775.
PRIDEiP10775.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi445517.
KEGGissc:445517.

Organism-specific databases

CTDi6050.

Phylogenomic databases

HOVERGENiHBG001059.
InParanoidiP10775.
KOiK16634.

Miscellaneous databases

EvolutionaryTraceiP10775.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR006553. Leu-rich_rpt_Cys-con_subtyp.
[Graphical view]
PfamiPF13516. LRR_6. 8 hits.
[Graphical view]
SMARTiSM00367. LRR_CC. 6 hits.
[Graphical view]
PROSITEiPS51450. LRR. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRINI_PIG
AccessioniPrimary (citable) accession number: P10775
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 113 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.