Q92834 · RPGR_HUMAN

  • Protein
    X-linked retinitis pigmentosa GTPase regulator
  • Gene
    RPGR
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Could be a guanine-nucleotide releasing factor. Plays a role in ciliogenesis. Probably regulates cilia formation by regulating actin stress filaments and cell contractility. Plays an important role in photoreceptor integrity. May play a critical role in spermatogenesis and in intraflagellar transport processes (By similarity).
May be involved in microtubule organization and regulation of transport in primary cilia

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcentrosome
Cellular Componentciliary basal body
Cellular Componentcytoplasm
Cellular ComponentGolgi apparatus
Cellular Componentphotoreceptor outer segment
Cellular Componentsperm flagellum
Molecular Functionguanyl-nucleotide exchange factor activity
Molecular FunctionRNA binding
Molecular Functionubiquitin protein ligase activity
Biological Processcilium assembly
Biological Processintracellular protein transport
Biological Processintraciliary transport
Biological Processprotein ubiquitination
Biological Processubiquitin-dependent protein catabolic process
Biological Processvisual perception

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    X-linked retinitis pigmentosa GTPase regulator

Gene names

    • Name
      RPGR
    • Synonyms
      RP3, XLRP3

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q92834
  • Secondary accessions
    • B1ARN3
    • E9PE28
    • O00702
    • O00737
    • Q3KN84

Proteomes

Organism-specific databases

Subcellular Location

Golgi apparatus
Note: In the retinal photoreceptor cell layer, localizes at the connecting cilium (By similarity).
Colocalizes with WHRN in the photoreceptor connecting cilium (By similarity).
Colocalizes with CEP290 in the photoreceptor connecting cilium (By similarity).
Colocalizes with RPGRIP1 in the photoreceptor connecting cilium (By similarity).

Isoform 6

Keywords

Disease & Variants

Involvement in disease

Retinitis pigmentosa 3 (RP3)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An X-linked retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. In RP3, affected males have a severe phenotype, and carrier females show a wide spectrum of clinical features ranging from completely asymptomatic to severe retinitis pigmentosa. Heterozygous women can manifest a form of choroidoretinal degeneration which is distinguished from other types by the absence of visual defects in the presence of a brilliant, scintillating, golden-hued, patchy appearance most striking around the macula, called a tapetal-like retinal reflex.
  • See also
    MIM:300029
Natural variants in RP3
Variant IDPosition(s)ChangeDescription
VAR_01805743G>Ein RP3; dbSNP:rs62638630
VAR_01805843G>Rin RP3; dbSNP:rs62638629
VAR_00850160G>Vin RP3; dbSNP:rs62638634
VAR_00850375I>Vin RP3; benign; dbSNP:rs111631988
VAR_00850498H>Qin RP3; reduces interaction with PDE6D; dbSNP:rs62638636
VAR_01362599T>Nin RP3; dbSNP:rs62638637
VAR_018059127R>Gin RP3; dbSNP:rs62638643
VAR_006850130F>Cin RP3; reduces interaction with PDE6D; dbSNP:rs62638644
VAR_025949152S>Lin RP3
VAR_018060173G>Rin RP3 and RPSRDF; dbSNP:rs137852550
VAR_008505215G>Vin RP3; reduces interaction with PDE6D; dbSNP:rs62650218
VAR_006851235P>Sin RP3; reduces interaction with PDE6D; dbSNP:rs62638651
VAR_008506250C>Rin RP3; reduces interaction with PDE6D; dbSNP:rs62650220
VAR_018061250C>Yin RP3; dbSNP:rs1601961064
VAR_018062258missingin RP3
VAR_008507262A>Gin RP3; uncertain significance; dbSNP:rs138018739
VAR_018063267G>Ein RP3
VAR_026127267G>Rin RP3; dbSNP:rs2147248035
VAR_006852275G>Sin RP3; reduces interaction with PDE6D; dbSNP:rs62642057
VAR_026128285E>Gin RP3
VAR_013626289I>Vin RP3; dbSNP:rs62640587
VAR_013627296-300missingin RP3
VAR_011561302C>Rin RP3; dbSNP:rs62640589
VAR_018064302C>Yin RP3; dbSNP:rs62640590
VAR_018065312D>Nin RP3
VAR_018066312D>Yin RP3
VAR_018067320G>Rin RP3; impairs protein folding; dbSNP:rs62640593
VAR_008510436G>Din RP3; dbSNP:rs62635004

Retinitis pigmentosa, X-linked, and sinorespiratory infections with or without deafness (RPSRDF)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A disease characterized by the association of retinitis pigmentosa with recurrent upper and lower airway infections. Some patients also develop progressive hearing loss.
  • See also
    MIM:300455
Natural variants in RPSRDF
Variant IDPosition(s)ChangeDescription
VAR_018060173G>Rin RP3 and RPSRDF; dbSNP:rs137852550

Cone-rod dystrophy, X-linked 1 (CORDX1)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa. In cone-rod dystrophy X-linked type 1 the degree of rod-photoreceptor involvement can be variable, with degeneration increasing as the disease progresses. Affected individuals (essentially all of whom are males) present with decreased visual acuity, myopia, photophobia, abnormal color vision, full peripheral visual fields, decreased photopic electroretinographic responses, and granularity of the macular retinal pigment epithelium. Although penetrance appears to be nearly 100%, there is variable expressivity with respect to age at onset and severity of symptoms.
  • See also
    MIM:304020

Macular degeneration, atrophic, X-linked (MDXLA)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An ocular disorder characterized by macular atrophy causing progressive loss of visual acuity with minimal peripheral visual impairment. Some patients manifest extensive macular degeneration plus peripheral loss of retinal pigment epithelium and choriocapillaries. Full-field electroretinograms (ERGs) show normal cone and rod responses in some affected males despite advanced macular degeneration.
  • See also
    MIM:300834

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis36Does not reduce interaction with PDE6D.
Natural variantVAR_01805743in RP3; dbSNP:rs62638630
Natural variantVAR_01805843in RP3; dbSNP:rs62638629
Natural variantVAR_00850160in RP3; dbSNP:rs62638634
Natural variantVAR_00850375in RP3; benign; dbSNP:rs111631988
Natural variantVAR_01362476in dbSNP:rs1801685
Natural variantVAR_00850498in RP3; reduces interaction with PDE6D; dbSNP:rs62638636
Natural variantVAR_01362599in RP3; dbSNP:rs62638637
Natural variantVAR_018059127in RP3; dbSNP:rs62638643
Natural variantVAR_006850130in RP3; reduces interaction with PDE6D; dbSNP:rs62638644
Natural variantVAR_025949152in RP3
Natural variantVAR_018060173in RP3 and RPSRDF; dbSNP:rs137852550
Natural variantVAR_033259184in dbSNP:rs5963403
Natural variantVAR_008505215in RP3; reduces interaction with PDE6D; dbSNP:rs62650218
Natural variantVAR_006851235in RP3; reduces interaction with PDE6D; dbSNP:rs62638651
Natural variantVAR_008506250in RP3; reduces interaction with PDE6D; dbSNP:rs62650220
Natural variantVAR_018061250in RP3; dbSNP:rs1601961064
Natural variantVAR_018062258in RP3
Natural variantVAR_008507262in RP3; uncertain significance; dbSNP:rs138018739
Natural variantVAR_018063267in RP3
Natural variantVAR_026127267in RP3; dbSNP:rs2147248035
Natural variantVAR_006852275in RP3; reduces interaction with PDE6D; dbSNP:rs62642057
Natural variantVAR_026128285in RP3
Natural variantVAR_013626289in RP3; dbSNP:rs62640587
Natural variantVAR_013627296-300in RP3
Natural variantVAR_011561302in RP3; dbSNP:rs62640589
Natural variantVAR_018064302in RP3; dbSNP:rs62640590
Natural variantVAR_018065312in RP3
Natural variantVAR_018066312in RP3
Natural variantVAR_018067320in RP3; impairs protein folding; dbSNP:rs62640593
Mutagenesis323Abolishes interaction with RPGRIP1.
Natural variantVAR_018068345in dbSNP:rs41305223
Natural variantVAR_008508425in dbSNP:rs1801687
Natural variantVAR_008509431in dbSNP:rs62635003
Natural variantVAR_008510436in RP3; dbSNP:rs62635004
Natural variantVAR_011562526
Natural variantVAR_011563533in dbSNP:rs41312104
Natural variantVAR_008511566in dbSNP:rs1801688

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 951 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data), lipidation, propeptide.

TypeIDPosition(s)SourceDescription
ChainPRO_00002066381-1017UniProtX-linked retinitis pigmentosa GTPase regulator
Modified residue418UniProtPhosphoserine
Modified residue (large scale data)418PRIDEPhosphoserine
Modified residue518UniProtPhosphoserine
Modified residue (large scale data)518PRIDEPhosphoserine
Modified residue (large scale data)895PRIDEPhosphoserine
Modified residue (large scale data)961PRIDEPhosphoserine
Modified residue1017UniProtCysteine methyl ester
Lipidation1017UniProtS-geranylgeranyl cysteine
PropeptidePRO_00003708441018-1020UniProtRemoved in mature form

Post-translational modification

Prenylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Heart, brain, placenta, lung, liver, muscle, kidney, retina, pancreas and fetal retinal pigment epithelium. Isoform 3 is found only in the retina. Colocalizes with RPGRIP1 in the outer segment of rod photoreceptors and cone outer segments.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with SPATA7 (By similarity).
Interacts with CEP290 (By similarity).
Interacts with WHRN (By similarity).
Interacts with PDE6D (PubMed:23559067, PubMed:24981858, PubMed:9990021).
Interacts with RPGRIP1 (PubMed:10958648, PubMed:24981858).
Interacts with RPGRIP1L (PubMed:19430481, PubMed:24981858).
PDE6D, RPGRIP1 and RPGRIP1L may compete for the same binding sites (PubMed:24981858).
Isoform 6 interacts with NPM1 (via C-terminus) (PubMed:15772089).
Isoform 6 interacts with SMC1A and SMC3 (PubMed:16043481).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for repeat, compositional bias, region.

TypeIDPosition(s)Description
Repeat54-105RCC1 1
Repeat106-158RCC1 2
Repeat159-208RCC1 3
Repeat209-261RCC1 4
Repeat262-313RCC1 5
Repeat314-367RCC1 6
Compositional bias609-667Basic and acidic residues
Region609-776Disordered
Compositional bias681-715Basic and acidic residues
Compositional bias749-776Basic and acidic residues
Compositional bias790-853Basic and acidic residues
Region790-906Disordered
Compositional bias861-875Basic and acidic residues
Compositional bias886-906Basic and acidic residues
Region989-1020Disordered
Compositional bias997-1020Polar residues

Domain

The RCC1 repeat region mediates interactions with RPGRIP1.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (6)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 6 isoforms produced by Alternative splicing. Additional isoforms seem to exist.

Q92834-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    1,020
  • Mass (Da)
    113,387
  • Last updated
    2002-09-19 v2
  • Checksum
    EAB16275A9A436C3
MREPEELMPDSGAVFTFGKSKFAENNPGKFWFKNDVPVHLSCGDEHSAVVTGNNKLYMFGSNNWGQLGLGSKSAISKPTCVKALKPEKVKLAACGRNHTLVSTEGGNVYATGGNNEGQLGLGDTEERNTFHVISFFTSEHKIKQLSAGSNTSAALTEDGRLFMWGDNSEGQIGLKNVSNVCVPQQVTIGKPVSWISCGYYHSAFVTTDGELYVFGEPENGKLGLPNQLLGNHRTPQLVSEIPEKVIQVACGGEHTVVLTENAVYTFGLGQFGQLGLGTFLFETSEPKVIENIRDQTISYISCGENHTALITDIGLMYTFGDGRHGKLGLGLENFTNHFIPTLCSNFLRFIVKLVACGGCHMVVFAAPHRGVAKEIEFDEINDTCLSVATFLPYSSLTSGNVLQRTLSARMRRRERERSPDSFSMRRTLPPIEGTLGLSACFLPNSVFPRCSERNLQESVLSEQDLMQPEEPDYLLDEMTKEAEIDNSSTVESLGETTDILNMTHIMSLNSNEKSLKLSPVQKQKKQQTIGELTQDTALTENDDSDEYEEMSEMKEGKACKQHVSQGIFMTQPATTIEAFSDEEVGNDTGQVGPQADTDGEGLQKEVYRHENNNGVDQLDAKEIEKESDGGHSQKESEAEEIDSEKETKLAEIAGMKDLREREKSTKKMSPFFGNLPDRGMNTESEENKDFVKKRESCKQDVIFDSERESVEKPDSYMEGASESQQGIADGFQQPEAIEFSSGEKEDDEVETDQNIRYGRKLIEQGNEKETKPIISKSMAKYDFKCDRLSEIPEEKEGAEDSKGNGIEEQEVEANEENVKVHGGRKEKTEILSDDLTDKAEDHEFSKTEELKLEDVDEEINAENVESKKKTVGDDESVPTGYHSKTEGAERTNDDSSAETIEKKEKANLEERAICEYNENPKGYMLDDADSSSLEILENSETTPSKDMKKTKKIFLFKRVPSINQKIVKNNNEPLPEIKSIGDQIILKSDNKDADQNHMSQNHQNIPPTNTERRSKSCTIL

Q92834-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q92834-3

Q92834-4

Q92834-5

  • Name
    5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q92834-6

  • Name
    6
  • Synonyms
    ORF15
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 585-1020: GNDTGQVGPQADTDGEGLQKEVYRHENNNGVDQLDAKEIEKESDGGHSQKESEAEEIDSEKETKLAEIAGMKDLREREKSTKKMSPFFGNLPDRGMNTESEENKDFVKKRESCKQDVIFDSERESVEKPDSYMEGASESQQGIADGFQQPEAIEFSSGEKEDDEVETDQNIRYGRKLIEQGNEKETKPIISKSMAKYDFKCDRLSEIPEEKEGAEDSKGNGIEEQEVEANEENVKVHGGRKEKTEILSDDLTDKAEDHEFSKTEELKLEDVDEEINAENVESKKKTVGDDESVPTGYHSKTEGAERTNDDSSAETIEKKEKANLEERAICEYNENPKGYMLDDADSSSLEILENSETTPSKDMKKTKKIFLFKRVPSINQKIVKNNNEPLPEIKSIGDQIILKSDNKDADQNHMSQNHQNIPPTNTERRSKSCTIL → EIPEEKEGAEDSKGNGIEEQEVEANEENVKVHGGRKEKTEILSDDLTDKAEVSEGKAKSVGEAEDGPEGRGDGTCEEGSSGAEHWQDEEREKGEKDKGRGEMERPGEGEKELAEKEEWKKRDGEEQEQKEREQGHQKERNQEMEEGGEEEHGEGEEEEGDREEEEEKEGEGKEEGEGEEVEGEREKEEGERKKEERAGKEEKGEEEGDQGEGEEEETEGRGEEKEEGGEVEGGEVEEGKGEREEEEEEGEGEEEEGEGEEEEGEGEEEEGEGKGEEEGEEGEGEEEGEEGEGEGEEEEGEGEGEEEGEGEGEEEEGEGEGEEEGEGEGEEEEGEGKGEEEGEEGEGEGEEEEGEGEGEDGEGEGEEEEGEWEGEEEEGEGEGEEEGEGEGEEGEGEGEEEEGEGEGEEEEGEEEGEEEGEGEEEGEGEGEEEEEGEVEGEVEGEEGEGEGEEEEGEEEGEEREKEGEGEENRRNREEEEEEEGKYQETGEEENERQDGEEYKKVSKIKGSVKYGKHKTYQKKSVTNTQGNGKEQRSKMPVQSKRLLKNGPSGSKKFWNNVLPHYLELK

Computationally mapped potential isoform sequences

There are 9 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2R8Y838A0A2R8Y838_HUMANRPGR540
A0A2R8Y414A0A2R8Y414_HUMANRPGR673
A0A2R8Y4C9A0A2R8Y4C9_HUMANRPGR325
A0A2R8YGY6A0A2R8YGY6_HUMANRPGR379
A0A2R8YDN2A0A2R8YDN2_HUMANRPGR508
A0A2R8YFT6A0A2R8YFT6_HUMANRPGR642
A0A2R8YF02A0A2R8YF02_HUMANRPGR167
H7C4H4H7C4H4_HUMANRPGR415
H7C4L1H7C4L1_HUMANRPGR129

Features

Showing features for sequence conflict, alternative sequence, compositional bias.

TypeIDPosition(s)Description
Sequence conflict1-3in Ref. 4; CAB54002
Sequence conflict190in Ref. 4; CAC86116
Alternative sequenceVSP_005547354-415in isoform 4
Alternative sequenceVSP_009183473-480in isoform 5
Alternative sequenceVSP_009184481-1020in isoform 5
Alternative sequenceVSP_005548585-789in isoform 2, isoform 3 and isoform 4
Alternative sequenceVSP_044559585-1020in isoform 6
Compositional bias609-667Basic and acidic residues
Compositional bias681-715Basic and acidic residues
Compositional bias749-776Basic and acidic residues
Compositional bias790-853Basic and acidic residues
Alternative sequenceVSP_005549841-851in isoform 3
Alternative sequenceVSP_005550852-1020in isoform 3
Compositional bias861-875Basic and acidic residues
Compositional bias886-906Basic and acidic residues
Compositional bias997-1020Polar residues
Sequence conflict1144In isoform Q92834-6; in Ref. 17; DAA05713

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U57629
EMBL· GenBank· DDBJ
AAC50481.1
EMBL· GenBank· DDBJ
mRNA
X97668
EMBL· GenBank· DDBJ
CAA66258.1
EMBL· GenBank· DDBJ
mRNA
AJ238395
EMBL· GenBank· DDBJ
CAB54002.1
EMBL· GenBank· DDBJ
mRNA
AJ318463
EMBL· GenBank· DDBJ
CAC86116.1
EMBL· GenBank· DDBJ
Genomic DNA
AL606748
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471141
EMBL· GenBank· DDBJ
EAW59441.1
EMBL· GenBank· DDBJ
Genomic DNA
BC031624
EMBL· GenBank· DDBJ
AAH31624.1
EMBL· GenBank· DDBJ
mRNA
AF286471
EMBL· GenBank· DDBJ
AAG00550.1
EMBL· GenBank· DDBJ
Genomic DNA
BK005711
EMBL· GenBank· DDBJ
DAA05713.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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