Q7JXA8 · RHINO_DROME
- ProteinChromo domain-containing protein rhino
- Generhi
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids418 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in piRNA (piwi-interacting RNA)-mediated transposon repression (PubMed:19732946, PubMed:36193674).
May be involved in formation of the perinuclear nuage, a subcellular structure implicated in RNA processing that may be involved in transposon RNA surveillance and silencing (PubMed:19732946, PubMed:36193674).
Required for ping-pong amplification during piRNA biogenesis, probably by promoting transcription of piRNA precursors (PubMed:19732946, PubMed:25085419, PubMed:36193674).
As part of the Rhino-Deadlock-Cutoff (RDC) Complex associates with, and drives non-canonical transcription of germline specific dual-strand piRNA clusters 80F, 38C and 42AB, but not single-stranded piRNA cluster 20A (PubMed:19732946, PubMed:24906153, PubMed:25085419, PubMed:36193674).
Induction of piRNA expression is potentially achieved through a mechanism that prevents transcriptional termination and leads to readthrough from flanking transcription units (PubMed:24906153).
Recruited to specific chromatin regions by a combination of H3K9me2/3 histone methylation and differentially expressed sequence-specific recruitment factors (PubMed:24906153, PubMed:25085419, PubMed:25613572, PubMed:36193674).
This association may involve direct interaction with DNA (PubMed:25613572).
Associates with chromatin upon exposure to homologous piRNA and facilitates transcriptional read-through (PubMed:27292797).
As part of the RDC complex, involved in suppression of splicing (PubMed:27292797).
In ovaries, recruitment to specific heterochromatin clusters is nucleated and stabilized by kipf/kipferl (PubMed:36193674).
During oogenesis, involved in axis specification and may regulate chromosome condensation at the onset of a mitotic-like phase that occurs during nurse cell chromosome duplication (PubMed:11729157).
Involved in the distribution of mRNAs for proteins that play a role in anterior-posterior and dorsal-ventral axes specification during development of the oocyte, including grk/gurken, osk/oskar and vas/vasa (PubMed:11729157, PubMed:19732946).
Mitigates meiotic double strand breaks and interacts with DNA damage signaling to mediate axis specification (PubMed:19732946).
May be involved in formation of the perinuclear nuage, a subcellular structure implicated in RNA processing that may be involved in transposon RNA surveillance and silencing (PubMed:19732946, PubMed:36193674).
Required for ping-pong amplification during piRNA biogenesis, probably by promoting transcription of piRNA precursors (PubMed:19732946, PubMed:25085419, PubMed:36193674).
As part of the Rhino-Deadlock-Cutoff (RDC) Complex associates with, and drives non-canonical transcription of germline specific dual-strand piRNA clusters 80F, 38C and 42AB, but not single-stranded piRNA cluster 20A (PubMed:19732946, PubMed:24906153, PubMed:25085419, PubMed:36193674).
Induction of piRNA expression is potentially achieved through a mechanism that prevents transcriptional termination and leads to readthrough from flanking transcription units (PubMed:24906153).
Recruited to specific chromatin regions by a combination of H3K9me2/3 histone methylation and differentially expressed sequence-specific recruitment factors (PubMed:24906153, PubMed:25085419, PubMed:25613572, PubMed:36193674).
This association may involve direct interaction with DNA (PubMed:25613572).
Associates with chromatin upon exposure to homologous piRNA and facilitates transcriptional read-through (PubMed:27292797).
As part of the RDC complex, involved in suppression of splicing (PubMed:27292797).
In ovaries, recruitment to specific heterochromatin clusters is nucleated and stabilized by kipf/kipferl (PubMed:36193674).
During oogenesis, involved in axis specification and may regulate chromosome condensation at the onset of a mitotic-like phase that occurs during nurse cell chromosome duplication (PubMed:11729157).
Involved in the distribution of mRNAs for proteins that play a role in anterior-posterior and dorsal-ventral axes specification during development of the oocyte, including grk/gurken, osk/oskar and vas/vasa (PubMed:11729157, PubMed:19732946).
Mitigates meiotic double strand breaks and interacts with DNA damage signaling to mediate axis specification (PubMed:19732946).
Miscellaneous
Wild-type eggs possess two dorsal respiratory appendages. Mutations in rhi/Rhino results in partial or complete fusion of these appendages resulting in a single appendage from which Rhino gets its name.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | heterochromatin | |
Cellular Component | nucleus | |
Cellular Component | pericentric heterochromatin | |
Cellular Component | Rhino-Deadlock-Cutoff Complex | |
Molecular Function | chromatin binding | |
Molecular Function | methylated histone binding | |
Biological Process | chorion-containing eggshell pattern formation | |
Biological Process | chromosome organization | |
Biological Process | heterochromatin formation | |
Biological Process | piRNA processing | |
Biological Process | piRNA transcription | |
Biological Process | positive regulation of piRNA transcription | |
Biological Process | positive regulation of snRNA transcription by RNA polymerase II | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | transcription antitermination |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameChromo domain-containing protein rhino
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ7JXA8
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to germline specific nuclear foci throughout oogenesis, which corelate with dual-strand piRNA source loci (PubMed:19732946, PubMed:24906153).
All components of the Rhino-Deadlock-Cutoff (RDC) Complex associate with these nuclear foci and are required for their formation (PubMed:24906153).
All components of the Rhino-Deadlock-Cutoff (RDC) Complex associate with these nuclear foci and are required for their formation (PubMed:24906153).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Females are sterile and produce eggs with various polarity defects.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 34 | Disrupts dimerization, reduces nuclear foci association in nurse cells, cannot inhibit transposon hyperexpression and is unable to rescue sterility phenotype of knockout mutants; when associated with A-76. | ||||
Sequence: F → A | ||||||
Mutagenesis | 45 | Abolishes binding to H3K9me3 peptide, reduces nuclear foci association in nurse cells, cannot inhibit transposon hyperexpression and is unable to rescue sterility phenotype of knockout mutants. | ||||
Sequence: W → A | ||||||
Mutagenesis | 48 | Abolishes binding to H3K9me3 peptide. | ||||
Sequence: F → A | ||||||
Mutagenesis | 76 | Disrupts dimerization, reduces nuclear foci association in nurse cells, cannot inhibit transposon hyperexpression and is unable to rescue sterility phenotype of knockout mutants; when associated with A-34. | ||||
Sequence: F → A | ||||||
Mutagenesis | 369-373 | Disrupts interaction with del/deadlock and nuclear foci accumulation, cannot inhibit transposon hyperexpression and is unable to rescue sterility phenotype of knockout mutants. Reduced protein stability. | ||||
Sequence: HCYQM → GCTQS | ||||||
Mutagenesis | 371-380 | Disrupts interaction with del/deadlock and nuclear foci accumulation, cannot inhibit transposon hyperexpression and is unable to rescue sterility phenotype of knockout mutants. Reduced protein stability. | ||||
Sequence: YQMNDDLFMF → TQMNDDLSMS | ||||||
Mutagenesis | 412-416 | Disrupts interaction with del/deadlock and nuclear foci accumulation, cannot inhibit transposon hyperexpression and is unable to rescue sterility phenotype of knockout mutants. Reduced protein stability. | ||||
Sequence: LRIIV → AAAAA |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000458884 | 1-418 | Chromo domain-containing protein rhino | |||
Sequence: MSRNHQRPNLGLVDAPPNDHVEEYVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENVGNCMKLVSDFESEVFRLHRKAAAKSVGKSKSSPSSSGPLITENGPSSSKKTQQHSKSVQAKNTAGMSKMNQKKGKNIKKTAGKIKDIENYPKTQMPSTSQVSTDSTEVFDGNPSATTTNMIKSPRIQSLFSDLNLIEPTKDKDVGDTSLKTPPKSRRLIEFPQREDAPLSSKHVSPMLIRKESQPLQSSCTDDSDLGESSSSMSLPTVSSTSSEKSIKVTKSEPKTLGQIKFSSRSSDGGHAASSLGAPKEGDIGLDLSGSDSMDSEVESMRRCPRRKRKKTYPDWKFPEMTKPFGVNRGLDLDKILHCYQMNDDLFMFVTWKGCSSIDAVHINDIKEAYPLQIIKYFESLRIIVPK |
Proteomic databases
Expression
Tissue specificity
Female specific, expressed in both somatic and germline cells but highly enriched in ovaries (PubMed:11729157).
In the germarium of the developing oocyte expressed in germline stem cells, cystoblasts and developing germline cysts (PubMed:36193674).
Expressed in nurse cells in the germarium and egg chamber (PubMed:36193674).
In the germarium of the developing oocyte expressed in germline stem cells, cystoblasts and developing germline cysts (PubMed:36193674).
Expressed in nurse cells in the germarium and egg chamber (PubMed:36193674).
Developmental stage
During oogenesis, low levels in region 1 of the germarium, accumulates in the oocyte by stage 5, and between stage 8 and 10A localizes to the posterior of the oocyte (PubMed:11729157).
By stage 10B posterior localization in the oocyte is lost but expression is significantly enhanced in nurse cells (PubMed:11729157).
Abundant early during embryogenesis with levels gradually tapering off (PubMed:11729157).
Displays an expression profile typical of maternal transcripts deposited into the embryo (PubMed:11729157).
By stage 10B posterior localization in the oocyte is lost but expression is significantly enhanced in nurse cells (PubMed:11729157).
Abundant early during embryogenesis with levels gradually tapering off (PubMed:11729157).
Displays an expression profile typical of maternal transcripts deposited into the embryo (PubMed:11729157).
Gene expression databases
Interaction
Subunit
Homodimer in solution (PubMed:25085419, PubMed:25613572).
Dimerization is essential for chromatin binding (PubMed:25613572).
Component of the Rhino-Deadlock-Cutoff (RDC) complex, composed of rhi/rhino, del/deadlock and cuff/cutoff (PubMed:24906153).
Interacts (via C-terminus) with del/deadlock (via N-terminus); this interaction is direct (PubMed:24906153, PubMed:29858487).
Two copies of del/deadlock associate with each rhi/rhino dimer (PubMed:29858487).
Interacts with cuff/cutoff; this interaction is indirect and is mediated by del/deadlock (PubMed:24906153, PubMed:25085419).
Interacts (via Chromo domain) with kipf/kipferl (via C2H2 type zinc finger 4) (PubMed:36193674).
Interacts (via Chromo domain) with His3/histone H3 (via N-terminus di- or tri-methylated on 'Lys-10' (H3K9me2/3)); this interaction is direct (PubMed:24906153, PubMed:25085419, PubMed:25613572).
Two His3 N-terminal tails oriented anti-parallel to each other are required for dimer binding to His3 (PubMed:25613572).
Dimerization is essential for chromatin binding (PubMed:25613572).
Component of the Rhino-Deadlock-Cutoff (RDC) complex, composed of rhi/rhino, del/deadlock and cuff/cutoff (PubMed:24906153).
Interacts (via C-terminus) with del/deadlock (via N-terminus); this interaction is direct (PubMed:24906153, PubMed:29858487).
Two copies of del/deadlock associate with each rhi/rhino dimer (PubMed:29858487).
Interacts with cuff/cutoff; this interaction is indirect and is mediated by del/deadlock (PubMed:24906153, PubMed:25085419).
Interacts (via Chromo domain) with kipf/kipferl (via C2H2 type zinc finger 4) (PubMed:36193674).
Interacts (via Chromo domain) with His3/histone H3 (via N-terminus di- or tri-methylated on 'Lys-10' (H3K9me2/3)); this interaction is direct (PubMed:24906153, PubMed:25085419, PubMed:25613572).
Two His3 N-terminal tails oriented anti-parallel to each other are required for dimer binding to His3 (PubMed:25613572).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q7JXA8 | H3C12 P68431 | 2 | EBI-149916, EBI-79722 | |
BINARY | Q7JXA8 | His3:CG33854 P02299 | 4 | EBI-149916, EBI-522090 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-74 | Chromo | ||||
Sequence: YVVEKILGKRFVNGRPQVLVKWSGFPNENNTWEPLENVGNCMKLVSDFESE | ||||||
Region | 84-167 | Disordered | ||||
Sequence: AKSVGKSKSSPSSSGPLITENGPSSSKKTQQHSKSVQAKNTAGMSKMNQKKGKNIKKTAGKIKDIENYPKTQMPSTSQVSTDST | ||||||
Compositional bias | 88-131 | Polar residues | ||||
Sequence: GKSKSSPSSSGPLITENGPSSSKKTQQHSKSVQAKNTAGMSKMN | ||||||
Compositional bias | 152-167 | Polar residues | ||||
Sequence: PKTQMPSTSQVSTDST | ||||||
Region | 199-337 | Disordered | ||||
Sequence: PTKDKDVGDTSLKTPPKSRRLIEFPQREDAPLSSKHVSPMLIRKESQPLQSSCTDDSDLGESSSSMSLPTVSSTSSEKSIKVTKSEPKTLGQIKFSSRSSDGGHAASSLGAPKEGDIGLDLSGSDSMDSEVESMRRCPR | ||||||
Compositional bias | 242-302 | Polar residues | ||||
Sequence: KESQPLQSSCTDDSDLGESSSSMSLPTVSSTSSEKSIKVTKSEPKTLGQIKFSSRSSDGGH | ||||||
Region | 353-418 | Required for interaction with del/deadlock | ||||
Sequence: TKPFGVNRGLDLDKILHCYQMNDDLFMFVTWKGCSSIDAVHINDIKEAYPLQIIKYFESLRIIVPK |
Domain
The Chromo domain mediates binding to chromatin through interaction with the histone H3 N-terminal tail. Binding requires di- or tri- methylation of histone H3 'Lys-10' (H3K9me2/3).
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length418
- Mass (Da)46,345
- Last updated2006-10-03 v1
- Checksum8996711F329D4B45
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 88-131 | Polar residues | ||||
Sequence: GKSKSSPSSSGPLITENGPSSSKKTQQHSKSVQAKNTAGMSKMN | ||||||
Compositional bias | 152-167 | Polar residues | ||||
Sequence: PKTQMPSTSQVSTDST | ||||||
Compositional bias | 242-302 | Polar residues | ||||
Sequence: KESQPLQSSCTDDSDLGESSSSMSLPTVSSTSSEKSIKVTKSEPKTLGQIKFSSRSSDGGH |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF411862 EMBL· GenBank· DDBJ | AAL05865.1 EMBL· GenBank· DDBJ | mRNA | ||
AE013599 EMBL· GenBank· DDBJ | AAF57822.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY094869 EMBL· GenBank· DDBJ | AAM11222.1 EMBL· GenBank· DDBJ | mRNA |