Q4Z8K6 · RBP9X_DROME

Function

function

May be involved in JAK/STAT signaling. Isoform D is required for the proper arrangement of niche cells and is autonomously required for proper niche cell size, isoform C negatively regulates the adhesive properties of the niche. The germline stem cell (GSC) niche in ovaries is made up of two somatic cell types: 8-9 cells in a single-filed array make up the terminal filament (TF), and a tight cluster of 5 or 6 cap cells (CpC). Regulating the size and adhesive properties of the CpCs is an important component of the mechanism that controls their capacity to support stem cells, isoform C and isoform D are important factors in mediating this regulation. In contrast, isoform C acts as a positive regulator of cell adhesion in follicle cell epithelium.

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 Componentcytoplasm
Cellular ComponentGID complex
Cellular Componentmembrane
Cellular Componentnucleus
Molecular Functionsmall GTPase binding
Biological Processcytoskeleton organization
Biological Processdorsal appendage formation
Biological Processfollicle cell of egg chamber-cell adhesion
Biological Processgerm-line stem-cell niche homeostasis
Biological Processlarval feeding behavior
Biological Processnegative regulation of cell adhesion
Biological Processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
Biological Processpositive regulation of protein export from nucleus

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ran-binding proteins 9/10 homolog
  • Alternative names
    • Ran-binding protein M

Gene names

    • Name
      RanBPM
    • ORF names
      CG42236

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q4Z8K6
  • Secondary accessions
    • A1Z895
    • A1Z896
    • A8E757
    • Q6NN33
    • Q8T0U5
    • Q960F3

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Membrane
Nucleus
Note: Distribution varies depending on cell type and developmental stage. At late embryogenesis expression is enriched in the nuclei of follicle cells and germline cells and at the nurse cell membranes. In pupal ovaries, expression is seen in niche cells at the cell periphery. In adult ovaries expression is in the nuclei and cytoplasm of the CpCs and TF cells of the niche.

Keywords

Phenotypes & Variants

Disruption phenotype

Lack of isoform D causes an increase in niche cell size and abnormal terminal filament organization. This in turn increases niche capacity by increasing the potential contact surface between CpCs and stem cells. Lack of isoform C causes defects in the organization of the follicle cell layer and defects in dorsal appendage morphogenesis.

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00003052401-962Ran-binding proteins 9/10 homolog
Modified residue387Phosphoserine
Modified residue393Phosphoserine
Modified residue395Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in the GSCs and in dividing cysts. Expression is reduced in the germline as individual egg chambers are formed. Isoform C is expressed in all somatic and germline cells of the ovary. Isoform D is expressed in the GSC niche.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-246Disordered
Compositional bias8-51Polar residues
Compositional bias52-73Pro residues
Compositional bias91-161Polar residues
Compositional bias162-219Basic and acidic residues
Compositional bias271-286Acidic residues
Region271-296Disordered
Region313-402Disordered
Compositional bias315-400Polar residues
Domain400-587B30.2/SPRY
Domain617-649LisH
Domain655-712CTLH
Region800-820Disordered

Sequence similarities

Belongs to the RANBP9/10 family.

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q4Z8K6-1

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.

  • Name
    D
  • Synonyms
    Long RanBPM
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    962
  • Mass (Da)
    106,654
  • Last updated
    2005-06-07 v1
  • Checksum
    91206B4DC4D9DB30
MENVEEAPPLSSESNSNSNNSSASSSSHQLSQSGAMGAEIAPSTSRSHSHSPTPSPPVPASSHDQPHPDHPSPPLNASETEARENSPHDHSPTPTFHQTAPPPTTSSTAPQRDEREQQQQQEAPPLQQDQQENSPAQDQELHPLLDQQNQEYPAVHQDQQAEQNQELHHIEGLIRHRESQNPEEHPPQASLENRETLGREDTNQEPDEPQVRDPEIEPEAEPPPPLLLEDLDEQDSGSQDLNEQQPPLIIDANAIAETIDANAVERIDDYEDDDEEVDEEEEVVEDRVDRAGEVASVSGAQRLHSVAVLPRYSSASRAPRSSNNNNNNISNHNNNNNNSNSNSLSRRTRHFYSNNGSHFSNDMFPSHNPRSSTQTSSPRVGGRRHHSTPAASSNSPQHQGVDPLRLLYPNVNESETPLPRCWSPHDKCLSIGLSQNNLRVTYKGVGKQHSDAASVRTAYPIPSSCGLYYFEVRIISKGRNGYMGIGLTAQQFRMNRLPGWDKQSYGYHGDDGNSFSSSGNGQTYGPTFTTGDVIGCCVNFVNNTCFYTKNGVDLGIAFRDLPTKLYPTVGLQTPGEEVDANFGQEPFKFDKIVDMMKEMRSNVLRKIDRYPHLLETPENLMNRLVSTYLVHNAFSKTAEAFNGYTNQTFNEDLASIKTRQKIIKLILTGKMSQAIEHTLRSFPGLLENNKNLWFALKCRQFIEMINGADIENVNNKVTATTQTMPTNQTSVIQSTKTFKHSKSGSGNGNVNINQTQQQNNTAIPAVIKPQGGDRPDIKNMLVDDNSNKCVEHDSNSMDVEMEPCQSHSNGGDSSSNGNASAVRNSLDAIDEEMDVDVSPSSRNCGRVIEKILEFGKELSSMGQQLEKENLMTEEERQMLEDAFSLIAYSNPWSSPLGWLLCPSRRESVSTTLNSAILESLNFERRPPLEYLVAHASELIKVIGQHSLGEDAFITIDDVFPQN

Q4Z8K6-2

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

Q4Z8K6-3

  • Name
    C
  • Synonyms
    Short RanBPM
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0B4KFL0A0A0B4KFL0_DROMERanBPM770
A0A0B4K851A0A0B4K851_DROMERanBPM961
A0A126GUM4A0A126GUM4_DROMERanBPM1127

Sequence caution

The sequence AAK93515.1 differs from that shown. Reason: Miscellaneous discrepancy Intron retention.
The sequence AAL39193.1 differs from that shown. Reason: Erroneous initiation
The sequence AAR99122.1 differs from that shown. Reason: Frameshift
The sequence AAX84045.1 differs from that shown. Reason: Frameshift
The sequence ABV82381.1 differs from that shown. Reason: Miscellaneous discrepancy Intron retention.

Features

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

Type
IDPosition(s)Description
Alternative sequenceVSP_0282961-362in isoform C
Compositional bias8-51Polar residues
Compositional bias52-73Pro residues
Compositional bias91-161Polar residues
Compositional bias162-219Basic and acidic residues
Compositional bias271-286Acidic residues
Compositional bias315-400Polar residues
Sequence conflict445in Ref. 5; AAK93515
Alternative sequenceVSP_028297834-835in isoform A and isoform C

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY973544
EMBL· GenBank· DDBJ
AAX84045.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AY973545
EMBL· GenBank· DDBJ
AAX84046.1
EMBL· GenBank· DDBJ
mRNA
AY973546
EMBL· GenBank· DDBJ
AAX84047.1
EMBL· GenBank· DDBJ
mRNA
AE013599
EMBL· GenBank· DDBJ
AAF58795.2
EMBL· GenBank· DDBJ
Genomic DNA
AE013599
EMBL· GenBank· DDBJ
AAM68758.1
EMBL· GenBank· DDBJ
Genomic DNA
AE013599
EMBL· GenBank· DDBJ
ABC66064.1
EMBL· GenBank· DDBJ
Genomic DNA
BT011464
EMBL· GenBank· DDBJ
AAR99122.1
EMBL· GenBank· DDBJ
mRNA Frameshift
BT030999
EMBL· GenBank· DDBJ
ABV82381.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AY052091
EMBL· GenBank· DDBJ
AAK93515.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AY069048
EMBL· GenBank· DDBJ
AAL39193.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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