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krimp krimper [ Drosophila melanogaster (fruit fly) ]

Gene ID: 36804, updated on 8-Apr-2026
Official Symbol
krimpprovided by FlyBase
Official Full Name
krimperprovided by FlyBase
Primary source
FLYBASE:FBgn0034098
Locus tag
Dmel_CG15707
See related
AllianceGenome:FB:FBgn0034098
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Drosophila melanogaster
Lineage
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora
Also known as
CG15707; Dmel\CG15707; Krimp; KRIMP; Krimper; mtc
Summary
Predicted to enable metal ion binding activity. Involved in negative regulation of gene expression and oogenesis. Located in P granule and perinuclear region of cytoplasm. Is expressed in female germline cell; male germline cell; and organism. [provided by Alliance of Genome Resources, Jul 2025]
Orthologs
all
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See krimp in Genome Data Viewer
Location:
53A1-53A1; 2-79 cM
Exon count:
2
Annotation release Status Assembly Chr Location
Release 6.54 current Release 6 plus ISO1 MT (GCF_000001215.4) 2R NT_033778.4 (16238103..16240722, complement)
Release 5.57 previous assembly Release 5 (GCF_000001215.2) 2R NT_033778.3 (12125608..12128227, complement)

Chromosome 2R - NT_033778.4Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene Cyclic nucleotide-gated ion channel subunit A

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Tudor-domain containing proteins act to make the piRNA pathways more robust in Drosophila. Sato K, et al. Fly (Austin), 2015. PMID 26647059, Free PMC Article
  2. Gender-Specific Hierarchy in Nuage Localization of PIWI-Interacting RNA Factors in Drosophila. Nagao A, et al. Front Genet, 2011. PMID 22303351, Free PMC Article
  3. Somatic Primary piRNA Biogenesis Driven by cis-Acting RNA Elements and trans-Acting Yb. Ishizu H, et al. Cell Rep, 2015 Jul 21. PMID 26166564
  4. Targeting and anchoring Tudor in the pole plasm of the Drosophila oocyte. Anne J. PLoS One, 2010 Dec 15. PMID 21179512, Free PMC Article
  5. Binding of guide piRNA triggers methylation of the unstructured N-terminal region of Aub leading to assembly of the piRNA amplification complex. Huang X, et al. Nat Commun, 2021 Jul 1. PMID 34210982, Free PMC Article

See all (96) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Krimper and Qin proteins play crucial roles in maintaining the levels of piRNAs loaded onto Piwi and Aub to efficiently repress transposons at transcriptional and post-transcriptional levels, respectively.
    Title: Tudor-domain containing proteins act to make the piRNA pathways more robust in Drosophila.
  2. Krimper interacts directly with Aub and Ago3 to coordinate the assembly of the ping-pong piRNA processing complex.
    Title: Aub and Ago3 Are Recruited to Nuage through Two Mechanisms to Form a Ping-Pong Complex Assembled by Krimper.
  3. Krimp enforces an antisense bias on piRNA pools by binding AGO3 and blocking its access to primary piRNAs.
    Title: Krimper Enforces an Antisense Bias on piRNA Pools by Binding AGO3 in the Drosophila Germline.
  4. Krimper, a component of the nuage, ensures the repression of selfish genetic elements in the female germ line.
    Title: Unique germ-line organelle, nuage, functions to repress selfish genetic elements in Drosophila melanogaster.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by FlyBase

Function Evidence Code Pubs
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in negative regulation of oskar mRNA translation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in oocyte dorsal/ventral axis specification IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in oocyte karyosome formation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in secondary piRNA processing IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in secondary piRNA processing IPI
Inferred from Physical Interaction
more info
 PubMed 
involved_in transposable element silencing by piRNA-mediated mRNA destabilization IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
is_active_in P granule IDA
Inferred from Direct Assay
more info
 PubMed 
located_in P granule IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytoplasmic ribonucleoprotein granule IEA
Inferred from Electronic Annotation
more info
  
located_in perinuclear region of cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in perinuclear region of cytoplasm IEA
Inferred from Electronic Annotation
more info
  
Preferred Names
krimper
Names
CG15707-PA
krimp-PA
montecristo

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NT_033778.4 Reference assembly

    Range
    16238103..16240722 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_137259.4 → NP_611103.2  krimper

    See identical proteins and their annotated locations for NP_611103.2

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    A1ZAC4
    UniProtKB/TrEMBL
    L0CRJ2
    Related
    FBpp0086333
    Conserved Domains (2) summary
    cd04508
    Location:618 → 662
    TUDOR; Tudor domains are found in many eukaryotic organisms and have been implicated in protein-protein interactions in which methylated protein substrates bind to these domains. For example, the Tudor domain of Survival of Motor Neuron (SMN) binds to ...
    pfam00567
    Location:568 → 679
    TUDOR; Tudor domain
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
A1ZAC4 A1ZAC4
Q8IGM1 Q8IGM1
Q95TQ3 Q95TQ3

Gene LinkOut

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