SG ID

SG00000313 

UniProt Accession

Q7KTX7_DROME;Q7KTX7;  

Theoretical PI

5.78  

Molecular Weight

54105 Da  

Genbank Nucleotide ID

AY093423; AF510072; AE014296; AE014296; BT044504;  

Genbank Protein ID

AAM18800.2; AAM43930.1; AAN12154.1; AAN12155.1; ACH95278.1; 

Gene Name

park 

Gene Synonyms/Alias

park-RC, parkin 

Protein Name

 

Protein Synonyms/Alias

SubName: FI05213pSubName: PARKINSubName: Parkin, isoform BEC=6.3.2.19SubName: Parkin, isoform CEC=6.3.2.19 

Drosophila melanogaster (Fruit fly) 

7227 

Temporarily unavailable 

The information of related literatures

1. M. G. Riparbelli and G. Callaini (2007) The Drosophila parkin homologue is required for normal mitochondrial dynamics during spermiogenesis. Dev Biol 303(1): 108-20. 

Abstract
Drosophila parkin, the ortholog of the human parkin gene, responsible for a familiar form of autosomal recessive juvenile parkinsonism, has been shown previously to be involved in Drosophila male fertility. Loss-of-function mutations in the parkin gene cause failure of spermatid individualization by affecting the proper progression of the actin-based investment cones that assemble in the nuclear region, but fail to translocate in synchrony down the cyst. In parkin mutants, the investment cones are scattered along the post-elongated spermatid bundles and fail to act properly in the process of sperm individualization. Using phase-contrast and electron microscopy analysis, we demonstrate that the parkin spermatids assemble a seemingly normal onion-stage nebenkern, but when the axoneme elongates only one mitochondrial derivative unfurls from the nebenkern. This unique mitochondrial derivative undergoes abnormal shaping and condensation during spermatid elongation. Our results indicate that parkin gene function is necessary for mitochondrial morphogenesis during earlier and later phases of spermiogenesis. The failure of cyst individualization may be due to the sensitivity of investment cone movement to the perturbation of mitochondrial morphology during spermatid elongation. PMID: [17123504] 

2. J. C. Greene, A. J. Whitworth, I. Kuo, L. A. Andrews, M. B. Feany and L. J. Pallanck (2003) Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants. Proc Natl Acad Sci U S A 100(7): 4078-83. 

Abstract
Parkinson's disease (PD) is a common neurodegenerative disorder characterized by loss of dopaminergic neurons in the substantia nigra. Several lines of evidence strongly implicate mitochondrial dysfunction as a major causative factor in PD, although the molecular mechanisms responsible for mitochondrial dysfunction are poorly understood. Recently, loss-of-function mutations in the parkin gene, which encodes a ubiquitin-protein ligase, were found to underlie a familial form of PD known as autosomal recessive juvenile parkinsonism (AR-JP). To gain insight into the molecular mechanism responsible for selective cell death in AR-JP, we have created a Drosophila model of this disorder. Drosophila parkin null mutants exhibit reduced lifespan, locomotor defects, and male sterility. The locomotor defects derive from apoptotic cell death of muscle subsets, whereas the male sterile phenotype derives from a spermatid individualization defect at a late stage of spermatogenesis. Mitochondrial pathology is the earliest manifestation of muscle degeneration and a prominent characteristic of individualizing spermatids in parkin mutants. These results indicate that the tissue-specific phenotypes observed in Drosophila parkin mutants result from mitochondrial dysfunction and raise the possibility that similar mitochondrial impairment triggers the selective cell loss observed in AR-JP. PMID: [12642658] 

Figures for illustrating the function of this protein/gene

Function

 

Subcellular Location

 

Tissue Specificity

 

Gene Ontology

GO ID	GO term	Evidence
GO:0005829	C:cytosol	IEA:InterPro.
GO:0005739	C:mitochondrion	IDA:FlyBase.
GO:0004842	F:ubiquitin-protein ligase activity	IDA:FlyBase.
GO:0008270	F:zinc ion binding	IEA:InterPro.
GO:0000266	P:mitochondrial fission	IGI:FlyBase.
GO:0046329	P:negative regulation of JNK cascade	IDA:FlyBase.
GO:0048477	P:oogenesis	IMP:FlyBase.
GO:0048078	P:positive regulation of compound eye pigmentation	IMP:BHF-UCL.
GO:0051865	P:protein autoubiquitination	IDA:FlyBase.
GO:0010821	P:regulation of mitochondrion organization	IMP:FlyBase.
GO:0006979	P:response to oxidative stress	IMP:FlyBase.
GO:0030382	P:sperm mitochondrion organization	IMP:FlyBase.
GO:0007283	P:spermatogenesis	IMP:FlyBase.

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Interpro

IPR003977;    Parkin.
IPR000626;    Ubiquitin.
IPR019955;    Ubiquitin_supergroup.
IPR002867;    Znf_C6HC.
IPR013083;    Znf_RING/FYVE/PHD.
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Pfam

PF01485;    IBR;    2.
PF00240;    ubiquitin;    1.
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SMART

SM00647;    IBR;    2.
SM00213;    UBQ;    1.
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PROSITE

PS50053;    UBIQUITIN_2;    1.
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PRINTS

PR01475;    PARKIN.;   
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Created Date

18-Oct-2012 

Record Type

Experiment identified 

Protein sequence Annotation

Nucleotide Sequence

Length: 1478 bp   Go to nucleotide: FASTA

Protein Sequence

Length: 482 bp   Go to amino acid: FASTA

The verified Protein-Protein interaction information

UniProt	Gene Symbol	Ref Databases
A1Z9T6_DROME	CG12860	IntAct
DLG1_DROME	dlg1	IntAct
MED9_DROME	MED9	IntAct
P23023-1	_	IntAct
Q7JWN2_DROME	CG13159	IntAct
Q7KJA9_DROME	sxc	BioGRID
A1Z9T6_DROME	CG12860	BioGRID
C1C536_DROME	dlg1	BioGRID
DLG1_DROME	dlg1	BioGRID
DSX_DROME	dsx	BioGRID
E1JJH5_DROME	dlg1	BioGRID
E1JJH6_DROME	dlg1	BioGRID
MED9_DROME	MED9	BioGRID
Q7JWN2_DROME	CG13159	BioGRID
Q9XTN4_DROME	brk	BioGRID
Q8INV9_DROME	Hakai	BioGRID
Q8INW0_DROME	Hakai	BioGRID
Q9VIT1_DROME	Hakai	BioGRID
Q9XTN4_DROME	brk	IntAct

Other Protein-Protein interaction resources

String database  

UniProt

Gene Symbol

Ref Databases

View Microarray data

Temporarily unavailable 

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