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Protein

Mitochondrial cardiolipin hydrolase

Gene

zuc

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cardiolipin hydrolase present at the mitochondrial outer membrane required for piRNA metabolic process. Acts by catalyzing the hydrolysis of cardiolipin (diphosphatidylglycerol) to form phosphatidate (phosphatidic acid or PA) at the mitochondrial outer membrane surface, promoting the piRNA metabolic process. Plays a key role in primary biogenesis of piRNAs and is required during oogenesis to repress transposable elements and prevent their mobilization. piRNAs mediate the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Involved in trans-silencing effect (TSE), a homology-dependent repression mechanism by which a P-transgene inserted in subtelomeric heterochromatin via its role in piRNA biogenesis.7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei169Curated1
Active sitei171Sequence analysis1
Active sitei176Sequence analysis1

GO - Molecular functioni

  • cardiolipin hydrolase activity Source: UniProtKB
  • cardiolipin synthase activity Source: GO_Central
  • endoribonuclease activity, producing 5'-phosphomonoesters Source: FlyBase

GO - Biological processi

  • cardiolipin biosynthetic process Source: GO_Central
  • dorsal appendage formation Source: FlyBase
  • gene silencing by RNA Source: FlyBase
  • karyosome formation Source: FlyBase
  • lipid catabolic process Source: UniProtKB-KW
  • meiotic cell cycle Source: UniProtKB-KW
  • oogenesis Source: FlyBase
  • piRNA metabolic process Source: UniProtKB
  • RNA phosphodiester bond hydrolysis, endonucleolytic Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Differentiation, Lipid degradation, Lipid metabolism, Meiosis, Oogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial cardiolipin hydrolase (EC:3.1.4.-)
Alternative name(s):
Mitochondrial phospholipaseBy similarity
Short name:
MitoPLDBy similarity
Protein zucchini1 Publication
Gene namesi
Name:zuc1 PublicationImported
ORF Names:CG12314Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0261266. zuc.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 13Mitochondrial intermembraneSequence analysisAdd BLAST13
Transmembranei14 – 30HelicalSequence analysisAdd BLAST17
Topological domaini31 – 253CytoplasmicSequence analysisAdd BLAST223

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: GO_Central
  • mitochondrion Source: UniProtKB
  • P granule Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Disruption phenotypei

Defects in mid oogenesis. Females are viable but produce eggs with a range of dorso-ventral patterning defects. Flies lay few eggs, all of which are completely ventralized and often collapsed. Effects are due to defects in piRNA biogenesis and derepression of retrotransposons. Defects are not only present in germ cells but also in somatic cells of the ovary.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi47A → D in zuc(RS49); produce some eggs with a more normal eggshell phenotype in addition to the ventralized eggs compared to null mutants. 1 Publication1
Mutagenesisi169H → N: Abolishes cardiolipin hydrolase activity. 2 Publications1
Mutagenesisi169H → Y in zuc(SG63); produce some eggs with a more normal eggshell phenotype in addition to the ventralized eggs compared to null mutants. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004083351 – 253Mitochondrial cardiolipin hydrolaseAdd BLAST253

Proteomic databases

PaxDbiQ9VKD7.
PRIDEiQ9VKD7.

Expressioni

Gene expression databases

BgeeiFBgn0261266.
GenevisibleiQ9VKD7. DM.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with miga/CG12125 (PubMed:26711011).By similarity1 Publication

Protein-protein interaction databases

DIPiDIP-59983N.
IntActiQ9VKD7. 1 interactor.
STRINGi7227.FBpp0079900.

Structurei

Secondary structure

1253
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi42 – 47Combined sources6
Beta strandi51 – 56Combined sources6
Turni58 – 63Combined sources6
Helixi64 – 67Combined sources4
Helixi69 – 72Combined sources4
Helixi89 – 101Combined sources13
Beta strandi104 – 110Combined sources7
Helixi117 – 129Combined sources13
Beta strandi132 – 136Combined sources5
Turni139 – 143Combined sources5
Helixi148 – 154Combined sources7
Beta strandi159 – 161Combined sources3
Beta strandi164 – 166Combined sources3
Beta strandi172 – 176Combined sources5
Helixi178 – 187Combined sources10
Beta strandi199 – 204Combined sources6
Helixi209 – 213Combined sources5
Beta strandi215 – 222Combined sources8
Helixi225 – 241Combined sources17
Beta strandi242 – 244Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GELX-ray1.76A/B41-253[»]
4GEMX-ray2.21A/B41-253[»]
4GENX-ray2.20A89-250[»]
4H4AX-ray2.20A89-253[»]
ProteinModelPortaliQ9VKD7.
SMRiQ9VKD7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini164 – 211PLD phosphodiesteraseAdd BLAST48

Domaini

In contrast to other members of the phospholipase D family, contains only one PLD phosphodiesterase domain, suggesting that it has a single half-catalytic and requires homodimerization to form a complete active site.By similarity

Sequence similaritiesi

Contains 1 PLD phosphodiesterase domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J0H4. Eukaryota.
COG1502. LUCA.
GeneTreeiENSGT00390000004368.
InParanoidiQ9VKD7.
KOiK16862.
OMAiASEVIWK.
OrthoDBiEOG091G0FI5.
PhylomeDBiQ9VKD7.

Family and domain databases

InterProiIPR025202. PLD-like_dom.
[Graphical view]
PfamiPF13091. PLDc_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VKD7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLITQIIMKQ IRDYPIVSTI SIAVSTVLAS EVIWKLVQCS RSKREKASRV
60 70 80 90 100
HEVIIFNELG EICAAVHMRN SSMGSQKPQV SPCCNTHCSL RNVAKIVEQI
110 120 130 140 150
DRAVYSIDLA IYTFTSLFLA DSIKRALQRG VIIRIISDGE MVYSKGSQIS
160 170 180 190 200
MLAQLGVPVR VPITTNLMHN KFCIIDGFER VEEIRLLRKL KFMRPCYSIV
210 220 230 240 250
ISGSVNWTAL GLGGNWENCI ITADDKLTAT FQAEFQRMWR AFAKTEGSQI

QLK
Length:253
Mass (Da):28,520
Last modified:May 1, 2000 - v1
Checksum:i4488BEA6DFF9E092
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti2L → V in strain: MEL20, ZBMEL131, ZBMEL186, ZBMEL384 and ZBMEL398. 1
Natural varianti225D → E in strain: =MEL01, MEL02, MEL11, MEL12, MEL14, MEL15, MEL16, MEL17, MEL18, MEL19, MEL20, ZBMEL82, ZBMEL95, ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229, ZBMEL377, ZBMEL384 and ZBMEL398. 1
Natural varianti252L → V in strain: ZBMEL191, ZBMEL229, ZBMEL377 and ZBMEL384. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM294430 Genomic DNA. Translation: CAL26369.1.
AM294431 Genomic DNA. Translation: CAL26370.1.
AM294432 Genomic DNA. Translation: CAL26371.1.
AM294433 Genomic DNA. Translation: CAL26372.1.
AM294434 Genomic DNA. Translation: CAL26373.1.
AM294435 Genomic DNA. Translation: CAL26374.1.
AM294436 Genomic DNA. Translation: CAL26375.1.
AM294437 Genomic DNA. Translation: CAL26377.1.
AM294438 Genomic DNA. Translation: CAL26381.1.
AM294439 Genomic DNA. Translation: CAL26382.1.
AM294440 Genomic DNA. Translation: CAL26383.1.
FM245502 Genomic DNA. Translation: CAR93428.1.
FM245503 Genomic DNA. Translation: CAR93429.1.
FM245504 Genomic DNA. Translation: CAR93430.1.
FM245505 Genomic DNA. Translation: CAR93431.1.
FM245506 Genomic DNA. Translation: CAR93432.1.
FM245507 Genomic DNA. Translation: CAR93433.1.
FM245508 Genomic DNA. Translation: CAR93434.1.
FM245509 Genomic DNA. Translation: CAR93435.1.
FM245510 Genomic DNA. Translation: CAR93436.1.
FM245511 Genomic DNA. Translation: CAR93437.1.
FM245512 Genomic DNA. Translation: CAR93438.1.
FM245513 Genomic DNA. Translation: CAR93439.1.
AE014134 Genomic DNA. Translation: AAF53139.1.
AY118493 mRNA. Translation: AAM49862.1.
RefSeqiNP_609530.1. NM_135686.3.
UniGeneiDm.11087.

Genome annotation databases

EnsemblMetazoaiFBtr0080316; FBpp0079900; FBgn0261266.
GeneIDi34609.
KEGGidme:Dmel_CG12314.
UCSCiCG12314-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM294430 Genomic DNA. Translation: CAL26369.1.
AM294431 Genomic DNA. Translation: CAL26370.1.
AM294432 Genomic DNA. Translation: CAL26371.1.
AM294433 Genomic DNA. Translation: CAL26372.1.
AM294434 Genomic DNA. Translation: CAL26373.1.
AM294435 Genomic DNA. Translation: CAL26374.1.
AM294436 Genomic DNA. Translation: CAL26375.1.
AM294437 Genomic DNA. Translation: CAL26377.1.
AM294438 Genomic DNA. Translation: CAL26381.1.
AM294439 Genomic DNA. Translation: CAL26382.1.
AM294440 Genomic DNA. Translation: CAL26383.1.
FM245502 Genomic DNA. Translation: CAR93428.1.
FM245503 Genomic DNA. Translation: CAR93429.1.
FM245504 Genomic DNA. Translation: CAR93430.1.
FM245505 Genomic DNA. Translation: CAR93431.1.
FM245506 Genomic DNA. Translation: CAR93432.1.
FM245507 Genomic DNA. Translation: CAR93433.1.
FM245508 Genomic DNA. Translation: CAR93434.1.
FM245509 Genomic DNA. Translation: CAR93435.1.
FM245510 Genomic DNA. Translation: CAR93436.1.
FM245511 Genomic DNA. Translation: CAR93437.1.
FM245512 Genomic DNA. Translation: CAR93438.1.
FM245513 Genomic DNA. Translation: CAR93439.1.
AE014134 Genomic DNA. Translation: AAF53139.1.
AY118493 mRNA. Translation: AAM49862.1.
RefSeqiNP_609530.1. NM_135686.3.
UniGeneiDm.11087.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GELX-ray1.76A/B41-253[»]
4GEMX-ray2.21A/B41-253[»]
4GENX-ray2.20A89-250[»]
4H4AX-ray2.20A89-253[»]
ProteinModelPortaliQ9VKD7.
SMRiQ9VKD7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59983N.
IntActiQ9VKD7. 1 interactor.
STRINGi7227.FBpp0079900.

Proteomic databases

PaxDbiQ9VKD7.
PRIDEiQ9VKD7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080316; FBpp0079900; FBgn0261266.
GeneIDi34609.
KEGGidme:Dmel_CG12314.
UCSCiCG12314-RA. d. melanogaster.

Organism-specific databases

CTDi34609.
FlyBaseiFBgn0261266. zuc.

Phylogenomic databases

eggNOGiENOG410J0H4. Eukaryota.
COG1502. LUCA.
GeneTreeiENSGT00390000004368.
InParanoidiQ9VKD7.
KOiK16862.
OMAiASEVIWK.
OrthoDBiEOG091G0FI5.
PhylomeDBiQ9VKD7.

Miscellaneous databases

GenomeRNAii34609.
PROiQ9VKD7.

Gene expression databases

BgeeiFBgn0261266.
GenevisibleiQ9VKD7. DM.

Family and domain databases

InterProiIPR025202. PLD-like_dom.
[Graphical view]
PfamiPF13091. PLDc_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiZUC_DROME
AccessioniPrimary (citable) accession number: Q9VKD7
Secondary accession number(s): A0AP42
, A0AP43, A0AP44, A0AP47, A0AP48, A0AP51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.