PLD6_XENLA
ID PLD6_XENLA Reviewed; 210 AA.
AC A1L1C2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Mitochondrial cardiolipin hydrolase;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q5SWZ9};
DE AltName: Full=Choline phosphatase 6;
DE AltName: Full=Mitochondrial phospholipase {ECO:0000250|UniProtKB:Q8N2A8};
DE Short=MitoPLD {ECO:0000250|UniProtKB:Q8N2A8};
DE EC=3.1.4.- {ECO:0000250|UniProtKB:Q8N2A8};
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D6;
DE AltName: Full=Phospholipase D6;
DE Short=PLD 6;
GN Name=pld6;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Presents phospholipase and nuclease activities, depending on
CC the different physiological conditions. Plays a key role in
CC mitochondrial fusion and fission via its phospholipase activity. In its
CC phospholipase role, it uses the mitochondrial lipid cardiolipin as
CC substrate to generate phosphatidate (PA or 1,2-diacyl-sn-glycero-3-
CC phosphate), a second messenger signaling lipid. Production of PA
CC facilitates Mitofusin-mediated fusion, whereas the cleavage of PA by
CC the Lipin family of phosphatases produces diacylgycerol (DAG) which
CC promotes mitochondrial fission. Regulates mitochondrial shape through
CC facilitating mitochondrial fusion. During spermatogenesis, plays a
CC critical role in PIWI-interacting RNA (piRNA) biogenesis (By
CC similarity). piRNAs provide essential protection against the activity
CC of mobile genetic elements. piRNA-mediated transposon silencing is thus
CC critical for maintaining genome stability, in particular in germline
CC cells when transposons are mobilized as a consequence of wide-spread
CC genomic demethylation. Has been shown to be a backbone-non-specific,
CC single strand-specific nuclease, cleaving either RNA or DNA substrates
CC with similar affinity (By similarity). Produces 5' phosphate and 3'
CC hydroxyl termini, suggesting it could directly participate in the
CC processing of primary piRNA transcripts (By similarity). Has been
CC proposed to act as a cardiolipin hydrolase to generate phosphatidic
CC acid at mitochondrial surface. Although it cannot be excluded that it
CC can act as a phospholipase in some circumstances, this activity could
CC not be confirmed (By similarity). {ECO:0000250|UniProtKB:Q5SWZ9,
CC ECO:0000250|UniProtKB:Q8N2A8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cardiolipin + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-
CC glycerol) + a 1,2-diacyl-sn-glycero-3-phosphate + H(+);
CC Xref=Rhea:RHEA:44884, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716;
CC Evidence={ECO:0000250|UniProtKB:Q8N2A8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44885;
CC Evidence={ECO:0000250|UniProtKB:Q8N2A8};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q5SWZ9}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q5SWZ9}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5SWZ9}.
CC -!- DOMAIN: In contrast to other members of the phospholipase D family,
CC contains only one PLD phosphodiesterase domain, suggesting that it has
CC a single half-catalytic and requires homodimerization to form a
CC complete active site. {ECO:0000250|UniProtKB:Q8N2A8}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. MitoPLD/Zucchini
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC128979; AAI28980.1; -; mRNA.
DR RefSeq; NP_001091258.1; NM_001097789.1.
DR AlphaFoldDB; A1L1C2; -.
DR SMR; A1L1C2; -.
DR DNASU; 100037063; -.
DR GeneID; 100037063; -.
DR KEGG; xla:100037063; -.
DR CTD; 100037063; -.
DR Xenbase; XB-GENE-5729953; pld6.S.
DR OrthoDB; 1489926at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 100037063; Expressed in oocyte and 10 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0035755; F:cardiolipin hydrolase activity; ISS:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0030719; P:P granule organization; ISS:UniProtKB.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 1.
DR PROSITE; PS50035; PLD; 1.
PE 2: Evidence at transcript level;
KW Differentiation; Endonuclease; Hydrolase; Lipid degradation;
KW Lipid metabolism; Meiosis; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Nuclease; Reference proteome;
KW Spermatogenesis; Transmembrane; Transmembrane helix.
FT CHAIN 1..210
FT /note="Mitochondrial cardiolipin hydrolase"
FT /id="PRO_0000325913"
FT TOPO_DOM 1..5
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 138..165
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
SQ SEQUENCE 210 AA; 23919 MW; 3218D8C5018A1ACD CRC64;
MLLWGRWKLA AGLAGLALSL ELFYRYMRRR KPLREVLFFP VPVTCIEPVL SPMKQCSCPL
PHTDSAFSRL LVQLLGAQRS LELCVFTFSS PSLARALLIL HRRDVRVRVI TDNDYMAAPG
SQIGPLRSAG VAVRHDQSSG YMHHKFAVVD GTVVLTGSLN WTVQAFQSNK ENILITDDTV
IVKAYQKEFE RLWEEYDPAT YNFFPEKENK
