Mitochondrial cardiolipin hydrolase

UniProt data

UniProt name: PLD6_HUMAN (Q8N2A8)

Gene name: PLD6

Organism: Homo sapiens (Human).

Function: Endonuclease that plays a critical role in PIWI- interacting RNA (piRNA) biogenesis during spermatogenesis. piRNAs provide essential protection against the activity of mobile genetic elements (By similarity). piRNA-mediated transposon silencing is thus critical for maintaining genome stability, in particular in germline cells when transposons are mobilized as a consequence of wide-spread genomic demethylation (By similarity). Has been proposed to act as a cardiolipin hydrolase to generate phosphatidic acid at mitochondrial surface (By similarity). Although it cannot be excluded that it can act as a phospholipase in some circumstances, it should be noted that cardiolipin hydrolase activity is either undetectable in vitro, or very low (PubMed:21397848). In addition, cardiolipin is almost exclusively found on the inner mitochondrial membrane, while PLD6 localizes to the outer mitochondrial membrane, facing the cytosol (PubMed:21397848). Has been shown to be a backbone-non-specific, single strand-specific nuclease, cleaving either RNA or DNA substrates with similar affinity. Produces 5' phosphate and 3' hydroxyl termini, suggesting it could directly participate in the processing of primary piRNA transcripts (By similarity). Also acts as a regulator of mitochondrial shape through facilitating mitochondrial fusion (PubMed:17028579, PubMed:26711011). {ECO:0000250|UniProtKB:Q5SWZ9, ECO:0000269|PubMed:17028579, ECO:0000269|PubMed:21397848, ECO:0000269|PubMed:26711011}.

Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:17028579}; Single-pass membrane protein {ECO:0000269|PubMed:17028579}.

Transmembrane domains:

  1. 5-27, 23 AA, Helical. {ECO:0000255}.

Sequence: 252 AA

10 20 30 40 50 60 MGRLSWQVAA AAAVGLALTL EALPWVLRWL RSRRRRPRRE ALFFPSQVTC TEALLRAPGA 70 80 90 100 110 120 ELAELPEGCP CGLPHGESAL SRLLRALLAA RASLDLCLFA FSSPQLGRAV QLLHQRGVRV 130 140 150 160 170 180 RVVTDCDYMA LNGSQIGLLR KAGIQVRHDQ DPGYMHHKFA IVDKRVLITG SLNWTTQAIQ 190 200 210 220 230 240 NNRENVLITE DDEYVRLFLE EFERIWEQFN PTKYTFFPPK KSHGSCAPPV SRAGGRLLSW 250 HRTCGTSSES QT

CATM prediction

The sequence of PLD6_HUMAN returned 1 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
          10        20        3
   +    |    +    |    +    |
(Å) (°) (Å) (°)  
GRLSWQVAAAAAVGLALTLEALAWVLRWL 7.0 -51.0° 3.3 48.0 -7.7
GRLSWQVAAAAAVGLALTLEALPWVLRWL          

* Note: this sequence contains Pro residues. CATM substituted them with Ala during the modeling. The positions are marked.

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


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Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 12, ALA, HA A, 11, ALA, O 3.00Å
B, 15, GLY, HA1 A, 12, ALA, O 3.04Å
B, 16, LEU, HA A, 19, THR, OG1 2.75Å
A, 12, ALA, HA B, 11, ALA, O 3.00Å
A, 15, GLY, HA1 B, 12, ALA, O 3.04Å
A, 16, LEU, HA B, 19, THR, OG1 2.75Å