PLD6_CHLRE
ID PLD6_CHLRE Reviewed; 223 AA.
AC A8IW99;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Mitochondrial cardiolipin hydrolase;
DE EC=3.1.-.-;
DE AltName: Full=Phospholipase D6 homolog;
DE Short=PLD 6;
GN ORFNames=CHLREDRAFT_190403;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503, and cw92;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
CC -!- FUNCTION: Plays a critical role in PIWI-interacting RNA (piRNA)
CC biogenesis (By similarity). piRNAs provide essential protection against
CC the activity of mobile genetic elements. piRNA-mediated transposon
CC silencing is thus critical for maintaining genome stability. Backbone-
CC non-specific, single strand-specific nuclease, cleaving either RNA or
CC DNA substrates with similar affinity (By similarity). Produces 5'
CC phosphate and 3' hydroxyl termini, suggesting it could directly
CC participate in the processing of primary piRNA transcripts (By
CC similarity). Has been proposed to act as a cardiolipin hydrolase to
CC generate phosphatidic acid at mitochondrial surface. Although it cannot
CC be excluded that it can act as a phospholipase in some circumstances,
CC this activity could not be confirmed (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
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}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. MitoPLD/Zucchini
CC subfamily. {ECO:0000305}.
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DR EMBL; DS496125; EDP03649.1; -; Genomic_DNA.
DR RefSeq; XP_001693080.1; XM_001693028.1.
DR AlphaFoldDB; A8IW99; -.
DR SMR; A8IW99; -.
DR STRING; 3055.EDP03649; -.
DR PaxDb; A8IW99; -.
DR EnsemblPlants; PNW74265; PNW74265; CHLRE_13g591900v5.
DR GeneID; 5718656; -.
DR Gramene; PNW74265; PNW74265; CHLRE_13g591900v5.
DR KEGG; cre:CHLRE_13g591900v5; -.
DR eggNOG; ENOG502RXG9; Eukaryota.
DR HOGENOM; CLU_080814_0_1_1; -.
DR InParanoid; A8IW99; -.
DR OMA; QPFIKEF; -.
DR OrthoDB; 1489926at2759; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF13091; PLDc_2; 1.
DR PROSITE; PS50035; PLD; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Lipid degradation; Lipid metabolism; Meiosis;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Nuclease; Transmembrane; Transmembrane helix.
FT CHAIN 1..223
FT /note="Mitochondrial cardiolipin hydrolase"
FT /id="PRO_0000408334"
FT TOPO_DOM 1..6
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 164..191
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
SQ SEQUENCE 223 AA; 24524 MW; D46BA857189A6FD2 CRC64;
MGCASSKEEV ALTPLSDVNA AKEVADLKAQ VDQLKRQLAS AGQSAAPAAA GAVKGGVVET
LFFPDEKLPC RNNRRPGGCK RQHCEYSHTP TSLSRFLDYL GSATRTLDIC VFTITNDDIS
DVVLELHNKG VRVRIISDND QAHTQGSDID KFRQAGIAVR QDKTAAHMHH KFAIIDGRLL
LNGSFNWTRQ AVTANNENVT VLSDPKLIAS FQQQFDKLWD MFK
