ID A0A151N1Z5_ALLMI Unreviewed; 127 AA.
AC A0A151N1Z5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Mitochondrial cardiolipin hydrolase {ECO:0000256|ARBA:ARBA00040549};
DE AltName: Full=Choline phosphatase 6 {ECO:0000256|ARBA:ARBA00042226};
DE AltName: Full=Mitochondrial phospholipase {ECO:0000256|ARBA:ARBA00043167};
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D6 {ECO:0000256|ARBA:ARBA00043135};
DE AltName: Full=Phospholipase D6 {ECO:0000256|ARBA:ARBA00041680};
GN Name=PLD6 {ECO:0000313|EMBL:KYO30780.1};
GN ORFNames=Y1Q_0008375 {ECO:0000313|EMBL:KYO30780.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO30780.1};
RN [1] {ECO:0000313|EMBL:KYO30780.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO30780.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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:0000256|ARBA:ARBA00036829};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44885;
CC Evidence={ECO:0000256|ARBA:ARBA00036829};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004572}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. MitoPLD/Zucchini
CC subfamily. {ECO:0000256|ARBA:ARBA00038012}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO30780.1}.
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; AKHW03004154; KYO30780.1; -; Genomic_DNA.
DR RefSeq; XP_019350193.1; XM_019494648.1.
DR AlphaFoldDB; A0A151N1Z5; -.
DR STRING; 8496.A0A151N1Z5; -.
DR KEGG; amj:109284904; -.
DR CTD; 201164; -.
DR eggNOG; ENOG502RXG9; Eukaryota.
DR OrthoDB; 1356899at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; 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 GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 1.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR43856; CARDIOLIPIN HYDROLASE; 1.
DR PANTHER; PTHR43856:SF1; MITOCHONDRIAL CARDIOLIPIN HYDROLASE; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR PROSITE; PS50035; PLD; 1.
PE 3: Inferred from homology;
KW Differentiation {ECO:0000256|ARBA:ARBA00022871};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000313|EMBL:KYO30780.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871}.
FT DOMAIN 56..83
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 127 AA; 14654 MW; DAA273FC2140F6B9 CRC64;
MRTNREATPW GGADTCAETR EPRAVERGAH AQKTMNQRGE GSHMRKGGIQ VRHDQESGYM
HHKFAIVDQK MLITGSLNWT TQAIQSNREN VLIVEDAEYV KPFLAEFERI WEEYNPANYT
FFPKGKK
//