ID A0A1S3Q697_SALSA Unreviewed; 226 AA.
AC A0A1S3Q697;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=LOC106589682 {ECO:0000313|RefSeq:XP_014035427.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014035427.1};
RN [1] {ECO:0000313|RefSeq:XP_014035427.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014035427.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR RefSeq; XP_014035427.1; XM_014179952.1.
DR AlphaFoldDB; A0A1S3Q697; -.
DR GeneID; 106589682; -.
DR OrthoDB; 1356899at2759; -.
DR Proteomes; UP000087266; Chromosome ssa02.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd09171; PLDc_vPLD6_like; 1.
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 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:0000256|ARBA:ARBA00022801,
KW ECO:0000313|RefSeq:XP_014035427.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 149..176
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 226 AA; 25145 MW; 8433E103C5539509 CRC64;
MSVVQMVKIV GLGAVALTLS VEWLGWLFCR LWPRKISRGP LKEVFFFPTE VACTERLFTP
DSPFPCPCPL PHNVNTSFTR LLGHILSASS SLDLCVFAFT NLDLSRAVLA LHARGIPIRI
LTDMDYTLIT GSQIGAIRRA GICVRCDSGA VHMHHKFAVV DGRRLITGSL NWTLTAIQSN
KENILVTEEP DLVLPFITEF QRLWDVNDPA RRHLPSIAEK TASLVL
//