ID   A0AAN8H5K4_CHAGU        Unreviewed;       279 AA.
AC   A0AAN8H5K4;
DT   02-OCT-2024, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2024, sequence version 1.
DT   27-NOV-2024, entry version 2.
DE   RecName: Full=Phospholipid phosphatase 1 {ECO:0000256|ARBA:ARBA00021834};
DE            EC=3.1.3.106 {ECO:0000256|ARBA:ARBA00012497};
DE            EC=3.1.3.4 {ECO:0000256|ARBA:ARBA00012638};
DE            EC=3.6.1.75 {ECO:0000256|ARBA:ARBA00038902};
DE   AltName: Full=Lipid phosphate phosphohydrolase 1 {ECO:0000256|ARBA:ARBA00030630};
DE   AltName: Full=PAP2-alpha {ECO:0000256|ARBA:ARBA00032601};
DE   AltName: Full=Phosphatidate phosphohydrolase type 2a {ECO:0000256|ARBA:ARBA00030413};
DE   AltName: Full=Phosphatidic acid phosphatase 2a {ECO:0000256|ARBA:ARBA00031161};
GN   ORFNames=CgunFtcFv8_025317 {ECO:0000313|EMBL:KAK5900354.1};
OS   Champsocephalus gunnari (Mackerel icefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Channichthyidae; Champsocephalus.
OX   NCBI_TaxID=52237 {ECO:0000313|EMBL:KAK5900354.1, ECO:0000313|Proteomes:UP001331515};
RN   [1] {ECO:0000313|EMBL:KAK5900354.1, ECO:0000313|Proteomes:UP001331515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=White muscle {ECO:0000313|EMBL:KAK5900354.1};
RX   PubMed=36806940; DOI=10.1093/molbev/msad029;
RA   Rivera-Colon A.G., Rayamajhi N., Minhas B.F., Madrigal G., Bilyk K.T.,
RA   Yoon V., Hune M., Gregory S., Cheng C.H.C., Catchen J.M.;
RT   "Genomics of Secondarily Temperate Adaptation in the Only Non-Antarctic
RT   Icefish.";
RL   Mol. Biol. Evol. 40:msad029-msad029(2023).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-
CC         octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937,
CC         ChEBI:CHEBI:84973; Evidence={ECO:0000256|ARBA:ARBA00000974};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885;
CC         Evidence={ECO:0000256|ARBA:ARBA00000974};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-
CC         di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333,
CC         ChEBI:CHEBI:74546; Evidence={ECO:0000256|ARBA:ARBA00000980};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC         Evidence={ECO:0000256|ARBA:ARBA00000980};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-
CC         dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859,
CC         ChEBI:CHEBI:82929; Evidence={ECO:0000256|ARBA:ARBA00001611};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC         Evidence={ECO:0000256|ARBA:ARBA00001611};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-
CC         octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544,
CC         ChEBI:CHEBI:75757; Evidence={ECO:0000256|ARBA:ARBA00000235};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC         Evidence={ECO:0000256|ARBA:ARBA00000235};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC         H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate;
CC         Xref=Rhea:RHEA:41255, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:64839, ChEBI:CHEBI:75466;
CC         Evidence={ECO:0000256|ARBA:ARBA00023681};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41256;
CC         Evidence={ECO:0000256|ARBA:ARBA00023681};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(9Z-octadecenoyl)-ethanolamine phosphate + H2O = N-(9Z-
CC         octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466,
CC         ChEBI:CHEBI:145465; Evidence={ECO:0000256|ARBA:ARBA00001542};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161;
CC         Evidence={ECO:0000256|ARBA:ARBA00001542};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(octanoyl)-sphing-4-enine-1-phosphate + H2O = N-
CC         octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815,
CC         ChEBI:CHEBI:85376; Evidence={ECO:0000256|ARBA:ARBA00001710};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041;
CC         Evidence={ECO:0000256|ARBA:ARBA00001710};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monoacyl-sn-glycero-3-phosphate + H2O = a monoacylglycerol +
CC         phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589;
CC         Evidence={ECO:0000256|ARBA:ARBA00001476};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737;
CC         Evidence={ECO:0000256|ARBA:ARBA00001476};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sphing-4-enine 1-phosphate + H2O = sphing-4-enine + phosphate;
CC         Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57756, ChEBI:CHEBI:60119;
CC         Evidence={ECO:0000256|ARBA:ARBA00001716};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC         Evidence={ECO:0000256|ARBA:ARBA00001716};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC         glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00001180};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC         Evidence={ECO:0000256|ARBA:ARBA00001180};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + phosphate + H(+); Xref=Rhea:RHEA:27449,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.6.1.75;
CC         Evidence={ECO:0000256|ARBA:ARBA00035886};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450;
CC         Evidence={ECO:0000256|ARBA:ARBA00035886};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol +
CC         phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683;
CC         EC=3.1.3.106; Evidence={ECO:0000256|ARBA:ARBA00001472};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156;
CC         Evidence={ECO:0000256|ARBA:ARBA00001472};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-
CC         enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674;
CC         Evidence={ECO:0000256|ARBA:ARBA00023977};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744;
CC         Evidence={ECO:0000256|ARBA:ARBA00023977};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00005074}.
CC   -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC   -!- SUBUNIT: Forms functional homodimers and homooligomers that are not
CC       required for substrate recognition and catalytic activity. Can also
CC       form heterooligomers with PLPP2 and PLPP3.
CC       {ECO:0000256|ARBA:ARBA00047093}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004424}. Membrane raft
CC       {ECO:0000256|ARBA:ARBA00004314}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004314}. Membrane, caveola
CC       {ECO:0000256|ARBA:ARBA00004189}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004189}.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family. {ECO:0000256|ARBA:ARBA00008816}.
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:KAK5900354.1}.
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DR   EMBL; JAURVH010001532; KAK5900354.1; -; Genomic_DNA.
DR   Proteomes; UP001331515; Unassembled WGS sequence.
DR   CDD; cd03384; PAP2_wunen; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR043216; PA_PP_rel.
DR   PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR   PANTHER; PTHR10165:SF26; PHOSPHOLIPID PHOSPHATASE 1; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        94..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        198..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        229..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          102..244
FT                   /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT                   /evidence="ECO:0000259|SMART:SM00014"
FT   REGION          258..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   279 AA;  31232 MW;  3D30B7585ADDABFC CRC64;
     MFEARGIPFV LLDITCLILG GLPLAAFNLG KVVPYQRGFF CSDDSLRYPF HSGTVTSTVL
     YTVGFTLPIG CMVIGECLLV YLERLKSKSS YGSYVSCVYK AVGTFLFGAA MSQSLTDIAK
     YSIGRLRPHF LDVCRPDWNL INCSVGDYIE TFACQGDAKM VNEGRLSFYS GHASFSMYCM
     LFLALYLQAR LQVEWARLLR PTMQFFLIAA SVFTGLSRVS DYKHHWSDVL TGLLQGAIMA
     LLVVFCVSDF FKPREAPRRE EDHTTLQETT NGNHCESPN
//