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}. 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; 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 //