ID A0A099ZUP7_TINGU Unreviewed; 266 AA. AC A0A099ZUP7; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 02-OCT-2024, entry version 34. 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}; DE Flags: Fragment; GN ORFNames=N309_08666 {ECO:0000313|EMBL:KGL85531.1}; OS Tinamus guttatus (White-throated tinamou). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus. OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL85531.1, ECO:0000313|Proteomes:UP000053641}; RN [1] {ECO:0000313|EMBL:KGL85531.1, ECO:0000313|Proteomes:UP000053641} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL85531.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. 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=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = 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=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = 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=H2O + monoacyl-sn-glycero-3-phosphate = 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=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine; 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 + H(+) + phosphate; 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 -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004424}. Cell membrane CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004651}. 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}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase CC family. {ECO:0000256|ARBA:ARBA00008816}. 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; KL898626; KGL85531.1; -; Genomic_DNA. DR AlphaFoldDB; A0A099ZUP7; -. DR STRING; 94827.A0A099ZUP7; -. DR UniPathway; UPA00085; -. DR Proteomes; UP000053641; Unassembled WGS sequence. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell. DR GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046839; P:phospholipid dephosphorylation; IEA:TreeGrafter. DR GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0007165; P:signal transduction; IEA:TreeGrafter. 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KGL85531.1}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053641}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 41..64 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 76..94 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 148..168 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 180..199 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 211..233 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 85..226 FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase" FT /evidence="ECO:0000259|SMART:SM00014" FT REGION 246..266 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 251..266 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:KGL85531.1" FT NON_TER 266 FT /evidence="ECO:0000313|EMBL:KGL85531.1" SQ SEQUENCE 266 AA; 29806 MW; E7DCC4CCB204CC67 CRC64; LLAGLPFAIL NSRRIPFQRG VFCSDDSIRY PYKEDTISYK LLAGIIVPFC IIVIIVGETL SVSYNHLHSN SFVRNSYIAT IYKAIGTFIF GAAASQSLTD IAKYSIGRLR PHFLAVCQPD WARINCTLGY VENFLCQGDK AKINEGRLSF YSGHSSFSMY CMLFLALYLQ ARMKGDWARL VRPTLQFALV AASIYVGLSR VSDYKHHWSD VLTGLIQGAV VAVLIVLYVS DFFKVRACTF QPKEDSHTTL HETPTNGNHF GSNHQP //