ID A0A099ZUP7_TINGU Unreviewed; 266 AA. AC A0A099ZUP7; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 03-MAY-2023, entry version 28. DE SubName: Full=Lipid phosphate phosphohydrolase 1 {ECO:0000313|EMBL:KGL85531.1}; 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {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:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0006644; P:phospholipid metabolic process; IEA:UniProtKB-UniPathway. 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 Hydrolase {ECO:0000313|EMBL:KGL85531.1}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053641}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW 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 //