ID PLD3_MACFA Reviewed; 490 AA. AC Q4R583; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 24-MAR-2009, entry version 24. DE RecName: Full=Phospholipase D3; DE Short=PLD 3; DE EC=3.1.4.4; DE AltName: Full=Choline phosphatase 3; DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D3; GN Name=PLD3; ORFNames=QccE-15167; OS Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG International consortium for macaque cDNA sequencing and analysis; RT "DNA sequences of macaque genes expressed in brain or testis and its RT evolutionary implications."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a CC phosphatidate. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC type II membrane protein (By similarity). CC -!- PTM: Glycosylated (By similarity). CC -!- SIMILARITY: Belongs to the phospholipase D family. CC -!- SIMILARITY: Contains 2 PLD phosphodiesterase domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB169661; BAE01742.1; -; mRNA. DR HOVERGEN; Q4R583; -. DR BRENDA; 3.1.4.4; 3438. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0070290; F:NAPE-specific phospholipase D activity; IEA:EC. DR GO; GO:0004630; F:phospholipase D activity; IEA:EC. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR InterPro; IPR013582; PLD_envelope. DR InterPro; IPR001736; PLipase_D/transphosphatidylase. DR Pfam; PF08371; PLD_envelope; 1. DR Pfam; PF00614; PLDc; 2. DR SMART; SM00155; PLDc; 2. DR PROSITE; PS50035; PLD; 2. PE 2: Evidence at transcript level; KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid degradation; KW Membrane; Repeat; Signal-anchor; Transmembrane. FT CHAIN 1 490 Phospholipase D3. FT /FTId=PRO_0000280327. FT TOPO_DOM 1 38 Cytoplasmic (Potential). FT TRANSMEM 39 59 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 60 490 Lumenal (Potential). FT DOMAIN 196 223 PLD phosphodiesterase 1. FT DOMAIN 411 437 PLD phosphodiesterase 2. FT ACT_SITE 201 201 Potential. FT ACT_SITE 203 203 Potential. FT ACT_SITE 208 208 Potential. FT CARBOHYD 132 132 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 490 AA; 54852 MW; ED2891E1920AB9DF CRC64; MKPKLMYQEL KVPAEEPANE LPMNEIEAWK AAEKKARWVL LVLILAVVGF GALMTQLFLW EYGDLHLFGP NQRPAPCYDP CEAVLVESIP EGLDFPNAST GNPSTSQAWL GLLAGAHSSL DIASFYWTLT NNDTHTQEPS AQQGEEVLRQ LQTLAPKGVN VRIAVSKPNG PQPQTDLQAL LQSGAQVRMV DMQKLTHGVL HTKFWVVDQT HFYLGSANMD WRSLTQVKEL GVVMYNCSCL ARDLTKIFEA YWFLGQAGSS IPSTWPRFYD TRYNQETPME ICLNGTPALA YLASAPPPLC PSGRTPDLKA LLNVVDNARS FIYIAVMNYL PTLEFSHPHR FWPAIDDGLR RAAYERGVKV RLLVSCWRHS ESSMRAFLLS LAALRDNHTH SDIQVKLFVV PADEAQARIP YARVNHNKYM VTERATYIGT SNWSGNYFTE TAGTSLLVMQ NGRGSLRSQL EAIFLRDWDS PYSHDLDASA DSVGNACRLL //