ID F1LMG4_RAT Unreviewed; 1074 AA. AC F1LMG4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 2. DT 27-MAR-2024, entry version 83. DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376}; DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376}; GN Name=Pld1 {ECO:0000313|Ensembl:ENSRNOP00000034466.4, GN ECO:0000313|RGD:3349}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000034466.4, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000034466.4, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000034466.4, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0007829|PubMed:22673903} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [3] {ECO:0000313|Ensembl:ENSRNOP00000034466.4} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000034466.4}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl- CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445, CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4; CC Evidence={ECO:0000256|PIRNR:PIRNR009376}; CC -!- SIMILARITY: Belongs to the phospholipase D family. CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}. 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 RefSeq; XP_006232267.1; XM_006232205.3. DR RefSeq; XP_006232268.1; XM_006232206.3. DR RefSeq; XP_017446126.1; XM_017590637.1. DR AlphaFoldDB; F1LMG4; -. DR SMR; F1LMG4; -. DR Ensembl; ENSRNOT00000039296.7; ENSRNOP00000034466.4; ENSRNOG00000028156.7. DR GeneID; 25096; -. DR CTD; 5337; -. DR RGD; 3349; Pld1. DR GeneTree; ENSGT00940000155015; -. DR OMA; EWRLDQI; -. DR OrthoDB; 335467at2759; -. DR TreeFam; TF300589; -. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000028156; Expressed in duodenum and 20 other cell types or tissues. DR ExpressionAtlas; F1LMG4; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl. DR GO; GO:0098981; C:cholinergic synapse; IEA:Ensembl. DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl. DR GO; GO:0005768; C:endosome; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule. DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro. DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule. DR GO; GO:0031670; P:cellular response to nutrient; IEA:Ensembl. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro. DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl. DR GO; GO:0032534; P:regulation of microvillus assembly; IEA:Ensembl. DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IEA:Ensembl. DR CDD; cd01254; PH_PLD; 1. DR CDD; cd09842; PLDc_vPLD1_1; 1. DR CDD; cd09844; PLDc_vPLD1_2; 1. DR CDD; cd07296; PX_PLD1; 1. DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3. DR Gene3D; 3.30.1520.10; Phox-like domain; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR025202; PLD-like_dom. DR InterPro; IPR001736; PLipase_D/transphosphatidylase. DR InterPro; IPR016555; PLipase_D_euk. DR InterPro; IPR015679; PLipase_D_fam. DR InterPro; IPR001683; PX_dom. DR InterPro; IPR036871; PX_dom_sf. DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1. DR PANTHER; PTHR18896:SF57; PHOSPHOLIPASE D1; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00614; PLDc; 1. DR Pfam; PF13091; PLDc_2; 1. DR Pfam; PF00787; PX; 1. DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00155; PLDc; 2. DR SMART; SM00312; PX; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF56024; Phospholipase D/nuclease; 3. DR SUPFAM; SSF64268; PX domain; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50035; PLD; 2. DR PROSITE; PS50195; PX; 1. PE 1: Evidence at protein level; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376}; KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, KW ECO:0000256|PIRNR:PIRNR009376}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963, KW ECO:0000256|PIRNR:PIRNR009376}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}. FT DOMAIN 81..212 FT /note="PX" FT /evidence="ECO:0000259|PROSITE:PS50195" FT DOMAIN 219..328 FT /note="PH" FT /evidence="ECO:0000259|PROSITE:PS50003" FT DOMAIN 459..486 FT /note="PLD phosphodiesterase" FT /evidence="ECO:0000259|PROSITE:PS50035" FT DOMAIN 891..918 FT /note="PLD phosphodiesterase" FT /evidence="ECO:0000259|PROSITE:PS50035" SQ SEQUENCE 1074 AA; 123786 MW; 17560B13BF580A87 CRC64; MSLKSEARVN TSTLQKIAAD MSNLIENLDT RELHFEGEEV EYDASPGDPT AQEACIPFSS IYNTQGFKEP NIQIYLSGCP VKAQVLEVER FTSTSRMPSV NLYTIELTHG EFTWQVKRKF KHFQEFHREL LKYKAFIRIP IPTKRHTFRR QNVKEEPREM PSLPRSSENA IQEEQFFGRR KQLEDYLTKI LKMPMYRNYH ATTEFLDVSQ LSFIHDLGPK GLEGMIMKRS GGHRIPGVNC CGHGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFRIKVGKKE TETKYGLRID NLSRTLILKC NSYRHARWWG GAIEEFIQKH GTDFLKDHRF GSYAAVHENI LAKWYVNAKG YFEDIANAME GATEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY KEVELALGIN SEYTKRTLMR LHPNIKVMRH PDHVSSSVYL WAHHEKLVII DQSVAFVGGI DLAYGRWDDN EHRLTDVGSV KRVTSGQSLG SLTAASVESM ESLSLKDKHQ SHKNEPVLKS VNDTDMKLKG IGKSRKFSKF SLYRQLHRRN LHNSDSISSV DSASSYFNHY RSHQNLIHGL KPHLKLFRPS SESEQGLTRH SADTGSIRSV QTGVGELHGE TRFWHGKDYC NFVFKDWVQL DKPFADFIDR YSTPRMPWHD IGSVVHGKAA RDVARHFIQR WNFTKIMKPK YRSLSYPFLL PKSQATAHEL RYQVPGAVHA KAQLLRSAAD WSAGIKHHEE SIHAAYTHVI ENSKHYIYIE NQFFISCADD KVVFNKVGNA IAQRILKAHR EGQRYRVYIV IPLLPGFEGD ISTGGGNALQ AIMHFNYRTM CRGESSILEQ LKPELGNKWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGR FAQGLRLECF RLVLGYLSDP SEDIQDPVSD KFFKEIWVST AARNATIYDK VFRCLPNDEV HNLIQLRDFI NKPILAKEDR LRAEEELRKI RGFLVQFPFY FLSEENLLPS VGTKEAIVPM EVWT //