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Phospholipase D1 (PLD 1) (EC 3.1.4.4) (Choline phosphatase 1) (Meiosis-specific sporulation-specific protein 14) (Phosphatidylcholine-hydrolyzing phospholipase D1)

 SPO14_YEAST             Reviewed;        1683 AA.
P36126; D6VX96;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 3.
22-NOV-2017, entry version 165.
RecName: Full=Phospholipase D1;
Short=PLD 1;
EC=3.1.4.4;
AltName: Full=Choline phosphatase 1;
AltName: Full=Meiosis-specific sporulation-specific protein 14;
AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D1;
Name=SPO14; Synonyms=PLD1; OrderedLocusNames=YKR031C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=1582554;
Honigberg S.M., Conicella C., Espositio R.E.;
"Commitment to meiosis in Saccharomyces cerevisiae: involvement of the
SPO14 gene.";
Genetics 130:703-716(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
CHARACTERIZATION AS A PLD.
PubMed=8618862; DOI=10.1073/pnas.92.26.12151;
Rose K., Rudge S.A., Frohman M.A., Morris A.J., Engebrecht J.;
"Phospholipase D signaling is essential for meiosis.";
Proc. Natl. Acad. Sci. U.S.A. 92:12151-12155(1995).
[5]
CHARACTERIZATION AS A PLD.
PubMed=8576189; DOI=10.1074/jbc.271.5.2361;
Waksman M., Eli Y., Liscovitch M., Gerst J.E.;
"Identification and characterization of a gene encoding phospholipase
D activity in yeast.";
J. Biol. Chem. 271:2361-2364(1996).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-8, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-145; SER-1461
AND THR-1462, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[11]
FUNCTION, ENZYME REGULATION, AND INTERACTION WITH SRF1.
PubMed=21347278; DOI=10.1371/journal.pgen.1001299;
Kennedy M.A., Kabbani N., Lambert J.P., Swayne L.A., Ahmed F.,
Figeys D., Bennett S.A., Bryan J., Baetz K.;
"Srf1 is a novel regulator of phospholipase D activity and is
essential to buffer the toxic effects of C16:0 platelet activating
factor.";
PLoS Genet. 7:E1001299-E1001299(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Required for meiosis and spore formation. Seems to be
involved in the coordinate induction of late meiotic events. PLD
activity is induced under sporulation conditions and seems to be
necessary to complete the meiotic cycle, but not for vegetative
cell growth. {ECO:0000269|PubMed:1582554,
ECO:0000269|PubMed:21347278}.
-!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
phosphatidate.
-!- ENZYME REGULATION: Activity is dependent of phosphatidylinositol
4,5-bisphosphate and the regulator SRF1. Inhibited by magnesium.
{ECO:0000269|PubMed:21347278}.
-!- SUBUNIT: Interacts with SRF1. {ECO:0000269|PubMed:21347278}.
-!- MISCELLANEOUS: Present with 49 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA74938.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L46807; AAA74938.1; ALT_INIT; Genomic_DNA.
EMBL; Z28256; CAA82103.1; -; Genomic_DNA.
EMBL; BK006944; DAA09186.1; -; Genomic_DNA.
PIR; S38103; S38103.
RefSeq; NP_012956.3; NM_001179821.3.
ProteinModelPortal; P36126; -.
BioGrid; 34164; 95.
DIP; DIP-2643N; -.
IntAct; P36126; 3.
MINT; MINT-424991; -.
STRING; 4932.YKR031C; -.
SwissLipids; SLP:000000072; -.
iPTMnet; P36126; -.
MaxQB; P36126; -.
PRIDE; P36126; -.
EnsemblFungi; YKR031C; YKR031C; YKR031C.
GeneID; 853902; -.
KEGG; sce:YKR031C; -.
EuPathDB; FungiDB:YKR031C; -.
SGD; S000001739; SPO14.
GeneTree; ENSGT00390000008356; -.
HOGENOM; HOG000193520; -.
InParanoid; P36126; -.
KO; K01115; -.
OMA; LMFRADS; -.
OrthoDB; EOG092C0382; -.
BioCyc; YEAST:YKR031C-MONOMER; -.
Reactome; R-SCE-1483166; Synthesis of PA.
Reactome; R-SCE-2029485; Role of phospholipids in phagocytosis.
Reactome; R-SCE-6798695; Neutrophil degranulation.
PRO; PR:P36126; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0005768; C:endosome; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005628; C:prospore membrane; IDA:SGD.
GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
GO; GO:0004630; F:phospholipase D activity; IDA:SGD.
GO; GO:0031321; P:ascospore-type prospore assembly; IMP:SGD.
GO; GO:0000753; P:cell morphogenesis involved in conjugation with cellular fusion; IMP:SGD.
GO; GO:0006887; P:exocytosis; IGI:SGD.
GO; GO:0048017; P:inositol lipid-mediated signaling; IEA:InterPro.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
GO; GO:0006644; P:phospholipid metabolic process; IDA:SGD.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR001683; Phox.
InterPro; IPR001736; PLipase_D/transphosphatidylase.
InterPro; IPR016555; PLipase_D_euk.
InterPro; IPR015679; PLipase_D_fam.
InterPro; IPR036871; PX_dom_sf.
PANTHER; PTHR18896; PTHR18896; 2.
Pfam; PF00614; PLDc; 2.
PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
SMART; SM00233; PH; 1.
SMART; SM00155; PLDc; 2.
SMART; SM00312; PX; 1.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS50035; PLD; 2.
1: Evidence at protein level;
Acetylation; Complete proteome; Hydrolase; Lipid degradation;
Lipid metabolism; Meiosis; Phosphoprotein; Reference proteome; Repeat;
Sporulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:22814378}.
CHAIN 2 1683 Phospholipase D1.
/FTId=PRO_0000218825.
DOMAIN 291 487 PX.
DOMAIN 496 664 PH.
DOMAIN 791 818 PLD phosphodiesterase 1.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
DOMAIN 1091 1118 PLD phosphodiesterase 2.
{ECO:0000255|PROSITE-ProRule:PRU00153}.
COMPBIAS 255 280 Asn-rich.
COMPBIAS 405 410 Poly-Asn.
COMPBIAS 628 633 Poly-Leu.
ACT_SITE 796 796 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 798 798 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 803 803 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 1096 1096 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 1098 1098 {ECO:0000255|PROSITE-ProRule:PRU00153}.
ACT_SITE 1103 1103 {ECO:0000255|PROSITE-ProRule:PRU00153}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:22814378}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:15665377}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 145 145 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 1461 1461 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 1462 1462 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
SEQUENCE 1683 AA; 195204 MW; 54047C977AE39CB7 CRC64;
MSNVSTASGT HFAPPQADRS VTEEVDRVNS RPDELENQEV LRQLPENGNL TSSLQREKRR
TPNGKEAERK HALPKSFVDR NLSDVSPNHS LDHIMHSNEH DPRRGSDEEN MHRLYNNLHS
SNNNVHSKRN SKREEERAPQ RRSSSVAYTQ QQFNGWKKEF GHAFKKISAI GRLKSSVNSP
TPAGSGHRHN QHQHQQVNEE DLYTQRLASD LLDSLLAGCP ASLFASTQFL RDEHGKRRAP
LLLAKLDVRV SPLKNDNNIL DITNSNHNHR GNNNNNTGEN SDRRPSIPRS SSIISISSNV
AEFMYSRNEN SLFRIHLEYG IDEDRLKWSI IRSYKDIKSL HHKLKIVAFQ QLTISKLYSD
NNRYHSLQLP HFPHYKEMVK ERNVMEKKAE NKPSSAASAP HTSENNNNDN GSNITSLETL
SSSEISEFNI DNVKMKHLQD LIDEPDDFSQ PIHLRLERYL RLLNIALCLR PHANRLFEFY
ELSPLGNLLS RESGFQGKQG YLVIRSTAKA QGWRVSHFGK HAFKDMIDRH TTKWFLVRNS
YLTYVSDLSS TTPLDVFLID WKFKVRFSGN KNNILDNENE INWIIHDPNL EINDELEEFG
IENDANNILD KNGKSKTHQK KSNISSKLLL LTLENSERKL KIICKSESSL KQWMSSIIKM
STSTPWSKPN RFGSFAPVRT NSFCKFLVDG RDYFWSLSEA LLMAKDVIYI HDWWLSPELY
LRRPVKGNQG FRIDRMLKSC AEKGIKIFIV IYRNVGNIVG TDSLWTKHSM LNLHPNIHII
RSPNQWLQNT YFWAHHEKFV VIDETFAFIG GTDLCYGRYD TFEHVLRDDA ESLLDQNFPG
KDYSNARIAD FHDLDKPFES MYDRKVIPRM PWHDVQMMTL GEPARDLARH FVQRWNYLLR
AKRPSRLTPL LTPPSDLTAE ELKSLPMFEI LREKSTCETQ ILRSAGNWSL GLKETECSIQ
NAYLKLIEQS EHFIYIENQF FITSTVWNGT CVLNKIGDAL VDRIVKANQE KKPWKAFILI
PLMPGFDSPV DTAEASSLRL IMQFQYQSIS RGEHSTFSKL KKLNIDPAQY IQFFSLRKWS
TFAPNERLIT EQLYVHAKIL IADDRRCIIG SANINERSQL GNRDSEVAIL IRDTDLIKTK
MNGDDYYAGK FPWELRQRLM REHLGCDVDL VEFVEKKFER FEKFAAKNYE KLHTLSKEGD
SGNNWSDREM IDSAMIELGY REIFGCKFSP QWKSGHGNSV DDGSTQCGIN EKEVGREDEN
VYEKFFNSVD YGKSSRKRTP LPKHNFASLG LTFNHRAGIE NVGIRDHKVL STDPRLRKND
EHKKEVDGYG PDCWKKESNK KFKADATEQL KEWALNSLAS KVLDDKEMIK SEIPEGFSNY
LPNEKDLEMY LTDKTVTNRN KWSMLKRICY LQYLSHKLDE RKTQRLKKIK DMRRHLSSST
ESTRNGSNSL PLNEKSNEGE STNVDQDIEG DEYHRLHEDI LKNQELDDGS LDDLLSQIIP
KITNFNSGEI DDAKKEELLK LNFIDPYSFE DPLISSFSEG LWFTIALRNT LLYKLVFHCQ
PDNAVQNWKE YGEFTELEQE FQINQEKLID LEAENINSTT TNVVDKDREK EKMRKAAELR
MKLSGSLLYG FNQKVFDKHT AQRILERIHG HLVIFPTEWL AKEVESRNWI FNSDRLSPME
IYN


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