SPO14_YEAST
ID SPO14_YEAST Reviewed; 1683 AA.
AC P36126; D6VX96;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Phospholipase D1;
DE Short=PLD 1;
DE EC=3.1.4.4;
DE AltName: Full=Choline phosphatase 1;
DE AltName: Full=Meiosis-specific sporulation-specific protein 14;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D1;
GN Name=SPO14; Synonyms=PLD1; OrderedLocusNames=YKR031C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1582554; DOI=10.1093/genetics/130.4.703;
RA Honigberg S.M., Conicella C., Espositio R.E.;
RT "Commitment to meiosis in Saccharomyces cerevisiae: involvement of the
RT SPO14 gene.";
RL Genetics 130:703-716(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CHARACTERIZATION AS A PLD.
RX PubMed=8618862; DOI=10.1073/pnas.92.26.12151;
RA Rose K., Rudge S.A., Frohman M.A., Morris A.J., Engebrecht J.;
RT "Phospholipase D signaling is essential for meiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:12151-12155(1995).
RN [5]
RP CHARACTERIZATION AS A PLD.
RX PubMed=8576189; DOI=10.1074/jbc.271.5.2361;
RA Waksman M., Eli Y., Liscovitch M., Gerst J.E.;
RT "Identification and characterization of a gene encoding phospholipase D
RT activity in yeast.";
RL J. Biol. Chem. 271:2361-2364(1996).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-8, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-145; SER-1461 AND
RP THR-1462, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH SRF1.
RX PubMed=21347278; DOI=10.1371/journal.pgen.1001299;
RA Kennedy M.A., Kabbani N., Lambert J.P., Swayne L.A., Ahmed F., Figeys D.,
RA Bennett S.A., Bryan J., Baetz K.;
RT "Srf1 is a novel regulator of phospholipase D activity and is essential to
RT buffer the toxic effects of C16:0 platelet activating factor.";
RL PLoS Genet. 7:E1001299-E1001299(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for meiosis and spore formation. Seems to be
CC involved in the coordinate induction of late meiotic events. PLD
CC activity is induced under sporulation conditions and seems to be
CC necessary to complete the meiotic cycle, but not for vegetative cell
CC growth. {ECO:0000269|PubMed:1582554, ECO:0000269|PubMed:21347278}.
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 -!- ACTIVITY REGULATION: Activity is dependent of phosphatidylinositol 4,5-
CC bisphosphate and the regulator SRF1. Inhibited by magnesium.
CC {ECO:0000269|PubMed:21347278}.
CC -!- SUBUNIT: Interacts with SRF1. {ECO:0000269|PubMed:21347278}.
CC -!- MISCELLANEOUS: Present with 49 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74938.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; L46807; AAA74938.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z28256; CAA82103.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09186.1; -; Genomic_DNA.
DR PIR; S38103; S38103.
DR RefSeq; NP_012956.3; NM_001179821.3.
DR AlphaFoldDB; P36126; -.
DR SMR; P36126; -.
DR BioGRID; 34164; 107.
DR DIP; DIP-2643N; -.
DR IntAct; P36126; 3.
DR MINT; P36126; -.
DR STRING; 4932.YKR031C; -.
DR SwissLipids; SLP:000000072; -.
DR iPTMnet; P36126; -.
DR MaxQB; P36126; -.
DR PaxDb; P36126; -.
DR PRIDE; P36126; -.
DR EnsemblFungi; YKR031C_mRNA; YKR031C; YKR031C.
DR GeneID; 853902; -.
DR KEGG; sce:YKR031C; -.
DR SGD; S000001739; SPO14.
DR VEuPathDB; FungiDB:YKR031C; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_3_0_1; -.
DR InParanoid; P36126; -.
DR OMA; QCQYQSI; -.
DR BioCyc; YEAST:YKR031C-MON; -.
DR BRENDA; 3.1.4.4; 984.
DR Reactome; R-SCE-1483166; Synthesis of PA.
DR Reactome; R-SCE-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR PRO; PR:P36126; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36126; protein.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0004630; F:phospholipase D activity; IDA:SGD.
DR GO; GO:0031321; P:ascospore-type prospore assembly; IMP:SGD.
DR GO; GO:0000753; P:cell morphogenesis involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IEA:InterPro.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:SGD.
DR InterPro; IPR001849; PH_domain.
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; PTHR18896; 2.
DR Pfam; PF00614; PLDc; 2.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50035; PLD; 2.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Lipid degradation; Lipid metabolism; Meiosis;
KW Phosphoprotein; Reference proteome; Repeat; Sporulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..1683
FT /note="Phospholipase D1"
FT /id="PRO_0000218825"
FT DOMAIN 291..487
FT /note="PX"
FT DOMAIN 496..664
FT /note="PH"
FT DOMAIN 791..818
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 1091..1118
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 796
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 798
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 803
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 1096
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 1098
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 1103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1462
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ 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
