P36126 (SPO14_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phospholipase D1
Short name=PLD 1
EC=3.1.4.4

Alternative name(s):
Choline phosphatase 1
Meiosis-specific sporulation-specific protein 14
Phosphatidylcholine-hydrolyzing phospholipase D1

Gene names

Name:	SPO14
Synonyms:	PLD1
Ordered Locus Names:	YKR031C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	1683 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.9
Catalytic activity	A phosphatidylcholine + H2O = choline + a phosphatidate.
Enzyme regulation	Activity is dependent of phosphatidylinositol 4,5-bisphosphate and the regulator SRF1. Inhibited by magnesium. Ref.9
Subunit structure	Interacts with SRF1. Ref.9
Miscellaneous	Present with 49 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the phospholipase D family. Contains 1 PH domain. Contains 2 PLD phosphodiesterase domains. Contains 1 PX (phox homology) domain.
Sequence caution	The sequence AAA74938.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism Meiosis Sporulation
Domain	Repeat
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ascospore-type prospore assembly Inferred from mutant phenotype PubMed 16554438. Source: SGD cell communication Inferred from electronic annotation. Source: InterPro cell morphogenesis involved in conjugation with cellular fusion Inferred from mutant phenotype PubMed 12702348. Source: SGD exocytosis Inferred from genetic interaction PubMed 10848624PubMed 11514437. Source: SGD lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW meiosis Inferred from electronic annotation. Source: UniProtKB-KW phospholipid metabolic process Inferred from direct assay Ref.5. Source: SGD
Cellular_component	endosome Inferred from direct assay PubMed 10848624. Source: SGD nucleus Inferred from direct assay PubMed 21954159. Source: SGD prospore membrane Inferred from direct assay PubMed 9693364. Source: SGD
Molecular_function	NAPE-specific phospholipase D activity Inferred from electronic annotation. Source: EC phosphatidylinositol-3-phosphate binding Inferred from direct assay PubMed 11557775. Source: SGD phospholipase D activity Inferred from direct assay PubMed 11514437. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1683	1683	Phospholipase D1		PRO_0000218825
Regions
	Domain	291 – 487	197	PX
	Domain	496 – 664	169	PH
	Domain	791 – 818	28	PLD phosphodiesterase 1
	Domain	1091 – 1118	28	PLD phosphodiesterase 2
	Compositional bias	255 – 280	26	Asn-rich
	Compositional bias	405 – 410	6	Poly-Asn
	Compositional bias	628 – 633	6	Poly-Leu
Sites
	Active site	796	1	Potential
	Active site	798	1	Potential
	Active site	803	1	Potential
	Active site	1096	1	Potential
	Active site	1098	1	Potential
	Active site	1103	1	Potential
Amino acid modifications
	Modified residue	30	1	Phosphoserine Ref.8
	Modified residue	1268	1	Phosphoserine Ref.7 Ref.8
	Modified residue	1447	1	Phosphoserine Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P36126 [UniParc]. Last modified October 3, 2006. Version 3. Checksum: 54047C977AE39CB7	FASTA	1,683	195,204
	10 20 30 40 50 60 MSNVSTASGT HFAPPQADRS VTEEVDRVNS RPDELENQEV LRQLPENGNL TSSLQREKRR 70 80 90 100 110 120 TPNGKEAERK HALPKSFVDR NLSDVSPNHS LDHIMHSNEH DPRRGSDEEN MHRLYNNLHS 130 140 150 160 170 180 SNNNVHSKRN SKREEERAPQ RRSSSVAYTQ QQFNGWKKEF GHAFKKISAI GRLKSSVNSP 190 200 210 220 230 240 TPAGSGHRHN QHQHQQVNEE DLYTQRLASD LLDSLLAGCP ASLFASTQFL RDEHGKRRAP 250 260 270 280 290 300 LLLAKLDVRV SPLKNDNNIL DITNSNHNHR GNNNNNTGEN SDRRPSIPRS SSIISISSNV 310 320 330 340 350 360 AEFMYSRNEN SLFRIHLEYG IDEDRLKWSI IRSYKDIKSL HHKLKIVAFQ QLTISKLYSD 370 380 390 400 410 420 NNRYHSLQLP HFPHYKEMVK ERNVMEKKAE NKPSSAASAP HTSENNNNDN GSNITSLETL 430 440 450 460 470 480 SSSEISEFNI DNVKMKHLQD LIDEPDDFSQ PIHLRLERYL RLLNIALCLR PHANRLFEFY 490 500 510 520 530 540 ELSPLGNLLS RESGFQGKQG YLVIRSTAKA QGWRVSHFGK HAFKDMIDRH TTKWFLVRNS 550 560 570 580 590 600 YLTYVSDLSS TTPLDVFLID WKFKVRFSGN KNNILDNENE INWIIHDPNL EINDELEEFG 610 620 630 640 650 660 IENDANNILD KNGKSKTHQK KSNISSKLLL LTLENSERKL KIICKSESSL KQWMSSIIKM 670 680 690 700 710 720 STSTPWSKPN RFGSFAPVRT NSFCKFLVDG RDYFWSLSEA LLMAKDVIYI HDWWLSPELY 730 740 750 760 770 780 LRRPVKGNQG FRIDRMLKSC AEKGIKIFIV IYRNVGNIVG TDSLWTKHSM LNLHPNIHII 790 800 810 820 830 840 RSPNQWLQNT YFWAHHEKFV VIDETFAFIG GTDLCYGRYD TFEHVLRDDA ESLLDQNFPG 850 860 870 880 890 900 KDYSNARIAD FHDLDKPFES MYDRKVIPRM PWHDVQMMTL GEPARDLARH FVQRWNYLLR 910 920 930 940 950 960 AKRPSRLTPL LTPPSDLTAE ELKSLPMFEI LREKSTCETQ ILRSAGNWSL GLKETECSIQ 970 980 990 1000 1010 1020 NAYLKLIEQS EHFIYIENQF FITSTVWNGT CVLNKIGDAL VDRIVKANQE KKPWKAFILI 1030 1040 1050 1060 1070 1080 PLMPGFDSPV DTAEASSLRL IMQFQYQSIS RGEHSTFSKL KKLNIDPAQY IQFFSLRKWS 1090 1100 1110 1120 1130 1140 TFAPNERLIT EQLYVHAKIL IADDRRCIIG SANINERSQL GNRDSEVAIL IRDTDLIKTK 1150 1160 1170 1180 1190 1200 MNGDDYYAGK FPWELRQRLM REHLGCDVDL VEFVEKKFER FEKFAAKNYE KLHTLSKEGD 1210 1220 1230 1240 1250 1260 SGNNWSDREM IDSAMIELGY REIFGCKFSP QWKSGHGNSV DDGSTQCGIN EKEVGREDEN 1270 1280 1290 1300 1310 1320 VYEKFFNSVD YGKSSRKRTP LPKHNFASLG LTFNHRAGIE NVGIRDHKVL STDPRLRKND 1330 1340 1350 1360 1370 1380 EHKKEVDGYG PDCWKKESNK KFKADATEQL KEWALNSLAS KVLDDKEMIK SEIPEGFSNY 1390 1400 1410 1420 1430 1440 LPNEKDLEMY LTDKTVTNRN KWSMLKRICY LQYLSHKLDE RKTQRLKKIK DMRRHLSSST 1450 1460 1470 1480 1490 1500 ESTRNGSNSL PLNEKSNEGE STNVDQDIEG DEYHRLHEDI LKNQELDDGS LDDLLSQIIP 1510 1520 1530 1540 1550 1560 KITNFNSGEI DDAKKEELLK LNFIDPYSFE DPLISSFSEG LWFTIALRNT LLYKLVFHCQ 1570 1580 1590 1600 1610 1620 PDNAVQNWKE YGEFTELEQE FQINQEKLID LEAENINSTT TNVVDKDREK EKMRKAAELR 1630 1640 1650 1660 1670 1680 MKLSGSLLYG FNQKVFDKHT AQRILERIHG HLVIFPTEWL AKEVESRNWI FNSDRLSPME IYN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Commitment to meiosis in Saccharomyces cerevisiae: involvement of the SPO14 gene." Honigberg S.M., Conicella C., Espositio R.E. Genetics 130:703-716(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"Complete DNA sequence of yeast chromosome XI." 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. Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Phospholipase D signaling is essential for meiosis." Rose K., Rudge S.A., Frohman M.A., Morris A.J., Engebrecht J. Proc. Natl. Acad. Sci. U.S.A. 92:12151-12155(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION AS A PLD.
[5]	"Identification and characterization of a gene encoding phospholipase D activity in yeast." Waksman M., Eli Y., Liscovitch M., Gerst J.E. J. Biol. Chem. 271:2361-2364(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION AS A PLD.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1268, MASS SPECTROMETRY. Strain: YAL6B.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-1268 AND SER-1447, MASS SPECTROMETRY.
[9]	"Srf1 is a novel regulator of phospholipase D activity and is essential to buffer the toxic effects of C16:0 platelet activating factor." Kennedy M.A., Kabbani N., Lambert J.P., Swayne L.A., Ahmed F., Figeys D., Bennett S.A., Bryan J., Baetz K. PLoS Genet. 7:E1001299-E1001299(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH SRF1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L46807 Genomic DNA. Translation: AAA74938.1. Different initiation. Z28256 Genomic DNA. Translation: CAA82103.1. BK006944 Genomic DNA. Translation: DAA09186.1.
PIR	S38103.
RefSeq	NP_012956.3. NM_001179821.3.
3D structure databases
ProteinModelPortal	P36126.
SMR	P36126. Positions 1093-1136.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2643N.
IntAct	P36126. 2 interactions.
MINT	MINT-424991.
STRING	4932.YKR031C.
Proteomic databases
PaxDb	P36126.
PeptideAtlas	P36126.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKR031C; YKR031C; YKR031C.
GeneID	853902.
KEGG	sce:YKR031C. sce:YKR035W-A.
Organism-specific databases
CYGD	YKR031c.
SGD	S000001739. SPO14.
Phylogenomic databases
eggNOG	COG1502.
GeneTree	ENSGT00390000008356.
HOGENOM	HOG000193520.
KO	K01115. K12197.
OMA	VIRSPNQ.
OrthoDB	EOG46T68R.
Gene expression databases
Genevestigator	P36126.
GermOnline	YKR031C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001683. Phox. IPR001849. Pleckstrin_homology. IPR001736. PLipase_D/transphosphatidylase. IPR016555. PLipase_D_euk. IPR015679. PLipase_D_fam. [Graphical view]
PANTHER	PTHR18896. PTHR18896. 1 hit.
Pfam	PF00614. PLDc. 2 hits. [Graphical view]
PIRSF	PIRSF009376. Phospholipase_D_euk. 1 hit.
SMART	SM00233. PH. 1 hit. SM00155. PLDc. 2 hits. SM00312. PX. 1 hit. [Graphical view]
PROSITE	PS50003. PH_DOMAIN. False negative. PS50035. PLD. 2 hits. PS50195. PX. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	975230.

Entry information

Entry name

SPO14_YEAST

Accession

Primary (citable) accession number: P36126
Secondary accession number(s): D6VX96

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	October 3, 2006
Last modified:	May 1, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program