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P36126 (SPO14_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1683 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.11

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.11

Subunit structure

Interacts with SRF1. Ref.11

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 16831682Phospholipase D1
PRO_0000218825

Regions

Domain291 – 487197PX
Domain496 – 664169PH
Domain791 – 81828PLD phosphodiesterase 1
Domain1091 – 111828PLD phosphodiesterase 2
Compositional bias255 – 28026Asn-rich
Compositional bias405 – 4106Poly-Asn
Compositional bias628 – 6336Poly-Leu

Sites

Active site7961 Potential
Active site7981 Potential
Active site8031 Potential
Active site10961 Potential
Active site10981 Potential
Active site11031 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.7 Ref.12
Modified residue81Phosphoserine Ref.7
Modified residue301Phosphoserine Ref.9 Ref.10
Modified residue1451Phosphoserine Ref.10
Modified residue14611Phosphoserine Ref.10
Modified residue14621Phosphothreonine Ref.10

Sequences

Sequence LengthMass (Da)Tools
P36126 [UniParc].

Last modified October 3, 2006. Version 3.
Checksum: 54047C977AE39CB7

FASTA1,683195,204
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 204508 / S288c.
[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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[8]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[9]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-145; SER-1461 AND THR-1462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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.
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS38103.
RefSeqNP_012956.3. NM_001179821.3.

3D structure databases

ProteinModelPortalP36126.
SMRP36126. Positions 1093-1136.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34164. 72 interactions.
DIPDIP-2643N.
IntActP36126. 3 interactions.
MINTMINT-424991.
STRING4932.YKR031C.

Proteomic databases

PaxDbP36126.
PeptideAtlasP36126.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKR031C; YKR031C; YKR031C.
GeneID853902.
KEGGsce:YKR031C.

Organism-specific databases

CYGDYKR031c.
SGDS000001739. SPO14.

Phylogenomic databases

eggNOGCOG1502.
GeneTreeENSGT00390000008356.
HOGENOMHOG000193520.
KOK01115.
OMAHVIRSPN.
OrthoDBEOG7H4F2W.

Enzyme and pathway databases

BioCycYEAST:YKR031C-MONOMER.

Gene expression databases

GenevestigatorP36126.

Family and domain databases

InterProIPR001683. Phox.
IPR001849. Pleckstrin_homology.
IPR001736. PLipase_D/transphosphatidylase.
IPR016555. PLipase_D_euk.
IPR015679. PLipase_D_fam.
[Graphical view]
PANTHERPTHR18896. PTHR18896. 1 hit.
PfamPF00614. PLDc. 2 hits.
[Graphical view]
PIRSFPIRSF009376. Phospholipase_D_euk. 1 hit.
SMARTSM00233. PH. 1 hit.
SM00155. PLDc. 2 hits.
SM00312. PX. 1 hit.
[Graphical view]
SUPFAMSSF64268. SSF64268. 1 hit.
PROSITEPS50035. PLD. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio975230.

Entry information

Entry nameSPO14_YEAST
AccessionPrimary (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: April 16, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families