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P36126

- SPO14_YEAST

UniProt

P36126 - SPO14_YEAST

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Protein
Phospholipase D1
Gene
SPO14, PLD1, YKR031C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

A phosphatidylcholine + H2O = choline + a phosphatidate.

Enzyme regulationi

Activity is dependent of phosphatidylinositol 4,5-bisphosphate and the regulator SRF1. Inhibited by magnesium.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei796 – 7961 Reviewed prediction
Active sitei798 – 7981 Reviewed prediction
Active sitei803 – 8031 Reviewed prediction
Active sitei1096 – 10961 Reviewed prediction
Active sitei1098 – 10981 Reviewed prediction
Active sitei1103 – 11031 Reviewed prediction

GO - Molecular functioni

  1. N-acylphosphatidylethanolamine-specific phospholipase D activity Source: UniProtKB-EC
  2. phosphatidylinositol-3-phosphate binding Source: SGD
  3. phospholipase D activity Source: SGD
Complete GO annotation...

GO - Biological processi

  1. ascospore-type prospore assembly Source: SGD
  2. cell morphogenesis involved in conjugation with cellular fusion Source: SGD
  3. exocytosis Source: SGD
  4. lipid catabolic process Source: UniProtKB-KW
  5. meiotic nuclear division Source: UniProtKB-KW
  6. phospholipid metabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism, Meiosis, Sporulation

Enzyme and pathway databases

BioCyciYEAST:YKR031C-MONOMER.
ReactomeiREACT_188407. Role of phospholipids in phagocytosis.
REACT_188995. Synthesis of PG.
REACT_191569. Synthesis of PA.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase D1 (EC:3.1.4.4)
Short name:
PLD 1
Alternative name(s):
Choline phosphatase 1
Meiosis-specific sporulation-specific protein 14
Phosphatidylcholine-hydrolyzing phospholipase D1
Gene namesi
Name:SPO14
Synonyms:PLD1
Ordered Locus Names:YKR031C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKR031c.
SGDiS000001739. SPO14.

Subcellular locationi

GO - Cellular componenti

  1. endosome Source: SGD
  2. nucleus Source: SGD
  3. prospore membrane Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 16831682Phospholipase D1
PRO_0000218825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei8 – 81Phosphoserine1 Publication
Modified residuei30 – 301Phosphoserine2 Publications
Modified residuei145 – 1451Phosphoserine1 Publication
Modified residuei1461 – 14611Phosphoserine1 Publication
Modified residuei1462 – 14621Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP36126.
PaxDbiP36126.
PeptideAtlasiP36126.

Expressioni

Gene expression databases

GenevestigatoriP36126.

Interactioni

Subunit structurei

Interacts with SRF1.1 Publication

Protein-protein interaction databases

BioGridi34164. 73 interactions.
DIPiDIP-2643N.
IntActiP36126. 3 interactions.
MINTiMINT-424991.
STRINGi4932.YKR031C.

Structurei

3D structure databases

ProteinModelPortaliP36126.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini291 – 487197PX
Add
BLAST
Domaini496 – 664169PH
Add
BLAST
Domaini791 – 81828PLD phosphodiesterase 1
Add
BLAST
Domaini1091 – 111828PLD phosphodiesterase 2
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi255 – 28026Asn-rich
Add
BLAST
Compositional biasi405 – 4106Poly-Asn
Compositional biasi628 – 6336Poly-Leu

Sequence similaritiesi

Belongs to the phospholipase D family.
Contains 1 PH domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1502.
GeneTreeiENSGT00390000008356.
HOGENOMiHOG000193520.
KOiK01115.
OMAiHVIRSPN.
OrthoDBiEOG7H4F2W.

Family and domain databases

InterProiIPR001849. PH_domain.
IPR001683. Phox.
IPR001736. PLipase_D/transphosphatidylase.
IPR016555. PLipase_D_euk.
IPR015679. PLipase_D_fam.
[Graphical view]
PANTHERiPTHR18896. PTHR18896. 1 hit.
PfamiPF00614. PLDc. 2 hits.
[Graphical view]
PIRSFiPIRSF009376. Phospholipase_D_euk. 1 hit.
SMARTiSM00233. PH. 1 hit.
SM00155. PLDc. 2 hits.
SM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50035. PLD. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P36126-1 [UniParc]FASTAAdd to Basket

« Hide

MSNVSTASGT HFAPPQADRS VTEEVDRVNS RPDELENQEV LRQLPENGNL     50
TSSLQREKRR TPNGKEAERK HALPKSFVDR NLSDVSPNHS LDHIMHSNEH 100
DPRRGSDEEN MHRLYNNLHS SNNNVHSKRN SKREEERAPQ RRSSSVAYTQ 150
QQFNGWKKEF GHAFKKISAI GRLKSSVNSP TPAGSGHRHN QHQHQQVNEE 200
DLYTQRLASD LLDSLLAGCP ASLFASTQFL RDEHGKRRAP LLLAKLDVRV 250
SPLKNDNNIL DITNSNHNHR GNNNNNTGEN SDRRPSIPRS SSIISISSNV 300
AEFMYSRNEN SLFRIHLEYG IDEDRLKWSI IRSYKDIKSL HHKLKIVAFQ 350
QLTISKLYSD NNRYHSLQLP HFPHYKEMVK ERNVMEKKAE NKPSSAASAP 400
HTSENNNNDN GSNITSLETL SSSEISEFNI DNVKMKHLQD LIDEPDDFSQ 450
PIHLRLERYL RLLNIALCLR PHANRLFEFY ELSPLGNLLS RESGFQGKQG 500
YLVIRSTAKA QGWRVSHFGK HAFKDMIDRH TTKWFLVRNS YLTYVSDLSS 550
TTPLDVFLID WKFKVRFSGN KNNILDNENE INWIIHDPNL EINDELEEFG 600
IENDANNILD KNGKSKTHQK KSNISSKLLL LTLENSERKL KIICKSESSL 650
KQWMSSIIKM STSTPWSKPN RFGSFAPVRT NSFCKFLVDG RDYFWSLSEA 700
LLMAKDVIYI HDWWLSPELY LRRPVKGNQG FRIDRMLKSC AEKGIKIFIV 750
IYRNVGNIVG TDSLWTKHSM LNLHPNIHII RSPNQWLQNT YFWAHHEKFV 800
VIDETFAFIG GTDLCYGRYD TFEHVLRDDA ESLLDQNFPG KDYSNARIAD 850
FHDLDKPFES MYDRKVIPRM PWHDVQMMTL GEPARDLARH FVQRWNYLLR 900
AKRPSRLTPL LTPPSDLTAE ELKSLPMFEI LREKSTCETQ ILRSAGNWSL 950
GLKETECSIQ NAYLKLIEQS EHFIYIENQF FITSTVWNGT CVLNKIGDAL 1000
VDRIVKANQE KKPWKAFILI PLMPGFDSPV DTAEASSLRL IMQFQYQSIS 1050
RGEHSTFSKL KKLNIDPAQY IQFFSLRKWS TFAPNERLIT EQLYVHAKIL 1100
IADDRRCIIG SANINERSQL GNRDSEVAIL IRDTDLIKTK MNGDDYYAGK 1150
FPWELRQRLM REHLGCDVDL VEFVEKKFER FEKFAAKNYE KLHTLSKEGD 1200
SGNNWSDREM IDSAMIELGY REIFGCKFSP QWKSGHGNSV DDGSTQCGIN 1250
EKEVGREDEN VYEKFFNSVD YGKSSRKRTP LPKHNFASLG LTFNHRAGIE 1300
NVGIRDHKVL STDPRLRKND EHKKEVDGYG PDCWKKESNK KFKADATEQL 1350
KEWALNSLAS KVLDDKEMIK SEIPEGFSNY LPNEKDLEMY LTDKTVTNRN 1400
KWSMLKRICY LQYLSHKLDE RKTQRLKKIK DMRRHLSSST ESTRNGSNSL 1450
PLNEKSNEGE STNVDQDIEG DEYHRLHEDI LKNQELDDGS LDDLLSQIIP 1500
KITNFNSGEI DDAKKEELLK LNFIDPYSFE DPLISSFSEG LWFTIALRNT 1550
LLYKLVFHCQ PDNAVQNWKE YGEFTELEQE FQINQEKLID LEAENINSTT 1600
TNVVDKDREK EKMRKAAELR MKLSGSLLYG FNQKVFDKHT AQRILERIHG 1650
HLVIFPTEWL AKEVESRNWI FNSDRLSPME IYN 1683
Length:1,683
Mass (Da):195,204
Last modified:October 3, 2006 - v3
Checksum:i54047C977AE39CB7
GO

Sequence cautioni

The sequence AAA74938.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L46807 Genomic DNA. Translation: AAA74938.1. Different initiation.
Z28256 Genomic DNA. Translation: CAA82103.1.
BK006944 Genomic DNA. Translation: DAA09186.1.
PIRiS38103.
RefSeqiNP_012956.3. NM_001179821.3.

Genome annotation databases

EnsemblFungiiYKR031C; YKR031C; YKR031C.
GeneIDi853902.
KEGGisce:YKR031C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L46807 Genomic DNA. Translation: AAA74938.1 . Different initiation.
Z28256 Genomic DNA. Translation: CAA82103.1 .
BK006944 Genomic DNA. Translation: DAA09186.1 .
PIRi S38103.
RefSeqi NP_012956.3. NM_001179821.3.

3D structure databases

ProteinModelPortali P36126.
ModBasei Search...

Protein-protein interaction databases

BioGridi 34164. 73 interactions.
DIPi DIP-2643N.
IntActi P36126. 3 interactions.
MINTi MINT-424991.
STRINGi 4932.YKR031C.

Proteomic databases

MaxQBi P36126.
PaxDbi P36126.
PeptideAtlasi P36126.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YKR031C ; YKR031C ; YKR031C .
GeneIDi 853902.
KEGGi sce:YKR031C.

Organism-specific databases

CYGDi YKR031c.
SGDi S000001739. SPO14.

Phylogenomic databases

eggNOGi COG1502.
GeneTreei ENSGT00390000008356.
HOGENOMi HOG000193520.
KOi K01115.
OMAi HVIRSPN.
OrthoDBi EOG7H4F2W.

Enzyme and pathway databases

BioCyci YEAST:YKR031C-MONOMER.
Reactomei REACT_188407. Role of phospholipids in phagocytosis.
REACT_188995. Synthesis of PG.
REACT_191569. Synthesis of PA.

Miscellaneous databases

NextBioi 975230.

Gene expression databases

Genevestigatori P36126.

Family and domain databases

InterProi IPR001849. PH_domain.
IPR001683. Phox.
IPR001736. PLipase_D/transphosphatidylase.
IPR016555. PLipase_D_euk.
IPR015679. PLipase_D_fam.
[Graphical view ]
PANTHERi PTHR18896. PTHR18896. 1 hit.
Pfami PF00614. PLDc. 2 hits.
[Graphical view ]
PIRSFi PIRSF009376. Phospholipase_D_euk. 1 hit.
SMARTi SM00233. PH. 1 hit.
SM00155. PLDc. 2 hits.
SM00312. PX. 1 hit.
[Graphical view ]
SUPFAMi SSF64268. SSF64268. 1 hit.
PROSITEi PS50035. PLD. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSPO14_YEAST
AccessioniPrimary (citable) accession number: P36126
Secondary accession number(s): D6VX96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 3, 2006
Last modified: September 3, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 49 molecules/cell in log phase SD medium.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3

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