Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P36126

- SPO14_YEAST

UniProt

P36126 - SPO14_YEAST

Protein

Phospholipase D1

Gene

SPO14

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (03 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 – 7961PROSITE-ProRule annotation
    Active sitei798 – 7981PROSITE-ProRule annotation
    Active sitei803 – 8031PROSITE-ProRule annotation
    Active sitei1096 – 10961PROSITE-ProRule annotation
    Active sitei1098 – 10981PROSITE-ProRule annotation
    Active sitei1103 – 11031PROSITE-ProRule annotation

    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

    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

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 16831682Phospholipase D1PRO_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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini291 – 487197PXAdd
    BLAST
    Domaini496 – 664169PHAdd
    BLAST
    Domaini791 – 81828PLD phosphodiesterase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1091 – 111828PLD phosphodiesterase 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the phospholipase D family.Curated
    Contains 1 PH domain.Curated
    Contains 2 PLD phosphodiesterase domains.PROSITE-ProRule annotation
    Contains 1 PX (phox homology) domain.Curated

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 135 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.1 Publication

    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