Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P36126

- SPO14_YEAST

UniProt

P36126 - SPO14_YEAST

(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)

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

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
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 – 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.
InParanoidiP36126.
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

        10         20         30         40         50
MSNVSTASGT HFAPPQADRS VTEEVDRVNS RPDELENQEV LRQLPENGNL
60 70 80 90 100
TSSLQREKRR TPNGKEAERK HALPKSFVDR NLSDVSPNHS LDHIMHSNEH
110 120 130 140 150
DPRRGSDEEN MHRLYNNLHS SNNNVHSKRN SKREEERAPQ RRSSSVAYTQ
160 170 180 190 200
QQFNGWKKEF GHAFKKISAI GRLKSSVNSP TPAGSGHRHN QHQHQQVNEE
210 220 230 240 250
DLYTQRLASD LLDSLLAGCP ASLFASTQFL RDEHGKRRAP LLLAKLDVRV
260 270 280 290 300
SPLKNDNNIL DITNSNHNHR GNNNNNTGEN SDRRPSIPRS SSIISISSNV
310 320 330 340 350
AEFMYSRNEN SLFRIHLEYG IDEDRLKWSI IRSYKDIKSL HHKLKIVAFQ
360 370 380 390 400
QLTISKLYSD NNRYHSLQLP HFPHYKEMVK ERNVMEKKAE NKPSSAASAP
410 420 430 440 450
HTSENNNNDN GSNITSLETL SSSEISEFNI DNVKMKHLQD LIDEPDDFSQ
460 470 480 490 500
PIHLRLERYL RLLNIALCLR PHANRLFEFY ELSPLGNLLS RESGFQGKQG
510 520 530 540 550
YLVIRSTAKA QGWRVSHFGK HAFKDMIDRH TTKWFLVRNS YLTYVSDLSS
560 570 580 590 600
TTPLDVFLID WKFKVRFSGN KNNILDNENE INWIIHDPNL EINDELEEFG
610 620 630 640 650
IENDANNILD KNGKSKTHQK KSNISSKLLL LTLENSERKL KIICKSESSL
660 670 680 690 700
KQWMSSIIKM STSTPWSKPN RFGSFAPVRT NSFCKFLVDG RDYFWSLSEA
710 720 730 740 750
LLMAKDVIYI HDWWLSPELY LRRPVKGNQG FRIDRMLKSC AEKGIKIFIV
760 770 780 790 800
IYRNVGNIVG TDSLWTKHSM LNLHPNIHII RSPNQWLQNT YFWAHHEKFV
810 820 830 840 850
VIDETFAFIG GTDLCYGRYD TFEHVLRDDA ESLLDQNFPG KDYSNARIAD
860 870 880 890 900
FHDLDKPFES MYDRKVIPRM PWHDVQMMTL GEPARDLARH FVQRWNYLLR
910 920 930 940 950
AKRPSRLTPL LTPPSDLTAE ELKSLPMFEI LREKSTCETQ ILRSAGNWSL
960 970 980 990 1000
GLKETECSIQ NAYLKLIEQS EHFIYIENQF FITSTVWNGT CVLNKIGDAL
1010 1020 1030 1040 1050
VDRIVKANQE KKPWKAFILI PLMPGFDSPV DTAEASSLRL IMQFQYQSIS
1060 1070 1080 1090 1100
RGEHSTFSKL KKLNIDPAQY IQFFSLRKWS TFAPNERLIT EQLYVHAKIL
1110 1120 1130 1140 1150
IADDRRCIIG SANINERSQL GNRDSEVAIL IRDTDLIKTK MNGDDYYAGK
1160 1170 1180 1190 1200
FPWELRQRLM REHLGCDVDL VEFVEKKFER FEKFAAKNYE KLHTLSKEGD
1210 1220 1230 1240 1250
SGNNWSDREM IDSAMIELGY REIFGCKFSP QWKSGHGNSV DDGSTQCGIN
1260 1270 1280 1290 1300
EKEVGREDEN VYEKFFNSVD YGKSSRKRTP LPKHNFASLG LTFNHRAGIE
1310 1320 1330 1340 1350
NVGIRDHKVL STDPRLRKND EHKKEVDGYG PDCWKKESNK KFKADATEQL
1360 1370 1380 1390 1400
KEWALNSLAS KVLDDKEMIK SEIPEGFSNY LPNEKDLEMY LTDKTVTNRN
1410 1420 1430 1440 1450
KWSMLKRICY LQYLSHKLDE RKTQRLKKIK DMRRHLSSST ESTRNGSNSL
1460 1470 1480 1490 1500
PLNEKSNEGE STNVDQDIEG DEYHRLHEDI LKNQELDDGS LDDLLSQIIP
1510 1520 1530 1540 1550
KITNFNSGEI DDAKKEELLK LNFIDPYSFE DPLISSFSEG LWFTIALRNT
1560 1570 1580 1590 1600
LLYKLVFHCQ PDNAVQNWKE YGEFTELEQE FQINQEKLID LEAENINSTT
1610 1620 1630 1640 1650
TNVVDKDREK EKMRKAAELR MKLSGSLLYG FNQKVFDKHT AQRILERIHG
1660 1670 1680
HLVIFPTEWL AKEVESRNWI FNSDRLSPME IYN
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.
InParanoidi P36126.
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: October 29, 2014
This is version 136 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