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Protein

Putative meiotic phospholipase SPO1

Gene

SPO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates spindle pole duplication in meiosis I, but not in mitosis. Required for meiosis I, meiosis II chromosome segregation and spore formation. Binds phosphatidylinositol (4)P mono- and polyphosphates.2 Publications

GO - Molecular functioni

  • phospholipase activity Source: SGD

GO - Biological processi

  • ascospore-type prospore membrane assembly Source: SGD
  • phospholipid catabolic process Source: InterPro
  • spindle pole body duplication Source: SGD
  • spore membrane bending pathway Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism, Meiosis, Sporulation

Enzyme and pathway databases

BioCyciYEAST:YNL012W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative meiotic phospholipase SPO1 (EC:3.1.1.-)
Alternative name(s):
Sporulation-specific protein 1
Gene namesi
Name:SPO1
Ordered Locus Names:YNL012W
ORF Names:N2858
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL012W.
SGDiS000004957. SPO1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei376 – 39621HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: SGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • nuclear membrane Source: UniProtKB-SubCell
  • nucleus Source: SGD
  • prospore membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi103 – 1031I → F in SPO1-1; defective in sporulation at 34 degrees Celsius. 1 Publication
Mutagenesisi122 – 1221S → A: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 631614Putative meiotic phospholipase SPO1PRO_0000120569Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence analysis
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence analysis
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence analysis
Glycosylationi500 – 5001N-linked (GlcNAc...)Sequence analysis
Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence analysis
Glycosylationi560 – 5601N-linked (GlcNAc...)Sequence analysis
Glycosylationi563 – 5631N-linked (GlcNAc...)Sequence analysis
Glycosylationi572 – 5721N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

Induced early in sporulation. Not detected during vegetative growth.1 Publication

Interactioni

Subunit structurei

Interacts with SPO23.1 Publication

Protein-protein interaction databases

BioGridi35813. 18 interactions.
DIPiDIP-1650N.
IntActiP53541. 4 interactions.
MINTiMINT-389680.

Structurei

3D structure databases

ProteinModelPortaliP53541.
SMRiP53541. Positions 6-131.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 631608PLA2cPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 6744Required for lipid-binding and function in meiosisAdd
BLAST

Sequence similaritiesi

Belongs to the lysophospholipase family.Curated
Contains 1 PLA2c domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00510000051940.
HOGENOMiHOG000074554.
InParanoidiP53541.
KOiK13357.
OMAiYSDYIAG.
OrthoDBiEOG7RJQ1R.

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamiPF01735. PLA2_B. 2 hits.
[Graphical view]
SMARTiSM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 2 hits.
PROSITEiPS51210. PLA2C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P53541-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKLLFVFSV LLTVVLATAP FQVQCPSSPL IREAKHELCP EETLYLKKKK
60 70 80 90 100
IKTKNKLIQF LKSLTEAKFS SKFYKRVLKD PPKIGIAISG GGYRSMLVGT
110 120 130 140 150
GFISQMNDYG LFEYSDYIAG LSGGSWILMD LVVQNFEVKS LLQEWDLEED
160 170 180 190 200
LLLGIPEFDI SEEEIVTNAK KEYNDNDLKM KKRQGGSLIT SSSNFYEQIE
210 220 230 240 250
EIMNSIEEIP EDYMITKRNL NPLARLKKIF FPNNTFTGTD AKIETFKKVL
260 270 280 290 300
DFYKSLHLKI KPKKMEGFQI SFTDYWGKAI VQRLKKNFDD DPNHSFSFSK
310 320 330 340 350
LVNSSKKFKE CSVPIPIFVA NCKNGLLSNV IFEFTPFEFG SWENILRLFV
360 370 380 390 400
KLPYLGSKIV SGKAEKCINN FDDLGFITAT SSSIFNNVLI FIWNLASQSS
410 420 430 440 450
REAMKALNMV MGIFGLGKEE IFSISKDSSR LETDYAVYQP NPFYLYPEKD
460 470 480 490 500
NVLTNKNHLY LVDGGEDGEN IPLRTLVIPE RELDVIFVLD SSSDIDNYPN
510 520 530 540 550
GSKLKRIFEK LDEENVHYQF PNNVKTFTHP IVIGCNATKR TGHDSFLPII
560 570 580 590 600
IYHANANHGN ASNTSTFKIT YNQSEVSSML PTGRGVFSND YDLYYKNCLG
610 620 630
CILTKRTMDR LPRKKKFSPF CLQCFKDYCY S
Length:631
Mass (Da):72,187
Last modified:September 5, 2006 - v2
Checksum:i2861BD03FB19C2D3
GO

Sequence cautioni

The sequence AAB38425.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAA95872.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39372 Genomic DNA. Translation: AAB38425.1. Sequence problems.
Z71288 Genomic DNA. Translation: CAA95872.1. Sequence problems.
BK006947 Genomic DNA. Translation: DAA10531.1.
PIRiS62110.
RefSeqiNP_014386.2. NM_001182851.1.

Genome annotation databases

EnsemblFungiiYNL012W; YNL012W; YNL012W.
GeneIDi855720.
KEGGisce:YNL012W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39372 Genomic DNA. Translation: AAB38425.1. Sequence problems.
Z71288 Genomic DNA. Translation: CAA95872.1. Sequence problems.
BK006947 Genomic DNA. Translation: DAA10531.1.
PIRiS62110.
RefSeqiNP_014386.2. NM_001182851.1.

3D structure databases

ProteinModelPortaliP53541.
SMRiP53541. Positions 6-131.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35813. 18 interactions.
DIPiDIP-1650N.
IntActiP53541. 4 interactions.
MINTiMINT-389680.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL012W; YNL012W; YNL012W.
GeneIDi855720.
KEGGisce:YNL012W.

Organism-specific databases

EuPathDBiFungiDB:YNL012W.
SGDiS000004957. SPO1.

Phylogenomic databases

GeneTreeiENSGT00510000051940.
HOGENOMiHOG000074554.
InParanoidiP53541.
KOiK13357.
OMAiYSDYIAG.
OrthoDBiEOG7RJQ1R.

Enzyme and pathway databases

BioCyciYEAST:YNL012W-MONOMER.

Miscellaneous databases

PROiP53541.

Family and domain databases

InterProiIPR016035. Acyl_Trfase/lysoPLipase.
IPR002642. LysoPLipase_cat_dom.
[Graphical view]
PfamiPF01735. PLA2_B. 2 hits.
[Graphical view]
SMARTiSM00022. PLAc. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 2 hits.
PROSITEiPS51210. PLA2C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The SPO1 gene product required for meiosis in yeast has a high similarity to phospholipase B enzymes."
    Tevzadze G.G., Mushegian A.R., Esposito R.E.
    Gene 177:253-255(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [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. "Spo1, a phospholipase B homolog, is required for spindle pole body duplication during meiosis in Saccharomyces cerevisiae."
    Tevzadze G.G., Swift H., Esposito R.E.
    Chromosoma 109:72-85(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-103 AND SER-122.
  5. "Test of intron predictions reveals novel splice sites, alternatively spliced mRNAs and new introns in meiotically regulated genes of yeast."
    Davis C.A., Grate L., Spingola M., Ares M. Jr.
    Nucleic Acids Res. 28:1700-1706(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF INTRON.
  6. "Genetic evidence for a SPO1-dependent signaling pathway controlling meiotic progression in yeast."
    Tevzadze G.G., Pierce J.V., Esposito R.E.
    Genetics 175:1213-1227(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SPO23, SUBCELLULAR LOCATION, GLYCOSYLATION, LIPID-BINDING REGION.

Entry informationi

Entry nameiSPO1_YEAST
AccessioniPrimary (citable) accession number: P53541
Secondary accession number(s): D6W1G5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 5, 2006
Last modified: June 8, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.