ID SPO1_YEAST Reviewed; 631 AA.
AC P53541; D6W1G5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Putative meiotic phospholipase SPO1;
DE EC=3.1.1.-;
DE AltName: Full=Sporulation-specific protein 1;
DE Flags: Precursor;
GN Name=SPO1; OrderedLocusNames=YNL012W; ORFNames=N2858;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8921875; DOI=10.1016/0378-1119(96)00261-2;
RA Tevzadze G.G., Mushegian A.R., Esposito R.E.;
RT "The SPO1 gene product required for meiosis in yeast has a high similarity
RT to phospholipase B enzymes.";
RL Gene 177:253-255(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-103 AND
RP SER-122.
RX PubMed=10855497; DOI=10.1007/s004120050414;
RA Tevzadze G.G., Swift H., Esposito R.E.;
RT "Spo1, a phospholipase B homolog, is required for spindle pole body
RT duplication during meiosis in Saccharomyces cerevisiae.";
RL Chromosoma 109:72-85(2000).
RN [5]
RP IDENTIFICATION OF INTRON.
RX PubMed=10734188; DOI=10.1093/nar/28.8.1700;
RA Davis C.A., Grate L., Spingola M., Ares M. Jr.;
RT "Test of intron predictions reveals novel splice sites, alternatively
RT spliced mRNAs and new introns in meiotically regulated genes of yeast.";
RL Nucleic Acids Res. 28:1700-1706(2000).
RN [6]
RP FUNCTION, INTERACTION WITH SPO23, SUBCELLULAR LOCATION, GLYCOSYLATION, AND
RP LIPID-BINDING REGION.
RX PubMed=17179081; DOI=10.1534/genetics.106.069252;
RA Tevzadze G.G., Pierce J.V., Esposito R.E.;
RT "Genetic evidence for a SPO1-dependent signaling pathway controlling
RT meiotic progression in yeast.";
RL Genetics 175:1213-1227(2007).
CC -!- FUNCTION: Regulates spindle pole duplication in meiosis I, but not in
CC mitosis. Required for meiosis I, meiosis II chromosome segregation and
CC spore formation. Binds phosphatidylinositol (4)P mono- and
CC polyphosphates. {ECO:0000269|PubMed:10855497,
CC ECO:0000269|PubMed:17179081}.
CC -!- SUBUNIT: Interacts with SPO23. {ECO:0000269|PubMed:17179081}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein. Nucleus membrane; Single-pass membrane protein.
CC -!- INDUCTION: Induced early in sporulation. Not detected during vegetative
CC growth. {ECO:0000269|PubMed:10855497}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:17179081}.
CC -!- SIMILARITY: Belongs to the lysophospholipase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB38425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA95872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L39372; AAB38425.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z71288; CAA95872.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006947; DAA10531.1; -; Genomic_DNA.
DR PIR; S62110; S62110.
DR RefSeq; NP_014386.2; NM_001182851.1.
DR AlphaFoldDB; P53541; -.
DR SMR; P53541; -.
DR BioGRID; 35813; 112.
DR DIP; DIP-1650N; -.
DR IntAct; P53541; 12.
DR MINT; P53541; -.
DR STRING; 4932.YNL012W; -.
DR GlyCosmos; P53541; 8 sites, No reported glycans.
DR GlyGen; P53541; 8 sites.
DR PaxDb; 4932-YNL012W; -.
DR PeptideAtlas; P53541; -.
DR EnsemblFungi; YNL012W_mRNA; YNL012W; YNL012W.
DR GeneID; 855720; -.
DR KEGG; sce:YNL012W; -.
DR AGR; SGD:S000004957; -.
DR SGD; S000004957; SPO1.
DR VEuPathDB; FungiDB:YNL012W; -.
DR eggNOG; KOG1325; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_014602_2_0_1; -.
DR InParanoid; P53541; -.
DR OMA; FIANCRN; -.
DR OrthoDB; 1980513at2759; -.
DR BioCyc; YEAST:YNL012W-MONOMER; -.
DR Reactome; R-SCE-111995; phospho-PLA2 pathway.
DR Reactome; R-SCE-1482788; Acyl chain remodelling of PC.
DR Reactome; R-SCE-1482798; Acyl chain remodeling of CL.
DR Reactome; R-SCE-1482801; Acyl chain remodelling of PS.
DR Reactome; R-SCE-1482839; Acyl chain remodelling of PE.
DR Reactome; R-SCE-1482922; Acyl chain remodelling of PI.
DR Reactome; R-SCE-1482925; Acyl chain remodelling of PG.
DR Reactome; R-SCE-1483115; Hydrolysis of LPC.
DR Reactome; R-SCE-1483152; Hydrolysis of LPE.
DR Reactome; R-SCE-1483166; Synthesis of PA.
DR Reactome; R-SCE-2142753; Arachidonic acid metabolism.
DR Reactome; R-SCE-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-SCE-432142; Platelet sensitization by LDL.
DR Reactome; R-SCE-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR PRO; PR:P53541; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53541; Protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0004620; F:phospholipase activity; ISS:SGD.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:SGD.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR GO; GO:0030474; P:spindle pole body duplication; IMP:SGD.
DR GO; GO:0070583; P:spore membrane bending pathway; IMP:SGD.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR10728:SF56; MEIOTIC PHOSPHOLIPASE SPO1-RELATED; 1.
DR Pfam; PF01735; PLA2_B; 2.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS51210; PLA2C; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Meiosis; Membrane; Nucleus; Reference proteome; Signal;
KW Sporulation; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..631
FT /note="Putative meiotic phospholipase SPO1"
FT /id="PRO_0000120569"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 24..631
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT REGION 24..67
FT /note="Required for lipid-binding and function in meiosis"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 103
FT /note="I->F: In SPO1-1; defective in sporulation at 34
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:10855497"
FT MUTAGEN 122
FT /note="S->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:10855497"
SQ SEQUENCE 631 AA; 72187 MW; 2861BD03FB19C2D3 CRC64;
MQKLLFVFSV LLTVVLATAP FQVQCPSSPL IREAKHELCP EETLYLKKKK IKTKNKLIQF
LKSLTEAKFS SKFYKRVLKD PPKIGIAISG GGYRSMLVGT GFISQMNDYG LFEYSDYIAG
LSGGSWILMD LVVQNFEVKS LLQEWDLEED LLLGIPEFDI SEEEIVTNAK KEYNDNDLKM
KKRQGGSLIT SSSNFYEQIE EIMNSIEEIP EDYMITKRNL NPLARLKKIF FPNNTFTGTD
AKIETFKKVL DFYKSLHLKI KPKKMEGFQI SFTDYWGKAI VQRLKKNFDD DPNHSFSFSK
LVNSSKKFKE CSVPIPIFVA NCKNGLLSNV IFEFTPFEFG SWENILRLFV KLPYLGSKIV
SGKAEKCINN FDDLGFITAT SSSIFNNVLI FIWNLASQSS REAMKALNMV MGIFGLGKEE
IFSISKDSSR LETDYAVYQP NPFYLYPEKD NVLTNKNHLY LVDGGEDGEN IPLRTLVIPE
RELDVIFVLD SSSDIDNYPN GSKLKRIFEK LDEENVHYQF PNNVKTFTHP IVIGCNATKR
TGHDSFLPII IYHANANHGN ASNTSTFKIT YNQSEVSSML PTGRGVFSND YDLYYKNCLG
CILTKRTMDR LPRKKKFSPF CLQCFKDYCY S
//
