CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008698
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative meiotic phospholipase SPO1 
Protein Synonyms/Alias
 Sporulation-specific protein 1 
Gene Name
 SPO1 
Gene Synonyms/Alias
 YNL012W; N2858 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
426EEIFSISKDSSRLETacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919
Functional Description
 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. 
Sequence Annotation
 DOMAIN 24 631 PLA2c.
 REGION 24 67 Required for lipid-binding and function
 CARBOHYD 233 233 N-linked (GlcNAc...) (Potential).
 CARBOHYD 293 293 N-linked (GlcNAc...) (Potential).
 CARBOHYD 303 303 N-linked (GlcNAc...) (Potential).
 CARBOHYD 500 500 N-linked (GlcNAc...) (Potential).
 CARBOHYD 536 536 N-linked (GlcNAc...) (Potential).
 CARBOHYD 560 560 N-linked (GlcNAc...) (Potential).
 CARBOHYD 563 563 N-linked (GlcNAc...) (Potential).
 CARBOHYD 572 572 N-linked (GlcNAc...) (Potential).  
Keyword
 Complete proteome; Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Meiosis; Membrane; Nucleus; Reference proteome; Signal; Sporulation; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 631 AA 
Protein Sequence
MQKLLFVFSV LLTVVLATAP FQVQCPSSPL IREAKHELCP EETLYLKKKK IKTKNKLIQF 60
LKSLTEAKFS SKFYKRVLKD PPKIGIAISG GGYRSMLVGT GFISQMNDYG LFEYSDYIAG 120
LSGGSWILMD LVVQNFEVKS LLQEWDLEED LLLGIPEFDI SEEEIVTNAK KEYNDNDLKM 180
KKRQGGSLIT SSSNFYEQIE EIMNSIEEIP EDYMITKRNL NPLARLKKIF FPNNTFTGTD 240
AKIETFKKVL DFYKSLHLKI KPKKMEGFQI SFTDYWGKAI VQRLKKNFDD DPNHSFSFSK 300
LVNSSKKFKE CSVPIPIFVA NCKNGLLSNV IFEFTPFEFG SWENILRLFV KLPYLGSKIV 360
SGKAEKCINN FDDLGFITAT SSSIFNNVLI FIWNLASQSS REAMKALNMV MGIFGLGKEE 420
IFSISKDSSR LETDYAVYQP NPFYLYPEKD NVLTNKNHLY LVDGGEDGEN IPLRTLVIPE 480
RELDVIFVLD SSSDIDNYPN GSKLKRIFEK LDEENVHYQF PNNVKTFTHP IVIGCNATKR 540
TGHDSFLPII IYHANANHGN ASNTSTFKIT YNQSEVSSML PTGRGVFSND YDLYYKNCLG 600
CILTKRTMDR LPRKKKFSPF CLQCFKDYCY S 631 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:SGD.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0005628; C:prospore membrane; IDA:SGD.
 GO:0004620; F:phospholipase activity; ISS:SGD.
 GO:0007126; P:meiosis; IMP:SGD.
 GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
 GO:0070583; P:spore membrane bending pathway; IMP:SGD. 
Interpro
 IPR016035; Acyl_Trfase/lysoPLipase.
 IPR002642; LysoPLipase_cat_dom. 
Pfam
 PF01735; PLA2_B 
SMART
 SM00022; PLAc 
PROSITE
 PS51210; PLA2C 
PRINTS