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Reviewed, UniProtKB/Swiss-Prot O14333 (PSD2_SCHPO)

Last modified October 13, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphatidylserine decarboxylase proenzyme 2, mitochondrial
    EC=4.1.1.65
Cleaved into the following 2 chains:
    1- Recommended name:
            Phosphatidylserine decarboxylase 2 beta chain
    2- Recommended name:
            Phosphatidylserine decarboxylase 2 alpha chain
Gene names
ORF Names: SPBC16E9.18, SPBC1E8.01
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

May be involved in the regulation of phospholipid biosynthesis and interorganelle trafficking of phosphatidylserine By similarity.

Catalytic activity

Phosphatidyl-L-serine = phosphatidylethanolamine + CO2.

Cofactor

Pyruvoyl group By similarity.

Pathway

Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.

Subcellular location

Mitochondrion. Ref.2

Sequence similarities

Belongs to the phosphatidylserine decarboxylase family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
   Molecular functionDecarboxylase
Lyase
   PTMZymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphosphatidylethanolamine biosynthetic process

Inferred from genetic interaction. Source: GeneDB_SPombe

regulation of cell morphogenesis

Inferred from genetic interaction. Source: GeneDB_SPombe

regulation of cytokinesis

Inferred from genetic interaction. Source: GeneDB_SPombe

   Cellular componentmitochondrion Ref.2

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionphosphatidylserine decarboxylase activity

Inferred from genetic interaction. Source: GeneDB_SPombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Potential
Chain29 – 437409Phosphatidylserine decarboxylase proenzyme 2, mitochondrial
PRO_0000353844
Chain29 – 400372Phosphatidylserine decarboxylase 2 beta chain
PRO_0000353845
Chain401 – 43737Phosphatidylserine decarboxylase 2 alpha chain
PRO_0000353846

Sites

Site400 – 4012Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue4011Pyruvic acid (Ser) By similarity

Sequences

Sequence LengthMass (Da)Tools
O14333-1 [UniParc].

Last modified August 21, 2007. Version 4.
Checksum: 792178F93BDB47DA

FASTA43749,129
        10         20         30         40         50         60 
MLKFHRNVKP QFGAFARYSS LGKHNSRKRV GIIRLAYGLT GIGLVGLAGF AWAQDRHEKT 

        70         80         90        100        110        120 
YQKKGVQVEG PWQFYVLTTL PLRTLSRWWG YVNRIEIPLW MRVPAFGLYS KIFGCNLTEA 

       130        140        150        160        170        180 
DPDDVRQYKN LAEFFTRKLK PGARVIDPDA PIVIPADGKI LNYGVIEGGQ LEQVKGITYS 

       190        200        210        220        230        240 
LDALLGDEKL ARLKRSHAIP SPDHIPHIRQ EEFAKLNGIH YSLQDLMGHD HGERPSHVKD 

       250        260        270        280        290        300 
ASAQHIDLLS STKVAAKSQF TLFGSRETNC LYYAVIYLAP GDYHRFHSPT DWVVERRRHF 

       310        320        330        340        350        360 
SGELFSVSPF MARRLGNLFI LNERVALMGR YKYGFMSMIP VGATNVGSIR IKFDKDLCTN 

       370        380        390        400        410        420 
QFGKLGPVGT FDEAVYTSSS SILHGHPLLR GDEVGNFELG STVVLVFEAP ADFEFLVKQG 

       430 
QKVRVGLPLG RVVPSSH 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

CU329671 Genomic DNA. Translation: CAB16910.2.
RefSeqNP_595799.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO14333.

Genome annotation databases

GeneID2539756.
KEGGspo:SPBC16E9.18.

Organism-specific databases

GeneDB_SpombeSPBC16E9.18.

Gene expression databases

ArrayExpressO14333.

Family and domain databases

InterProIPR003817. PS_Dcarbxylase.
IPR005221. PS_decarb.
[Graphical view]
PfamPF02666. PS_Dcarbxylase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00163. PS_decarb. 1 hit.
ProtoNetSearch...

Entry information

Entry namePSD2_SCHPO
AccessionPrimary (citable) accession number: O14333
Secondary accession number(s): O42966
Entry history
Integrated into UniProtKB/Swiss-Prot: November 4, 2008
Last sequence update: August 21, 2007
Last modified: October 13, 2009
This is version 51 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents