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P27465 (PISD_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphatidylserine decarboxylase proenzyme
EC=4.1.1.65

Cleaved into the following 2 chains:

  1. Phosphatidylserine decarboxylase alpha chain
  2. Phosphatidylserine decarboxylase beta chain
Gene names
Name:PISD
Synonyms:PSSC
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Phosphatidyl-L-serine = phosphatidylethanolamine + CO2.

Cofactor

Pyruvoyl group By similarity.

Pathway

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

Subunit structure

Heterodimer.

Subcellular location

Mitochondrion Ref.2.

Sequence similarities

Belongs to the phosphatidylserine decarboxylase family.

Sequence caution

The sequence CAA56630.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentMitochondrion
   LigandPyruvate
   Molecular functionDecarboxylase
Lyase
   PTMZymogen
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionphosphatidylserine decarboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Phosphatidylserine decarboxylase beta chain
PRO_0000029833
Chain378 – 40932Phosphatidylserine decarboxylase alpha chain
PRO_0000029834

Sites

Site377 – 3782Cleavage (non-hydrolytic)

Amino acid modifications

Modified residue3781Pyruvic acid (Ser) By similarity

Experimental info

Mutagenesis3781S → A: Blocks the formation of alpha chain. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P27465 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: F034559B714EE6F5

FASTA40946,758
        10         20         30         40         50         60 
MAASVCRPYV RSLPGVMPWR SSSCHYEYTA MHHFLGSFQK LPFEPFNTGA RKIHTAPVRS 

        70         80         90        100        110        120 
LFLLRPVPIL LATGGGYAGY RQYEKYRDQK LEKLGLEIPP KLASHWEVAL YKSVPTRLLS 

       130        140        150        160        170        180 
RAWGRLNQVE LPYWLRRPVY SLYIWTFGVN MTEAAVEDLH HYRNLSEFFR RKLKPQARPV 

       190        200        210        220        230        240 
CGLHSVISPS DGKILTFGQV KNCEVEQVKG VTYSLESFLG PRTYTEDLSF PPASSRDSFR 

       250        260        270        280        290        300 
NQLVTREGNE LYHCVIYLAP GDYHCFHSPT DWTVSHRRHF PGSLMSVNPG MARWIKELFC 

       310        320        330        340        350        360 
HNERVVLSGD WKHGFFSLTA VGATNVGSIR IYFDQDLHTN SPRYSKGSYN DLSFVTHANK 

       370        380        390        400 
EGIPMRKGEH LGEFNLGSTI VLIFEAPKDF NFRLKAGQKI RFGEALGSL

« Hide

References

[1]"A cloned gene encoding phosphatidylserine decarboxylase complements the phosphatidylserine biosynthetic defect of a Chinese hamster ovary cell mutant."
Kuge O., Nishijima M., Akamatsu Y.
J. Biol. Chem. 266:6370-6376(1991) [PubMed: 2007589] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-409.
[2]"Post-translational processing of the phosphatidylserine decarboxylase gene product in Chinese hamster ovary cells."
Kuge O., Saito K., Kojima M., Akamatsu Y., Nishijima M.
Biochem. J. 319:33-38(1996) [PubMed: 8870646] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-99, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-378.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M62722 mRNA. Translation: AAA37015.1.
X80455 mRNA. Translation: CAA56630.1. Different initiation.
PIRS72438.
RefSeqXP_003504168.1. XM_003504120.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689093.

Phylogenomic databases

HOVERGENHBG039630.

Family and domain databases

InterProIPR003817. PS_Dcarbxylase.
IPR005221. PS_decarb.
[Graphical view]
PANTHERPTHR10067. PS_decarb. 1 hit.
PfamPF02666. PS_Dcarbxylase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00163. PS_decarb. 1 hit.
ProtoNetSearch...

Entry information

Entry namePISD_CRIGR
AccessionPrimary (citable) accession number: P27465
Secondary accession number(s): Q64402
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 16, 2004
Last modified: January 25, 2012
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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