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Q8BSF4 (PISD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the phosphatidylserine decarboxylase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   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 – 374374Phosphatidylserine decarboxylase beta chain
PRO_0000029837
Chain375 – 40632Phosphatidylserine decarboxylase alpha chain
PRO_0000029838

Sites

Site374 – 3752Cleavage (non-hydrolytic) By similarity

Amino acid modifications

Modified residue3751Pyruvic acid (Ser) By similarity

Experimental info

Sequence conflict338 – 3403SPR → KPK in BAC28786. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BSF4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 6614312FA8BA9704

FASTA40645,927
        10         20         30         40         50         60 
MAASGGRACV RSLRGGVLWR SSPCHYESTA TRHFLGTLQK LPLQAGVRNF HTAPVRSLFL 

        70         80         90        100        110        120 
LRPVPILLAT GGGYAGYRQY EKYRERKLEK LGLEIPPKLA SHWEVSLYKS VPTRLLSRAC 

       130        140        150        160        170        180 
GRLNQVELPY WLRRPVYSLY IWTFGVNMTE AAVEDLHHYR NLSEFFRRKL KPQARPVCGL 

       190        200        210        220        230        240 
HCVTSPSDGK ILTFGQVKNS EVEQVKGVTY SLESFLGPRA NTEDLPFPPA SSSDSFRNQL 

       250        260        270        280        290        300 
VTREGNELYH CVIYLAPGDY HCFHSPTDWT ISHRRHFPGS LMSVNPGMAR WIKELFCHNE 

       310        320        330        340        350        360 
RVVLTGDWKH GFFSLTAVGA TNVGSIRIHF DRDLHTNSPR YSKGSYNDLS FVTHANKEGI 

       370        380        390        400 
PMRKGEPLGE FNLGSTIVLI FEAPKDFNFR LKAGQKIRFG EALGSL

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Colon.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK033483 mRNA. Translation: BAC28313.1.
AK034656 mRNA. Translation: BAC28786.1.
BC070408 mRNA. Translation: AAH70408.1.
IPIIPI00310099.
RefSeqNP_796272.2. NM_177298.3.
UniGeneMm.273765.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BSF4.

PTM databases

PhosphoSiteQ8BSF4.

Proteomic databases

PRIDEQ8BSF4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000061895; ENSMUSP00000051438; ENSMUSG00000023452.
GeneID320951.
KEGGmmu:320951.

Organism-specific databases

CTD23761.
MGIMGI:2445114. Pisd.

Phylogenomic databases

GeneTreeENSGT00390000013484.
HOGENOMHBG395511.
HOVERGENHBG039630.
InParanoidQ8BSF4.
OMAMCQSEAR.
PhylomeDBQ8BSF4.

Gene expression databases

ArrayExpressQ8BSF4.
BgeeQ8BSF4.
CleanExMM_PISD.
GenevestigatorQ8BSF4.
GermOnlineENSMUSG00000023452. Mus musculus.

Family and domain databases

InterProIPR003817. PS_Dcarbxylase.
IPR005221. PS_decarb.
[Graphical view]
KOK01613.
PANTHERPTHR10067. PS_decarb. 1 hit.
PfamPF02666. PS_Dcarbxylase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00163. PS_decarb. 1 hit.
ProtoNetSearch...

Other

NextBio397752.
SOURCESearch...

Entry information

Entry namePISD_MOUSE
AccessionPrimary (citable) accession number: Q8BSF4
Secondary accession number(s): Q8BSD6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: March 1, 2003
Last modified: November 16, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents