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Protein

Phosphatidylserine decarboxylase proenzyme, mitochondrial

Gene

Pisd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine.UniRule annotation

Catalytic activityi

Phosphatidyl-L-serine = phosphatidylethanolamine + CO2.UniRule annotation

Cofactori

pyruvateUniRule annotationNote: Binds 1 pyruvoyl group covalently per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei188 – 1881Charge relay system; for autoendoproteolytic cleavage activityUniRule annotation
Active sitei264 – 2641Charge relay system; for autoendoproteolytic cleavage activityUniRule annotation
Active sitei375 – 3751Charge relay system; for autoendoproteolytic cleavage activityUniRule annotation
Active sitei375 – 3751Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activityUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

Pyruvate

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylserine decarboxylase proenzyme, mitochondrialUniRule annotation (EC:4.1.1.65UniRule annotation)
Cleaved into the following 2 chains:
Phosphatidylserine decarboxylase beta chainUniRule annotation
Phosphatidylserine decarboxylase alpha chainUniRule annotation
Gene namesi
Name:PisdUniRule annotation
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2445114. Pisd.

Subcellular locationi

Chain Phosphatidylserine decarboxylase beta chain :
  • Mitochondrion inner membrane UniRule annotation1 Publication; Single-pass membrane protein UniRule annotation; Intermembrane side UniRule annotation
Chain Phosphatidylserine decarboxylase alpha chain :
  • Mitochondrion inner membrane UniRule annotation1 Publication; Peripheral membrane protein UniRule annotation; Intermembrane side UniRule annotation

  • Note: Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain.UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini50 – 6011Mitochondrial matrixUniRule annotationAdd
BLAST
Transmembranei61 – 7919HelicalUniRule annotationAdd
BLAST
Topological domaini80 – 406327Mitochondrial intermembraneUniRule annotationAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial inner membrane Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Disruption phenotypei

Mutant embryos die in utero between 8 and 10 dpc. They exhibit large numbers of aberrantly shaped mitochondria. In mutant embryonic fibroblasts, fragmented, rounded mitochondria of irregular diameter are widely dispersed throughout the cell rather than being concentrated around the nucleus.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4949MitochondrionUniRule annotationAdd
BLAST
Chaini50 – 406357Phosphatidylserine decarboxylase proenzymePRO_0000435572Add
BLAST
Chaini50 – 374325Phosphatidylserine decarboxylase beta chainUniRule annotationPRO_0000029837Add
BLAST
Chaini375 – 40632Phosphatidylserine decarboxylase alpha chainUniRule annotationPRO_0000029838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei375 – 3751Pyruvic acid (Ser); by autocatalysisUniRule annotation

Post-translational modificationi

Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei374 – 3752Cleavage (non-hydrolytic); by autocatalysisUniRule annotation

Keywords - PTMi

Zymogen

Proteomic databases

EPDiQ8BSF4.
MaxQBiQ8BSF4.
PaxDbiQ8BSF4.
PeptideAtlasiQ8BSF4.
PRIDEiQ8BSF4.

PTM databases

iPTMnetiQ8BSF4.
PhosphoSiteiQ8BSF4.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in testis, including Sertoli cells, followed by liver.1 Publication

Developmental stagei

Expressed during development in tissues rich in mitochondria, such as heart. In liver, low expression level observed in embryos and newborn animals increases 10-fold in adult.1 Publication

Gene expression databases

BgeeiQ8BSF4.
CleanExiMM_PISD.
ExpressionAtlasiQ8BSF4. baseline and differential.
GenevisibleiQ8BSF4. MM.

Interactioni

Subunit structurei

Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051438.

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily.UniRule annotation

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2420. Eukaryota.
COG0688. LUCA.
GeneTreeiENSGT00390000013484.
HOGENOMiHOG000282409.
HOVERGENiHBG039630.
InParanoidiQ8BSF4.
KOiK01613.
PhylomeDBiQ8BSF4.
TreeFamiTF313148.

Family and domain databases

HAMAPiMF_03208. PS_decarb_PSD_B_type1_euk.
InterProiIPR003817. PS_Dcarbxylase.
IPR033177. PSD.
[Graphical view]
PANTHERiPTHR10067. PTHR10067. 1 hit.
PfamiPF02666. PS_Dcarbxylase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00163. PS_decarb. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BSF4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASGGRACV RSLRGGVLWR SSPCHYESTA TRHFLGTLQK LPLQAGVRNF
60 70 80 90 100
HTAPVRSLFL LRPVPILLAT GGGYAGYRQY EKYRERKLEK LGLEIPPKLA
110 120 130 140 150
SHWEVSLYKS VPTRLLSRAC GRLNQVELPY WLRRPVYSLY IWTFGVNMTE
160 170 180 190 200
AAVEDLHHYR NLSEFFRRKL KPQARPVCGL HCVTSPSDGK ILTFGQVKNS
210 220 230 240 250
EVEQVKGVTY SLESFLGPRA NTEDLPFPPA SSSDSFRNQL VTREGNELYH
260 270 280 290 300
CVIYLAPGDY HCFHSPTDWT ISHRRHFPGS LMSVNPGMAR WIKELFCHNE
310 320 330 340 350
RVVLTGDWKH GFFSLTAVGA TNVGSIRIHF DRDLHTNSPR YSKGSYNDLS
360 370 380 390 400
FVTHANKEGI PMRKGEPLGE FNLGSTIVLI FEAPKDFNFR LKAGQKIRFG

EALGSL
Length:406
Mass (Da):45,927
Last modified:March 1, 2003 - v1
Checksum:i6614312FA8BA9704
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti338 – 3403SPR → KPK in BAC28786 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033483 mRNA. Translation: BAC28313.1.
AK034656 mRNA. Translation: BAC28786.1.
BC070408 mRNA. Translation: AAH70408.1.
CCDSiCCDS19194.1.
RefSeqiNP_796272.2. NM_177298.3.
UniGeneiMm.273765.

Genome annotation databases

EnsembliENSMUST00000061895; ENSMUSP00000051438; ENSMUSG00000023452.
GeneIDi320951.
KEGGimmu:320951.
UCSCiuc008wzv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033483 mRNA. Translation: BAC28313.1.
AK034656 mRNA. Translation: BAC28786.1.
BC070408 mRNA. Translation: AAH70408.1.
CCDSiCCDS19194.1.
RefSeqiNP_796272.2. NM_177298.3.
UniGeneiMm.273765.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051438.

PTM databases

iPTMnetiQ8BSF4.
PhosphoSiteiQ8BSF4.

Proteomic databases

EPDiQ8BSF4.
MaxQBiQ8BSF4.
PaxDbiQ8BSF4.
PeptideAtlasiQ8BSF4.
PRIDEiQ8BSF4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000061895; ENSMUSP00000051438; ENSMUSG00000023452.
GeneIDi320951.
KEGGimmu:320951.
UCSCiuc008wzv.1. mouse.

Organism-specific databases

CTDi23761.
MGIiMGI:2445114. Pisd.

Phylogenomic databases

eggNOGiKOG2420. Eukaryota.
COG0688. LUCA.
GeneTreeiENSGT00390000013484.
HOGENOMiHOG000282409.
HOVERGENiHBG039630.
InParanoidiQ8BSF4.
KOiK01613.
PhylomeDBiQ8BSF4.
TreeFamiTF313148.

Miscellaneous databases

ChiTaRSiPisd. mouse.
PROiQ8BSF4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BSF4.
CleanExiMM_PISD.
ExpressionAtlasiQ8BSF4. baseline and differential.
GenevisibleiQ8BSF4. MM.

Family and domain databases

HAMAPiMF_03208. PS_decarb_PSD_B_type1_euk.
InterProiIPR003817. PS_Dcarbxylase.
IPR033177. PSD.
[Graphical view]
PANTHERiPTHR10067. PTHR10067. 1 hit.
PfamiPF02666. PS_Dcarbxylase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00163. PS_decarb. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Phosphatidylserine decarboxylase is located on the external side of the inner mitochondrial membrane."
    Zborowski J., Dygas A., Wojtczak L.
    FEBS Lett. 157:179-182(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  4. "Disruption of the phosphatidylserine decarboxylase gene in mice causes embryonic lethality and mitochondrial defects."
    Steenbergen R., Nanowski T.S., Beigneux A., Kulinski A., Young S.G., Vance J.E.
    J. Biol. Chem. 280:40032-40040(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPISD_MOUSE
AccessioniPrimary (citable) accession number: Q8BSF4
Secondary accession number(s): Q8BSD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2003
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.