Q9UG56 · PISD_HUMAN
- ProteinPhosphatidylserine decarboxylase proenzyme, mitochondrial
- GenePISD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids409 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (By similarity).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H+ = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2This reaction proceeds in the forward direction.
Cofactor
Pathway
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 191 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: D | ||||||
Active site | 267 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: H | ||||||
Site | 377-378 | Cleavage (non-hydrolytic); by autocatalysis | ||||
Sequence: GS | ||||||
Active site | 378 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: S | ||||||
Active site | 378 | Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | Golgi apparatus | |
Cellular Component | lipid droplet | |
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | phosphatidylserine decarboxylase activity | |
Biological Process | lipid droplet formation | |
Biological Process | mitochondrial protein catabolic process | |
Biological Process | phosphatidylethanolamine biosynthetic process | |
Biological Process | protein autoprocessing | |
Biological Process | regulation of mitochondrion organization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylserine decarboxylase proenzyme, mitochondrial
- EC number
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UG56
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phosphatidylserine decarboxylase beta chain
Phosphatidylserine decarboxylase alpha chain
Isoform 1
Isoform 2
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 53-63 | Mitochondrial matrix | ||||
Sequence: IHTAPARTMFL | ||||||
Transmembrane | 64-82 | Helical | ||||
Sequence: LRPLPILLVTGGGYAGYRQ | ||||||
Topological domain | 83-409 | Mitochondrial intermembrane | ||||
Sequence: YEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Liberfarb syndrome (LIBF)
- Note
- DescriptionAn autosomal recessive multisystem disorder affecting the eye, ear, bone, and brain development. Clinical features include early-onset retinal degeneration, congenital cataracts, sensorineural hearing loss, microcephaly, intellectual disability, white matter changes, mild facial dysmorphism, and skeletal dysplasia with platyspondyly, scoliosis and short stature.
- See alsoMIM:618889
Natural variants in LIBF
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_084458 | 277 | R>Q | in LIBF; loss of autocatalytic processing; decreased protein abundance; decreased phosphatidylserine decarboxylase activity; changed mitochondrion organization; dbSNP:rs147371584 | |
VAR_084459 | 300 | C>Y | in LIBF; loss of autocatalytic processing; probably decreased phosphatidylserine decarboxylase activity; changed mitochondrion organization; patient-derived fibroblasts show fragmented mitochondrial morphology around the nucleus; decreased cell viability with increased CASP3 and CASP7 activation; dbSNP:rs2072505076 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_084458 | 277 | in LIBF; loss of autocatalytic processing; decreased protein abundance; decreased phosphatidylserine decarboxylase activity; changed mitochondrion organization; dbSNP:rs147371584 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_084459 | 300 | in LIBF; loss of autocatalytic processing; probably decreased phosphatidylserine decarboxylase activity; changed mitochondrion organization; patient-derived fibroblasts show fragmented mitochondrial morphology around the nucleus; decreased cell viability with increased CASP3 and CASP7 activation; dbSNP:rs2072505076 | |||
Sequence: C → Y | ||||||
Mutagenesis | 378 | Loss of autocatalytic processing. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 521 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-52 | UniProt | Mitochondrion | ||||
Sequence: MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARK | |||||||
Chain | PRO_0000029835 | 53-377 | UniProt | Phosphatidylserine decarboxylase beta chain | |||
Sequence: IHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLG | |||||||
Chain | PRO_0000435571 | 53-409 | UniProt | Phosphatidylserine decarboxylase proenzyme, mitochondrial | |||
Sequence: IHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL | |||||||
Modified residue (large scale data) | 341 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 378 | UniProt | Pyruvic acid (Ser); by autocatalysis | ||||
Sequence: S | |||||||
Chain | PRO_0000029836 | 378-409 | UniProt | Phosphatidylserine decarboxylase alpha chain | |||
Sequence: STIVLIFEAPKDFNFQLKTGQKIRFGEALGSL |
Post-translational modification
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UG56-2 | CIDEB Q9UHD4 | 3 | EBI-17870882, EBI-7062247 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 36-103 | In isoform Q9UG56-2; Necessary for localization to both lipid droplets and mitochondria | ||||
Sequence: QPLRKLPFRAFRTDARKIHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLA |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q9UG56-3
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsPISD-M
- Length409
- Mass (Da)46,672
- Last updated2010-11-02 v4
- Checksum6A5148265369D9DF
Q9UG56-2
- Name2
- SynonymsPISD-LD
- Differences from canonical
- 1-107: MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWE → MMCQSEARQGPELRAAKWLHFPQLALRRRLGQLSCMSRPALKLRSWPLTVLYYLLPFGALRPLSRVGWRPVSR
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_007540 | 1-107 | in isoform 2 | |||
Sequence: MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWE → MMCQSEARQGPELRAAKWLHFPQLALRRRLGQLSCMSRPALKLRSWPLTVLYYLLPFGALRPLSRVGWRPVSR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR456540 EMBL· GenBank· DDBJ | CAG30426.1 EMBL· GenBank· DDBJ | mRNA | ||
AL050371 EMBL· GenBank· DDBJ | CAB43678.2 EMBL· GenBank· DDBJ | Transcribed RNA | Sequence problems. | |
AL096768 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL031255 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471095 EMBL· GenBank· DDBJ | EAW59984.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001482 EMBL· GenBank· DDBJ | AAH01482.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009315 EMBL· GenBank· DDBJ | AAH09315.1 EMBL· GenBank· DDBJ | mRNA | ||
AF035304 EMBL· GenBank· DDBJ | AAB88186.1 EMBL· GenBank· DDBJ | mRNA |