PISD
entrez
23761
canonical
uniprot
Q9UG56
canonical
ensembl
ENSG00000241878
resolver
ensp
ENSP00000266095
resolver
ensp
ENSP00000391739
resolver
ensp
ENSP00000562663
resolver
ensp
ENSP00000661866
resolver
genesymbol
PISD
resolver
hgnc
HGNC:8999
resolver
uniprot
B1AKM7
resolver
uniprot
O43207
resolver
uniprot
O95535
resolver
uniprot
Q6IC28
resolver
uniprot
Q96GQ2
resolver
uniprot
Q9UGA9
resolver
uniprot_entry
PISD_HUMAN
resolver
uniprot_sec
B1AKM7
resolver
uniprot_sec
O43207
resolver
uniprot_sec
O95535
resolver
uniprot_sec
Q6IC28
resolver
uniprot_sec
Q96GQ2
resolver
uniprot_sec
Q9UGA9
resolver
amino_acid_sequence
MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL
uniprot
proteins
disease_involvement
DISEASE: Liberfarb syndrome (LIBF) [MIM:618889]: An 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. {ECO:0000269|PubMed:30488656, ECO:0000269|PubMed:30858161, ECO:0000269|PubMed:31263216}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
4.1.1.65
uniprot
proteins
function
FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer) (PubMed:30488656, PubMed:30858161). 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). {ECO:0000250|UniProtKB:A0A8H4BVL9, ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:30488656, ECO:0000269|PubMed:30858161}.
uniprot
proteins
mass_dalton
46672
uniprot
proteins
mutagenesis
MUTAGEN 378; /note="S->A: Loss of autocatalytic processing."; /evidence="ECO:0000269|PubMed:30858161
uniprot
proteins
pathway_participation
PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis. {ECO:0000269|PubMed:30858161}.
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:30858161}.
uniprot
proteins
protein_family
Eukaryotic type I sub-subfamily
uniprot
proteins
protein_family
PSD-B subfamily
uniprot
proteins
protein_family
Phosphatidylserine decarboxylase family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
30488656
uniprot
proteins
pubmed
30858161
uniprot
proteins
pubmed
31263216
uniprot
proteins
pubmed
33593792
uniprot
proteins
pubmed
33718843
uniprot
proteins
sequence_length
409
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase beta chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:30858161, ECO:0000305|PubMed:33718843}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}.; SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase alpha chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:30858161, ECO:0000305|PubMed:33718843}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Cytoplasm {ECO:0000269|PubMed:33593792}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion inner membrane {ECO:0000269|PubMed:33593792}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion inner membrane {ECO:0000269|PubMed:33593792}. Lipid droplet {ECO:0000269|PubMed:33593792}. Note=Predominantly localizes to lipid droplets in lipid-replete conditions, and to mitochondria in lipid-deplete conditions. {ECO:0000269|PubMed:33593792}.
uniprot
proteins
transmembrane_region
TRANSMEM 64..82; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208
uniprot
proteins