Pisd
entrez
320951
canonical
uniprot
Q8BSF4
canonical
ensembl
ENSMUSG00000023452
resolver
ensp
ENSMUSP00000051438
resolver
ensp
ENSMUSP00000112573
resolver
ensp
ENSMUSP00000317615
resolver
ensp
ENSMUSP00000317618
resolver
ensp
ENSMUSP00000317621
resolver
ensp
ENSMUSP00000317623
resolver
enst
ENSMUST00000061895
resolver
enst
ENSMUST00000120591
resolver
genesymbol
Pisd
resolver
genesymbol_syn
PISD
resolver
uniprot
E9PX91
resolver
uniprot
Q505E1
resolver
uniprot
Q8BSD6
resolver
uniprot_entry
E9PX91_MOUSE
resolver
uniprot_entry
PISD_MOUSE
resolver
uniprot_entry
Q505E1_MOUSE
resolver
uniprot_sec
Q8BSD6
resolver
amino_acid_sequence
MAASGGRACVRSLRGGVLWRSSPCHYESTATRHFLGTLQKLPLQAGVRNFHTAPVRSLFLLRPVPILLATGGGYAGYRQYEKYRERKLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPYWLRRPVYSLYIWTFGVNMTEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHCVTSPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRANTEDLPFPPASSSDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTISHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIHFDRDLHTNSPRYSKGSYNDLSFVTHANKEGIPMRKGEPLGEFNLGSTIVLIFEAPKDFNFRLKAGQKIRFGEALGSL
uniprot
proteins
ec_number
4.1.1.65
uniprot
proteins
function
FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). 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}.
uniprot
proteins
mass_dalton
45927
uniprot
proteins
pathway_participation
PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis. {ECO:0000250|UniProtKB:Q9UG56}.
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}.
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
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16192276
uniprot
proteins
pubmed
6862014
uniprot
proteins
sequence_length
406
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase beta chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}; 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:0000269|PubMed:6862014}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Cytoplasm {ECO:0000250|UniProtKB:Q9UG56}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}.; SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UG56}. Lipid droplet {ECO:0000250|UniProtKB:Q9UG56}. Note=Predominantly localizes to lipid droplets in lipid-replete conditions, and to mitochondria in lipid-deplete conditions. {ECO:0000250|UniProtKB:Q9UG56}.
uniprot
proteins
transmembrane_region
TRANSMEM 61..79; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208
uniprot
proteins