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MGP004284

UniProt Annotations

Entry Information
Gene Nameserine palmitoyltransferase, long chain base subunit 1
Protein EntrySPTC1_HUMAN
UniProt IDO15269
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=O15269-1; Sequence=Displayed; Name=2; IsoId=O15269-2; Sequence=VSP_043127, VSP_043128; Note=No experimental confirmation available.;
Biophysicochemical PropertiesKinetic parameters: KM=0.75 mM for serine {ECO:0000269|PubMed:20504773}; Vmax=1350 pmol/min/mg enzyme {ECO:0000269|PubMed:20504773};
Catalytic ActivityPalmitoyl-CoA + L-serine = CoA + 3-dehydro-D- sphinganine + CO(2). {ECO:0000269|PubMed:19416851}.
CautionVariant Ala-387 has been originally thought to cause HSAN1A (PubMed:15037712). Subsequently, it has been shown to be a rare, benign polymorphism found in homozygous state in a healthy individual (PubMed:19132419). {ECO:0000305|PubMed:15037712, ECO:0000305|PubMed:19132419}.
CofactorName=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250};
DiseaseNeuropathy, hereditary sensory and autonomic, 1A (HSAN1A) [MIM:162400]: A form of hereditary sensory and autonomic neuropathy, a genetically and clinically heterogeneous group of disorders characterized by degeneration of dorsal root and autonomic ganglion cells, and by prominent sensory abnormalities with a variable degree of motor and autonomic dysfunction. The neurological phenotype is often complicated by severe infections, osteomyelitis, and amputations. HSAN1A is an autosomal dominant axonal form with onset in the second or third decades. Initial symptoms are loss of pain, touch, heat, and cold sensation over the feet, followed by distal muscle wasting and weakness. Loss of pain sensation leads to chronic skin ulcers and distal amputations. {ECO:0000269|PubMed:11242114, ECO:0000269|PubMed:19651702, ECO:0000269|PubMed:21618344, ECO:0000269|PubMed:22302274}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionSerine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1- SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference. {ECO:0000269|PubMed:19416851}.
PathwayLipid metabolism; sphingolipid metabolism.
PtmPhosphorylation at Tyr-164 inhibits activity and promotes cell survival. {ECO:0000269|PubMed:23629659}.
SimilarityBelongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.
Subcellular LocationEndoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
SubunitHeterodimer with SPTLC2 or SPTLC3. Component of the serine palmitoyltransferase (SPT) complex, composed of SPTLC1, either SPTLC2 or SPTLC3, and either SPTSSA or SPTSSB. Interacts with SPTSSA and SPTSSB; the interaction is direct. Interacts with ORMDL3. {ECO:0000269|PubMed:19416851, ECO:0000269|PubMed:20182505}.
Tissue SpecificityWidely expressed. Not detected in small intestine. {ECO:0000269|PubMed:17023427}.
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