Q9C0D9 · EPT1_HUMAN
- ProteinEthanolaminephosphotransferase 1
- GeneSELENOI
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids397 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ethanolaminephosphotransferase that catalyzes the transfer of phosphoethanolamine (PE) from CDP-ethanolamine to lipid acceptors, the final step in the synthesis of PE via the 'Kennedy' pathway (PubMed:17132865, PubMed:28052917, PubMed:29500230).
PE is the second most abundant phospholipid of membranes in mammals and is involved in various membrane-related cellular processes (PubMed:17132865).
The enzyme is critical for the synthesis of several PE species and also catalyzes the synthesis of plasmanyl-PE, a lipid required for proper myelination and neurodevelopment, from 1-alkyl-2-acylglycerol (PubMed:29500230).
PE is the second most abundant phospholipid of membranes in mammals and is involved in various membrane-related cellular processes (PubMed:17132865).
The enzyme is critical for the synthesis of several PE species and also catalyzes the synthesis of plasmanyl-PE, a lipid required for proper myelination and neurodevelopment, from 1-alkyl-2-acylglycerol (PubMed:29500230).
Catalytic activity
- a 1,2-diacyl-sn-glycerol + CDP-ethanolamine = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CMP + H+This reaction proceeds in the forward direction.
- 1-O-alkyl-2-acyl-sn-glycerol + CDP-ethanolamine = 1-O-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine + CMP + H+This reaction proceeds in the forward direction.
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.8 μM | CDP-ethanolamine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
76.3 pmol/min/mg | with CDP-ethanolamine as substrate |
Pathway
Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | Golgi apparatus | |
Molecular Function | ethanolaminephosphotransferase activity | |
Molecular Function | metal ion binding | |
Biological Process | ether lipid biosynthetic process | |
Biological Process | myelination | |
Biological Process | phosphatidylethanolamine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEthanolaminephosphotransferase 1
- EC number
- Short nameshEPT1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9C0D9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 47-69 | Helical | ||||
Sequence: WLAPNLITFSGFLLVVFNFLLMA | ||||||
Transmembrane | 84-103 | Helical | ||||
Sequence: HVPDWVWIVVGILNFVAYTL | ||||||
Transmembrane | 123-145 | Helical | ||||
Sequence: LFDHGLDSWSCVYFVVTVYSIFG | ||||||
Transmembrane | 150-172 | Helical | ||||
Sequence: GVSVFVLYLLLWVVLFSFILSHW | ||||||
Transmembrane | 179-201 | Helical | ||||
Sequence: ILFLPWGYDISQVTISFVYIVTA | ||||||
Transmembrane | 221-243 | Helical | ||||
Sequence: LFTAMIIGCALCVTLPMSLLNFF | ||||||
Transmembrane | 256-278 | Helical | ||||
Sequence: VYEAMVPLFSPCLLFILSTAWIL | ||||||
Transmembrane | 291-310 | Helical | ||||
Sequence: VFYFMVGTAFANSTCQLIVC | ||||||
Transmembrane | 317-339 | Helical | ||||
Sequence: CPTLNWLLVPLFLVVLVVNLGVA | ||||||
Transmembrane | 344-366 | Helical | ||||
Sequence: SILLYTLTTAFTLAHIHYGVRVV |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Spastic paraplegia 81, autosomal recessive (SPG81)
- Note
- DescriptionA form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG81 is a complicated form characterized by white matter abnormalities, hypomyelination with progressive white matter loss, delayed motor development, progressive spasticity, and impaired intellectual development and speech delay. Additional features may include bifid uvula, microcephaly, seizures, and variable ocular anomalies.
- See alsoMIM:618768
Natural variants in SPG81
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_083878 | 112 | R>P | in SPG81; loss of ethanolaminephosphotransferase activity; dbSNP:rs933233143 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_083878 | 112 | in SPG81; loss of ethanolaminephosphotransferase activity; dbSNP:rs933233143 | |||
Sequence: R → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 346 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000056813 | 2-397 | Ethanolaminephosphotransferase 1 | |||
Sequence: AGYEYVSPEQLAGFDKYKYSAVDTNPLSLYVMHPFWNTIVKVFPTWLAPNLITFSGFLLVVFNFLLMAYFDPDFYASAPGHKHVPDWVWIVVGILNFVAYTLDGVDGKQARRTNSSTPLGELFDHGLDSWSCVYFVVTVYSIFGRGSTGVSVFVLYLLLWVVLFSFILSHWEKYNTGILFLPWGYDISQVTISFVYIVTAVVGVEAWYEPFLFNFLYRDLFTAMIIGCALCVTLPMSLLNFFRSYKNNTLKLNSVYEAMVPLFSPCLLFILSTAWILWSPSDILELHPRVFYFMVGTAFANSTCQLIVCQMSSTRCPTLNWLLVPLFLVVLVVNLGVASYVESILLYTLTTAFTLAHIHYGVRVVKQLSSHFQIYPFSLRKPNSDULGMEEKNIGL |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Abundant in brain, placenta, liver and pancreas, followed by heart, skeletal muscle, lung and kidney. In brain it is strongly expressed in cerebellum, followed by the occipital pole and the frontal lobe.
Gene expression databases
Organism-specific databases
Structure
Sequence
- Sequence statusComplete
- Length397
- Mass (Da)45,229
- Last updated2008-02-26 v3
- Checksum24CDB1F19EFE4202
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for non-standard residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-standard residue | 387 | Selenocysteine | ||||
Sequence: U |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BK001426 EMBL· GenBank· DDBJ | DAA01514.1 EMBL· GenBank· DDBJ | mRNA | ||
AB051511 EMBL· GenBank· DDBJ | BAB21815.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |