Q8WUD6 · CHPT1_HUMAN
- ProteinCholinephosphotransferase 1
- GeneCHPT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids406 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the final step of de novo phosphatidylcholine (PC) synthesis, i.e. the transfer of choline phosphate from CDP-choline to the free hydroxyl of a diacylglycerol (DAG), producing a PC. It thereby plays a central role in the formation and maintenance of vesicular membranes.
Catalytic activity
- a 1,2-diacyl-sn-glycerol + CDP-choline = a 1,2-diacyl-sn-glycero-3-phosphocholine + CMP + H+This reaction proceeds in the forward direction.
- 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + CDP-choline = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + CMP + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + CDP-choline = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + CMP + H+This reaction proceeds in the forward direction.
- 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycerol + CDP-choline = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + CMP + H+This reaction proceeds in the forward direction.
- 1,2-dioctanoyl-sn-glycerol + CDP-choline = 1,2-dioctanoyl-sn-glycero-3-phosphocholine + CMP + H+This reaction proceeds in the forward direction.
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Pathway
Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 2/2.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 64 | CDP-choline (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 111 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 111 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 114 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 119 | CDP-choline (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 129 | Increases basicity of active site His | ||||
Sequence: E | ||||||
Binding site | 132 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 132 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 133 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 136 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | membrane | |
Molecular Function | diacylglycerol binding | |
Molecular Function | diacylglycerol cholinephosphotransferase activity | |
Molecular Function | metal ion binding | |
Biological Process | CDP-choline pathway | |
Biological Process | lipid metabolic process | |
Biological Process | phosphatidylcholine biosynthetic process | |
Biological Process | platelet activating factor biosynthetic process | |
Biological Process | regulation of cell growth |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameCholinephosphotransferase 1
- EC number
- Short nameshCPT1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8WUD6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 2-62 | Cytoplasmic | ||||
Sequence: AAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLWMA | ||||||
Transmembrane | 63-83 | Helical; Name=1 | ||||
Sequence: PNSITLLGLAVNVVTTLVLIS | ||||||
Topological domain | 84-93 | Lumenal | ||||
Sequence: YCPTATEEAP | ||||||
Transmembrane | 94-118 | Helical; Name=2 | ||||
Sequence: YWTYLLCALGLFIYQSLDAIDGKQA | ||||||
Topological domain | 119-125 | Cytoplasmic | ||||
Sequence: RRTNSCS | ||||||
Transmembrane | 126-150 | Helical; Name=3 | ||||
Sequence: PLGELFDHGCDSLSTVFMAVGASIA | ||||||
Topological domain | 151-160 | Lumenal | ||||
Sequence: ARLGTYPDWF | ||||||
Transmembrane | 161-179 | Helical; Name=4 | ||||
Sequence: FFCSFIGMFVFYCAHWQTY | ||||||
Topological domain | 180-190 | Cytoplasmic | ||||
Sequence: VSGMLRFGKVD | ||||||
Transmembrane | 191-207 | Helical; Name=5 | ||||
Sequence: VTEIQIALVIVFVLSAF | ||||||
Topological domain | 208-222 | Lumenal | ||||
Sequence: GGATMWDYTIPILEI | ||||||
Transmembrane | 223-248 | Helical; Name=6 | ||||
Sequence: KLKILPVLGFLGGVIFSCSNYFHVIL | ||||||
Topological domain | 249-265 | Cytoplasmic | ||||
Sequence: HGGVGKNGSTIAGTSVL | ||||||
Transmembrane | 266-281 | Helical; Name=7 | ||||
Sequence: SPGLHIGLIIILAIMI | ||||||
Topological domain | 282-293 | Lumenal | ||||
Sequence: YKKSATDVFEKH | ||||||
Transmembrane | 294-316 | Helical; Name=8 | ||||
Sequence: PCLYILMFGCVFAKVSQKLVVAH | ||||||
Topological domain | 317-329 | Cytoplasmic | ||||
Sequence: MTKSELYLQDTVF | ||||||
Transmembrane | 330-339 | Helical; Name=9 | ||||
Sequence: LGPGLLFLDQ | ||||||
Topological domain | 340-346 | Lumenal | ||||
Sequence: YFNNFID | ||||||
Transmembrane | 347-376 | Helical; Name=10 | ||||
Sequence: EYVVLWMAMVISSFDMVIYFSALCLQISRH | ||||||
Topological domain | 377-406 | Cytoplasmic | ||||
Sequence: LHLNIFKTACHQAPEQVQVLSSKSHQNNMD |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_032612 | 162 | in dbSNP:rs3205421 | |||
Sequence: F → S | ||||||
Natural variant | VAR_032613 | 323 | in MCF-12A cell line | |||
Sequence: Y → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 433 variants from UniProt as well as other sources including ClinVar and dbSNP.
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_0000289252 | 2-406 | Cholinephosphotransferase 1 | |||
Sequence: AAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLWMAPNSITLLGLAVNVVTTLVLISYCPTATEEAPYWTYLLCALGLFIYQSLDAIDGKQARRTNSCSPLGELFDHGCDSLSTVFMAVGASIAARLGTYPDWFFFCSFIGMFVFYCAHWQTYVSGMLRFGKVDVTEIQIALVIVFVLSAFGGATMWDYTIPILEIKLKILPVLGFLGGVIFSCSNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATDVFEKHPCLYILMFGCVFAKVSQKLVVAHMTKSELYLQDTVFLGPGLLFLDQYFNNFIDEYVVLWMAMVISSFDMVIYFSALCLQISRHLHLNIFKTACHQAPEQVQVLSSKSHQNNMD |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in testis, colon, small intestine, heart, prostate and spleen. Also detected in kidney, skeletal muscle, pancreas, leukocytes, ovary and thymus. Weakly expressed in the brain, placenta and lung. Overexpressed in cancerous breast epithelial cell lines.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8WUD6 | TLCD4 Q96MV1 | 3 | EBI-11337856, EBI-12947623 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8WUD6-1
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
- SynonymsAlpha
- Length406
- Mass (Da)45,097
- Last updated2002-03-01 v1
- ChecksumAE5357C02ED40E4C
Q8WUD6-2
- Name2
- SynonymsBeta
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 86 | in Ref. 5; AAD44019 | ||||
Sequence: P → L | ||||||
Sequence conflict | 109 | in Ref. 5; AAD44019 | ||||
Sequence: S → P | ||||||
Alternative sequence | VSP_025989 | 217-218 | in isoform 2 | |||
Sequence: IP → FS | ||||||
Alternative sequence | VSP_025990 | 219-406 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 269 | in Ref. 5; AAD44019 | ||||
Sequence: L → P | ||||||
Sequence conflict | 346 | in Ref. 5; AAD44019 | ||||
Sequence: D → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF195623 EMBL· GenBank· DDBJ | AAF87947.1 EMBL· GenBank· DDBJ | mRNA | ||
AF195624 EMBL· GenBank· DDBJ | AAF87948.1 EMBL· GenBank· DDBJ | mRNA | ||
AK075211 EMBL· GenBank· DDBJ | BAG52084.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471054 EMBL· GenBank· DDBJ | EAW97675.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC020819 EMBL· GenBank· DDBJ | AAH20819.1 EMBL· GenBank· DDBJ | mRNA | ||
BC050429 EMBL· GenBank· DDBJ | AAH50429.1 EMBL· GenBank· DDBJ | mRNA | ||
AF047431 EMBL· GenBank· DDBJ | AAD44019.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AF111803 EMBL· GenBank· DDBJ | AAL39005.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY280609 EMBL· GenBank· DDBJ | AAP34412.1 EMBL· GenBank· DDBJ | mRNA | ||
AY280610 EMBL· GenBank· DDBJ | AAP34413.1 EMBL· GenBank· DDBJ | mRNA | ||
AY294627 EMBL· GenBank· DDBJ | AAP37157.1 EMBL· GenBank· DDBJ | mRNA | ||
AY166717 EMBL· GenBank· DDBJ | AAN86122.1 EMBL· GenBank· DDBJ | mRNA | ||
AY166718 EMBL· GenBank· DDBJ | AAN86123.1 EMBL· GenBank· DDBJ | mRNA |