PCYT1A
entrez
5130
canonical
uniprot
P49585
canonical
ensembl
ENSG00000161217
resolver
ensp
ENSP00000292823
resolver
ensp
ENSP00000394617
resolver
ensp
ENSP00000545645
resolver
enst
ENST00000292823
resolver
enst
ENST00000431016
resolver
enst
ENST00000875586
resolver
genesymbol
PCYT1A
resolver
genesymbol_syn
CTPCT
resolver
genesymbol_syn
PCYT1
resolver
hgnc
HGNC:8754
resolver
uniprot
A9LYK9
resolver
uniprot
B4E322
resolver
uniprot
C9JNT9
resolver
uniprot
D3DXB1
resolver
uniprot
Q86Y88
resolver
uniprot_entry
B4E322_HUMAN
resolver
uniprot_entry
PCY1A_HUMAN
resolver
uniprot_sec
A9LYK9
resolver
uniprot_sec
C9JNT9
resolver
uniprot_sec
D3DXB1
resolver
uniprot_sec
Q86Y88
resolver
activity_regulation
ACTIVITY REGULATION: Interconverts between an inactive cytosolic form and an active membrane-bound form (By similarity). Activation involves disruption of an inhibitory interaction between helices at the base of the active site and the autoinhibitory (AI) region (By similarity). Activated by anionic lipid vesicles and by oleic acid or diacylglycerol-containing phosphatidylcholine vesicles (PubMed:7918629, PubMed:8155650). {ECO:0000250|UniProtKB:P19836, ECO:0000269|PubMed:7918629, ECO:0000269|PubMed:8155650}.
uniprot
proteins
amino_acid_sequence
MDAQCSAKVNARKRRKEAPGPNGATEEDGVPSKVQRCAVGLRQPAPFSDEIEVDFSKPYVRVTMEEASRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQAISPKQSPSSSPTRERSPSPSFRWPFSGKTSPPCSPANLSRHKAAAYDISEDEED
uniprot
proteins
disease_involvement
DISEASE: Spondylometaphyseal dysplasia with cone-rod dystrophy (SMDCRD) [MIM:608940]: An autosomal recessive disorder characterized by postnatal growth deficiency resulting in profound short stature, rhizomelia with bowing of the lower extremities, platyspondyly with anterior vertebral protrusions, progressive metaphyseal irregularity and cupping with shortened tubular bones, and early-onset progressive visual impairment associated with a pigmentary maculopathy and electroretinographic evidence of cone-rod dysfunction. {ECO:0000269|PubMed:24387990, ECO:0000269|PubMed:24387991}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Lipodystrophy, congenital generalized, 5 (CGL5) [MIM:620680]: A form of congenital generalized lipodystrophy, a metabolic disorder characterized by a near complete absence of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and diabetes mellitus. CGL5 is an autosomal recessive form with onset in early childhood. Affected individuals also have short stature. {ECO:0000269|PubMed:24889630}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.7.15
uniprot
proteins
function
FUNCTION: Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis. {ECO:0000269|PubMed:10480912, ECO:0000269|PubMed:30559292, ECO:0000269|PubMed:7918629}.
uniprot
proteins
mass_dalton
41731
uniprot
proteins
mutagenesis
MUTAGEN 37; /note="C->S: Abolishes formation of the interchain disulfide that can be observed when the enzyme is treated with copper phenanthrolene (in vitro)."; /evidence="ECO:0000269|PubMed:15069071"; MUTAGEN 93; /note="A->T: Decreased solubility. Decreased lipid vesicle-dependent choline-phosphate cytidylyltransferase activity. 4-fold decreased Vmax. No effect on affinity for phosphocholine and CTP."; /evidence="ECO:0000269|PubMed:30559292"; MUTAGEN 240; /note="Y->H: Decreased solubility."; /evidence="ECO:0000269|PubMed:30559292
uniprot
proteins
pathway_participation
PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2. {ECO:0000269|PubMed:10480912, ECO:0000269|PubMed:7918629}.
uniprot
proteins
post_translational_modification
PTM: The serine residues of the C-terminus are phosphorylated. The inactive soluble form is stabilized by phosphorylation, the active membrane bound form is promoted by anionic lipids or diacylglycerol, and is stabilized by dephosphorylation (By similarity). {ECO:0000250|UniProtKB:P19836}.; PTM: Monoubiquitinated by the SCF(FBXL2) complex, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P49586}.
uniprot
proteins
protein_family
Cytidylyltransferase family
uniprot
proteins
pubmed
10480912
uniprot
proteins
pubmed
15069071
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24387990
uniprot
proteins
pubmed
24387991
uniprot
proteins
pubmed
24889630
uniprot
proteins
pubmed
30559292
uniprot
proteins
pubmed
7918629
uniprot
proteins
pubmed
8155650
uniprot
proteins
pubmed
8810902
uniprot
proteins
sequence_length
367
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P19836}. Membrane {ECO:0000250|UniProtKB:P19836}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19836}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10480912}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19836}. Nucleus {ECO:0000269|PubMed:10480912}. Note=It can interconvert between an inactive cytosolic form and an active membrane-bound form. {ECO:0000250|UniProtKB:P19836}.
uniprot
proteins