LCAT
entrez
3931
canonical
uniprot
P04180
canonical
ensembl
ENSG00000213398
resolver
ensp
ENSP00000264005
resolver
enst
ENST00000264005
resolver
genesymbol
LCAT
resolver
hgnc
HGNC:6522
resolver
uniprot
A0A140VK24
resolver
uniprot
Q53XQ3
resolver
uniprot_entry
A0A140VK24_HUMAN
resolver
uniprot_entry
LCAT_HUMAN
resolver
uniprot_sec
Q53XQ3
resolver
activity_regulation
ACTIVITY REGULATION: APOA1 is the most potent activator in plasma (PubMed:19065001, PubMed:8016111). Also activated by APOE, APOC1 and APOA4 (PubMed:19065001, PubMed:8016111). Inhibited by haptoglobin and 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) (PubMed:24620755, PubMed:8016111). {ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:24620755, ECO:0000269|PubMed:8016111}.
uniprot
proteins
amino_acid_sequence
MGPPGSPWQWVTLLLGLLLPPAAPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQLEAKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEYYRKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGSIKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGRDFQRFFADLHFEEGWYMWLQSRDLLAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYTDPVGVLYEDGDDTVATRSTELCGLWQGRQPQPVHLLPLHGIQHLNMVFSNLTLEHINAILLGAYRQGPPASPTASPEPPPPE
uniprot
proteins
disease_involvement
DISEASE: Lecithin-cholesterol acyltransferase deficiency (LCATD) [MIM:245900]: A disorder of lipoprotein metabolism characterized by inadequate esterification of plasmatic cholesterol. Two clinical forms are recognized: complete LCAT deficiency and fish-eye disease. LCATD is generally referred to the complete form which is associated with absence of both alpha and beta LCAT activities resulting in esterification anomalies involving both HDL (alpha-LCAT activity) and LDL (beta-LCAT activity). It causes a typical triad of diffuse corneal opacities, target cell hemolytic anemia, and proteinuria with renal failure. {ECO:0000269|PubMed:11423760, ECO:0000269|PubMed:12957688, ECO:0000269|PubMed:15994445, ECO:0000269|PubMed:16051254, ECO:0000269|PubMed:16216249, ECO:0000269|PubMed:1681161, ECO:0000269|PubMed:1859405, ECO:0000269|PubMed:2370048, ECO:0000269|PubMed:7607641, ECO:0000269|PubMed:7711728, ECO:0000269|PubMed:8318557, ECO:0000269|PubMed:8432868, ECO:0000269|PubMed:8445342, ECO:0000269|PubMed:8807342, ECO:0000269|PubMed:9007616, ECO:0000269|PubMed:9741700}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Fish-eye disease (FED) [MIM:136120]: A disorder of lipoprotein metabolism due to partial lecithin-cholesterol acyltransferase deficiency that affects only alpha-LCAT activity. FED is characterized by low plasma HDL and corneal opacities due to accumulation of cholesterol deposits in the cornea ('fish-eye'). {ECO:0000269|PubMed:1516702, ECO:0000269|PubMed:1571050, ECO:0000269|PubMed:15994445, ECO:0000269|PubMed:1737840, ECO:0000269|PubMed:21901787, ECO:0000269|PubMed:8620346, ECO:0000269|PubMed:9261271}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.1.43
uniprot
proteins
ec_number
3.1.1.47
uniprot
proteins
function
FUNCTION: Central enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs) (PubMed:10329423, PubMed:19065001, PubMed:26195816). The cholesterol ester is then transported back to the liver. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines (PubMed:8820107). Also produced in the brain by primary astrocytes, and esterifies free cholesterol on nascent APOE-containing lipoproteins secreted from glia and influences cerebral spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins. Required for remodeling high-density lipoprotein particles into their spherical forms (PubMed:10722751). Catalyzes the hydrolysis of 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-activating factor or PAF) to 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (PubMed:8016111). Also catalyzes the transfer of the acetate group from PAF to 1-hexadecanoyl-sn-glycero-3-phosphocholine forming lyso-PAF (PubMed:8016111). Catalyzes the esterification of (24S)-hydroxycholesterol (24(S)OH-C), also known as cerebrosterol to produce 24(S)OH-C monoesters (PubMed:24620755). {ECO:0000269|PubMed:10329423, ECO:0000269|PubMed:10722751, ECO:0000269|PubMed:12354767, ECO:0000269|PubMed:14636062, ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:24620755, ECO:0000269|PubMed:26195816, ECO:0000269|PubMed:8016111, ECO:0000269|PubMed:8820107}.
uniprot
proteins
mass_dalton
49578
uniprot
proteins
mutagenesis
MUTAGEN 173; /note="E->A: Increased activity towards PAPC. Increased PAPC/POPC activity ratio."; /evidence="ECO:0000269|PubMed:14636062"; MUTAGEN 173; /note="E->D: Little change in enzyme specific activity nor in PAPC/POPC activity ratio."; /evidence="ECO:0000269|PubMed:14636062"; MUTAGEN 173; /note="E->K: Decreased enzyme specific activity. Increased PAPC/POPC activity ratio."; /evidence="ECO:0000269|PubMed:14636062"; MUTAGEN 173; /note="E->L: Increased activity towards PAPC. Increased PAPC/POPC activity ratio."; /evidence="ECO:0000269|PubMed:14636062"; MUTAGEN 173; /note="E->Q: Decreased enzyme specific activity. Increased PAPC/POPC activity ratio."; /evidence="ECO:0000269|PubMed:14636062
uniprot
proteins
post_translational_modification
PTM: O- and N-glycosylated. O-glycosylation on Thr-431 and Ser-433 consists of sialylated galactose beta 1-->3N-acetylgalactosamine structures. N-glycosylated sites contain sialylated triantennary and/or biantennary complex structures. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:7613477}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Lipase family
uniprot
proteins
pubmed
10222237
uniprot
proteins
pubmed
10329423
uniprot
proteins
pubmed
10722751
uniprot
proteins
pubmed
11423760
uniprot
proteins
pubmed
12354767
uniprot
proteins
pubmed
12957688
uniprot
proteins
pubmed
12966036
uniprot
proteins
pubmed
14636062
uniprot
proteins
pubmed
1516702
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
1571050
uniprot
proteins
pubmed
15994445
uniprot
proteins
pubmed
16051254
uniprot
proteins
pubmed
16216249
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
1681161
uniprot
proteins
pubmed
16874701
uniprot
proteins
pubmed
1737840
uniprot
proteins
pubmed
17950106
uniprot
proteins
pubmed
1859405
uniprot
proteins
pubmed
19065001
uniprot
proteins
pubmed
21901787
uniprot
proteins
pubmed
2370048
uniprot
proteins
pubmed
24620755
uniprot
proteins
pubmed
25727495
uniprot
proteins
pubmed
26195816
uniprot
proteins
pubmed
2823801
uniprot
proteins
pubmed
2823898
uniprot
proteins
pubmed
2880847
uniprot
proteins
pubmed
3458198
uniprot
proteins
pubmed
3797244
uniprot
proteins
pubmed
7607641
uniprot
proteins
pubmed
7613477
uniprot
proteins
pubmed
7711728
uniprot
proteins
pubmed
8016111
uniprot
proteins
pubmed
8318557
uniprot
proteins
pubmed
8432868
uniprot
proteins
pubmed
8445342
uniprot
proteins
pubmed
8620346
uniprot
proteins
pubmed
8807342
uniprot
proteins
pubmed
8820107
uniprot
proteins
pubmed
9007616
uniprot
proteins
pubmed
9261271
uniprot
proteins
pubmed
9741700
uniprot
proteins
sequence_length
440
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10222237, ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:3458198, ECO:0000269|PubMed:8016111, ECO:0000269|PubMed:8820107}. Note=Secreted into blood plasma (PubMed:10222237, PubMed:3458198, PubMed:8820107). Produced in astrocytes and secreted into cerebral spinal fluid (CSF) (PubMed:10222237). {ECO:0000269|PubMed:10222237, ECO:0000269|PubMed:3458198, ECO:0000269|PubMed:8820107}.
uniprot
proteins