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UniProtKB - P04180 (LCAT_HUMAN)

Entry version 211 (07 Apr 2021)
Sequence version 1 (20 Mar 1987)
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Protein

Phosphatidylcholine-sterol acyltransferase

Gene

LCAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).9 Publications

Miscellaneous

Levels of LCAT activity correlates inversely with leptin levels as well as with obesity for a wide range of BMI values.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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:8016111, PubMed:24620755).3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Affinity for LDL is 2.3 to 4-fold lower than for HDL. Relative reactivities are 16% for HDL3, 1.3% for HDL2 and 6.5% for LDL.
  1. KM=0.97 mM for LDL1 Publication
  2. KM=0.4 mM for HDL21 Publication
  3. KM=0.10 mM for HDL31 Publication
  4. KM=12.8 µM for 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine1 Publication
  5. KM=125.5 µM for (24S)-hydroxycholesterol (in the presence of APOA1)1 Publication
  6. KM=417.3 µM for (24S)-hydroxycholesterol (in the presence of APOE)1 Publication
  1. Vmax=8.3 mmol/min/mg enzyme with LDL as substrate1 Publication
  2. Vmax=0.58 mmol/min/mg enzyme with HDL2 as substrate1 Publication
  3. Vmax=2.0 mmol/min/mg enzyme with HDL3 as substrate1 Publication
  4. Vmax=0.2 µmol/h/mg enzyme with 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine as substrate1 Publication
  5. Vmax=12 µmol/h/mg enzyme with cholesterol as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei173Determinant for substrate specificity1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei205Nucleophile1 Publication1
Active sitei369Charge relay system1 Publication1
Active sitei401Charge relay system1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Hydrolase, Transferase
Biological processCholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.1.43, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P04180

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-8964058, HDL remodeling

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P04180

SIGNOR Signaling Network Open Resource

More...SIGNORi		P04180

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...ESTHERi		human-LCAT, PC-sterol_acyltransferase

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000660

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Phosphatidylcholine-sterol acyltransferase (EC:2.3.1.437 Publications)
Alternative name(s):
1-alkyl-2-acetylglycerophosphocholine esterase (EC:3.1.1.471 Publication)
Lecithin-cholesterol acyltransferase
Phospholipid-cholesterol acyltransferase
Platelet-activating factor acetylhydrolase1 Publication
Short name:
PAF acetylhydrolase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LCAT
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 16

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:6522, LCAT

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		606967, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P04180

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000213398.7

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Lecithin-cholesterol acyltransferase deficiency (LCATD)15 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_00425117L → LLLPPAAPFWL in LCATD. 1
Natural variantiVAR_03902029N → I in LCATD. 1 Publication1
Natural variantiVAR_03902237T → M in LCATD. 1 PublicationCorresponds to variant dbSNP:rs971887742Ensembl.1
Natural variantiVAR_00425354G → S in LCATD. 1 PublicationCorresponds to variant dbSNP:rs1461145750Ensembl.1
Natural variantiVAR_00425457G → R in LCATD. 1 Publication1
Natural variantiVAR_004255117A → T in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940886EnsemblClinVar.1
Natural variantiVAR_004257159R → W in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28940887EnsemblClinVar.1
Natural variantiVAR_039028164R → C in LCATD. 1 PublicationCorresponds to variant dbSNP:rs1380009545Ensembl.1
Natural variantiVAR_004258164R → H in LCATD; also found in a patient with intermediate phenotype between LCATD and FED; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs769485083Ensembl.1
Natural variantiVAR_004259171R → W in LCATD. 2 Publications1
Natural variantiVAR_004260180Y → N in LCATD. Corresponds to variant dbSNP:rs749740660Ensembl.1
Natural variantiVAR_039030205S → N in LCATD. 1 Publication1
Natural variantiVAR_004262233L → P in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28942087EnsemblClinVar.1
Natural variantiVAR_039031242K → N in LCATD. 1 Publication1
Natural variantiVAR_004263252N → K in LCATD. 1 PublicationCorresponds to variant dbSNP:rs121908049EnsemblClinVar.1
Natural variantiVAR_039032268R → H in LCATD. 1 PublicationCorresponds to variant dbSNP:rs780824776Ensembl.1
Natural variantiVAR_039033298T → A in FED and LCATD. 2 Publications1
Natural variantiVAR_039034298T → I in LCATD. 1 Publication1
Natural variantiVAR_004265317M → I in LCATD; partially defective enzyme. 2 PublicationsCorresponds to variant dbSNP:rs121908048EnsemblClinVar.1
Natural variantiVAR_039035331P → S in LCATD. 1 Publication1
Natural variantiVAR_039036333V → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs776035233EnsemblClinVar.1
Natural variantiVAR_004266345T → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940888EnsemblClinVar.1
Natural variantiVAR_039038406F → V in LCATD. 1 Publication1
Fish-eye disease (FED)7 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA 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').
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00425234P → L in FED. 1 PublicationCorresponds to variant dbSNP:rs121908051EnsemblClinVar.1
Natural variantiVAR_03902134P → Q in FED. 1 Publication1
Natural variantiVAR_03902370V → E in FED. 1 PublicationCorresponds to variant dbSNP:rs748427834Ensembl.1
Natural variantiVAR_06686299W → S in FED; loss of activity. 1 Publication1
Natural variantiVAR_039026123R → C in FED. 1 PublicationCorresponds to variant dbSNP:rs140068549EnsemblClinVar.1
Natural variantiVAR_004256147T → I in FED. 1 PublicationCorresponds to variant dbSNP:rs121908050EnsemblClinVar.1
Natural variantiVAR_039027159R → Q in FED. 1 PublicationCorresponds to variant dbSNP:rs768017317Ensembl.1
Natural variantiVAR_004264276M → K in FED. 1 PublicationCorresponds to variant dbSNP:rs121908054EnsemblClinVar.1
Natural variantiVAR_039033298T → A in FED and LCATD. 2 Publications1
Natural variantiVAR_066867338L → F in FED; results in reduced protein secretion and activity. 1 PublicationCorresponds to variant dbSNP:rs1330635214Ensembl.1
Natural variantiVAR_066868347R → C in FED; results in reduced activity. 1 PublicationCorresponds to variant dbSNP:rs202017590EnsemblClinVar.1
Natural variantiVAR_004267371T → M in FED. 1 PublicationCorresponds to variant dbSNP:rs121908053EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi173E → A: Increased activity towards PAPC. Increased PAPC/POPC activity ratio. 1 Publication1
Mutagenesisi173E → D: Little change in enzyme specific activity nor in PAPC/POPC activity ratio. 1 Publication1
Mutagenesisi173E → K: Decreased enzyme specific activity. Increased PAPC/POPC activity ratio. 1 Publication1
Mutagenesisi173E → L: Increased activity towards PAPC. Increased PAPC/POPC activity ratio. 1 Publication1
Mutagenesisi173E → Q: Decreased enzyme specific activity. Increased PAPC/POPC activity ratio. 1 Publication1

Keywords - Diseasei

Corneal dystrophy, Disease variant

Organism-specific databases

DisGeNET

More...DisGeNETi		3931

MalaCards human disease database

More...MalaCardsi		LCAT
MIMi136120, phenotype
245900, phenotype

Open Targets

More...OpenTargetsi		ENSG00000213398

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		79293, Familial LCAT deficiency
79292, Fish-eye disease

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA226

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P04180, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5942

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		LCAT

Domain mapping of disease mutations (DMDM)

More...DMDMi		125993

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 241 PublicationAdd BLAST24
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001780225 – 440Phosphatidylcholine-sterol acyltransferaseAdd BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi44N-linked (GlcNAc...) (complex) asparagine2 Publications1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi74 ↔ 98Combined sources2 Publications
Glycosylationi108N-linked (GlcNAc...) (complex) asparagineCombined sources2 Publications1
Glycosylationi296N-linked (GlcNAc...) (complex) asparagineCombined sources3 Publications1
Disulfide bondi337 ↔ 380Combined sources2 Publications
Glycosylationi408N-linked (GlcNAc...) (complex) asparagineCombined sources2 Publications1
Glycosylationi431O-linked (GalNAc...) threonine1 Publication1
Glycosylationi433O-linked (GalNAc...) serine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P04180

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P04180

MaxQB - The MaxQuant DataBase

More...MaxQBi		P04180

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P04180

PeptideAtlas

More...PeptideAtlasi		P04180

PRoteomics IDEntifications database

More...PRIDEi		P04180

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		51671

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		495, 13 N-Linked glycans (2 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P04180, 6 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P04180

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P04180

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in blood plasma (PubMed:3458198, PubMed:8820107, PubMed:10222237). Detected in cerebral spinal fluid (at protein level) (PubMed:10222237). Detected in liver (PubMed:3797244, PubMed:3458198). Expressed mainly in brain, liver and testes.4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000213398, Expressed in right lobe of liver and 159 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P04180, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P04180, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000213398, Group enriched (brain, liver)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		110123, 6 interactors

Database of interacting proteins

More...DIPi		DIP-29620N

Protein interaction database and analysis system

More...IntActi		P04180, 2 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000264005

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P04180

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P04180, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P04180

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi426 – 439Pro-richAdd BLAST14

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2369, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160052

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P04180

Identification of Orthologs from Complete Genome Data

More...OMAi		WEDTKNL

Database of Orthologous Groups

More...OrthoDBi		828056at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P04180

TreeFam database of animal gene trees

More...TreeFami		TF313258

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029058, AB_hydrolase
IPR003386, LACT/PDAT_acylTrfase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02450, LCAT, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53474, SSF53474, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00120, LIPASE_SER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All

P04180-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGPPGSPWQW VTLLLGLLLP PAAPFWLLNV LFPPHTTPKA ELSNHTRPVI 
        60         70         80         90        100
LVPGCLGNQL EAKLDKPDVV NWMCYRKTED FFTIWLDLNM FLPLGVDCWI 
       110        120        130        140        150
DNTRVVYNRS SGLVSNAPGV QIRVPGFGKT YSVEYLDSSK LAGYLHTLVQ 
       160        170        180        190        200
NLVNNGYVRD ETVRAAPYDW RLEPGQQEEY YRKLAGLVEE MHAAYGKPVF 
       210        220        230        240        250
LIGHSLGCLH LLYFLLRQPQ AWKDRFIDGF ISLGAPWGGS IKPMLVLASG 
       260        270        280        290        300
DNQGIPIMSS IKLKEEQRIT TTSPWMFPSR MAWPEDHVFI STPSFNYTGR 
       310        320        330        340        350
DFQRFFADLH FEEGWYMWLQ SRDLLAGLPA PGVEVYCLYG VGLPTPRTYI 
       360        370        380        390        400
YDHGFPYTDP VGVLYEDGDD TVATRSTELC GLWQGRQPQP VHLLPLHGIQ 
       410        420        430        440
HLNMVFSNLT LEHINAILLG AYRQGPPASP TASPEPPPPE
Length:440
Mass (Da):49,578
Last modified:March 20, 1987 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB315EF118AA7A378
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
I3L0J6I3L0J6_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
80Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
I3L1Q6I3L1Q6_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
107Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QSE5J3QSE5_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
255Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QKT0J3QKT0_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
138Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
I3L3R0I3L3R0_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
93Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
I3L215I3L215_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
61Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti257I → H in CAB56610 (PubMed:2823898).Curated1
Sequence conflicti257I → H in AAA59499 (PubMed:2823898).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00425117L → LLLPPAAPFWL in LCATD. 1
Natural variantiVAR_03902029N → I in LCATD. 1 Publication1
Natural variantiVAR_00425234P → L in FED. 1 PublicationCorresponds to variant dbSNP:rs121908051EnsemblClinVar.1
Natural variantiVAR_03902134P → Q in FED. 1 Publication1
Natural variantiVAR_03902237T → M in LCATD. 1 PublicationCorresponds to variant dbSNP:rs971887742Ensembl.1
Natural variantiVAR_00425354G → S in LCATD. 1 PublicationCorresponds to variant dbSNP:rs1461145750Ensembl.1
Natural variantiVAR_00425457G → R in LCATD. 1 Publication1
Natural variantiVAR_03902370V → E in FED. 1 PublicationCorresponds to variant dbSNP:rs748427834Ensembl.1
Natural variantiVAR_03902495G → R Found in a patient with intermediate phenotype between LCATD and FED; reduction of activity. 1 Publication1
Natural variantiVAR_06686299W → S in FED; loss of activity. 1 Publication1
Natural variantiVAR_039025115S → P1 PublicationCorresponds to variant dbSNP:rs1412883954Ensembl.1
Natural variantiVAR_004255117A → T in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940886EnsemblClinVar.1
Natural variantiVAR_039026123R → C in FED. 1 PublicationCorresponds to variant dbSNP:rs140068549EnsemblClinVar.1
Natural variantiVAR_066863134 – 135EY → DN in a patient with low HDL-cholesterol levels; results in reduced activity. 1 Publication2
Natural variantiVAR_004256147T → I in FED. 1 PublicationCorresponds to variant dbSNP:rs121908050EnsemblClinVar.1
Natural variantiVAR_039027159R → Q in FED. 1 PublicationCorresponds to variant dbSNP:rs768017317Ensembl.1
Natural variantiVAR_004257159R → W in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28940887EnsemblClinVar.1
Natural variantiVAR_039028164R → C in LCATD. 1 PublicationCorresponds to variant dbSNP:rs1380009545Ensembl.1
Natural variantiVAR_004258164R → H in LCATD; also found in a patient with intermediate phenotype between LCATD and FED; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs769485083Ensembl.1
Natural variantiVAR_039029165A → T1 PublicationCorresponds to variant dbSNP:rs1369994093Ensembl.1
Natural variantiVAR_004259171R → W in LCATD. 2 Publications1
Natural variantiVAR_004260180Y → N in LCATD. Corresponds to variant dbSNP:rs749740660Ensembl.1
Natural variantiVAR_004261182R → C2 PublicationsCorresponds to variant dbSNP:rs387906300EnsemblClinVar.1
Natural variantiVAR_039030205S → N in LCATD. 1 Publication1
Natural variantiVAR_017030232S → T3 PublicationsCorresponds to variant dbSNP:rs4986970Ensembl.1
Natural variantiVAR_004262233L → P in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28942087EnsemblClinVar.1
Natural variantiVAR_039031242K → N in LCATD. 1 Publication1
Natural variantiVAR_066864246V → F in a patient with low HDL-cholesterol levels; the mutant is hardly secreted and is catalytically inactive. 1 Publication1
Natural variantiVAR_004263252N → K in LCATD. 1 PublicationCorresponds to variant dbSNP:rs121908049EnsemblClinVar.1
Natural variantiVAR_066865268R → C in a patient with low HDL-cholesterol levels; the mutant is hardly secreted and is catalytically inactive. 1 PublicationCorresponds to variant dbSNP:rs745320775Ensembl.1
Natural variantiVAR_039032268R → H in LCATD. 1 PublicationCorresponds to variant dbSNP:rs780824776Ensembl.1
Natural variantiVAR_004264276M → K in FED. 1 PublicationCorresponds to variant dbSNP:rs121908054EnsemblClinVar.1
Natural variantiVAR_039033298T → A in FED and LCATD. 2 Publications1
Natural variantiVAR_039034298T → I in LCATD. 1 Publication1
Natural variantiVAR_004265317M → I in LCATD; partially defective enzyme. 2 PublicationsCorresponds to variant dbSNP:rs121908048EnsemblClinVar.1
Natural variantiVAR_066866322R → C in a patient with low HDL-cholesterol levels; reduced protein secretion. 1 PublicationCorresponds to variant dbSNP:rs1407191796Ensembl.1
Natural variantiVAR_039035331P → S in LCATD. 1 Publication1
Natural variantiVAR_039036333V → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs776035233EnsemblClinVar.1
Natural variantiVAR_066867338L → F in FED; results in reduced protein secretion and activity. 1 PublicationCorresponds to variant dbSNP:rs1330635214Ensembl.1
Natural variantiVAR_004266345T → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940888EnsemblClinVar.1
Natural variantiVAR_066868347R → C in FED; results in reduced activity. 1 PublicationCorresponds to variant dbSNP:rs202017590EnsemblClinVar.1
Natural variantiVAR_004267371T → M in FED. 1 PublicationCorresponds to variant dbSNP:rs121908053EnsemblClinVar.1
Natural variantiVAR_039037396L → R in a patient with LCATD. 2 Publications1
Natural variantiVAR_039038406F → V in LCATD. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X04981 Genomic DNA Translation: CAA28651.1
M12625 mRNA Translation: AAA59498.1
AY422210 Genomic DNA Translation: AAR03499.1
BT009748 mRNA Translation: AAP88750.1
AC040162 Genomic DNA No translation available.
CH471092 Genomic DNA Translation: EAW83190.1
BC014781 mRNA Translation: AAH14781.1
M26268 mRNA Translation: AAA59499.1
X06537 mRNA Translation: CAB56610.1
M17959 Genomic DNA Translation: AAA59500.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS10854.1

Protein sequence database of the Protein Information Resource

More...PIRi		A00571, XXHUN

NCBI Reference Sequences

More...RefSeqi		NP_000220.1, NM_000229.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000264005; ENSP00000264005; ENSG00000213398

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3931

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3931

UCSC genome browser

More...UCSCi		uc002euy.2, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Lecithin-cholesterol acyltransferase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04981 Genomic DNA Translation: CAA28651.1
M12625 mRNA Translation: AAA59498.1
AY422210 Genomic DNA Translation: AAR03499.1
BT009748 mRNA Translation: AAP88750.1
AC040162 Genomic DNA No translation available.
CH471092 Genomic DNA Translation: EAW83190.1
BC014781 mRNA Translation: AAH14781.1
M26268 mRNA Translation: AAA59499.1
X06537 mRNA Translation: CAB56610.1
M17959 Genomic DNA Translation: AAA59500.1
CCDSiCCDS10854.1
PIRiA00571, XXHUN
RefSeqiNP_000220.1, NM_000229.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4X96X-ray8.69A/B/C/D45-421[»]
4XWGX-ray2.65A25-440[»]
4XX1X-ray3.60A/B/J25-440[»]
5BV7X-ray2.45A25-440[»]
5TXFX-ray3.10A/B/C/D25-440[»]
6MVDX-ray3.10A/B45-421[»]
SMRiP04180
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi110123, 6 interactors
DIPiDIP-29620N
IntActiP04180, 2 interactors
STRINGi9606.ENSP00000264005

Chemistry databases

BindingDBiP04180
ChEMBLiCHEMBL5942
SwissLipidsiSLP:000000660

Protein family/group databases

ESTHERihuman-LCAT, PC-sterol_acyltransferase

PTM databases

GlyConnecti495, 13 N-Linked glycans (2 sites)
GlyGeniP04180, 6 sites
iPTMnetiP04180
PhosphoSitePlusiP04180

Genetic variation databases

BioMutaiLCAT
DMDMi125993

Proteomic databases

jPOSTiP04180
MassIVEiP04180
MaxQBiP04180
PaxDbiP04180
PeptideAtlasiP04180
PRIDEiP04180
ProteomicsDBi51671

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P04180, 3 sequenced antibodies

Antibodypedia a portal for validated antibodies

More...Antibodypediai		15960, 401 antibodies

The DNASU plasmid repository

More...DNASUi		3931

Genome annotation databases

EnsembliENST00000264005; ENSP00000264005; ENSG00000213398
GeneIDi3931
KEGGihsa:3931
UCSCiuc002euy.2, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3931
DisGeNETi3931

GeneCards: human genes, protein and diseases

More...GeneCardsi		LCAT
HGNCiHGNC:6522, LCAT
HPAiENSG00000213398, Group enriched (brain, liver)
MalaCardsiLCAT
MIMi136120, phenotype
245900, phenotype
606967, gene
neXtProtiNX_P04180
OpenTargetsiENSG00000213398
Orphaneti79293, Familial LCAT deficiency
79292, Fish-eye disease
PharmGKBiPA226
VEuPathDBiHostDB:ENSG00000213398.7

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2369, Eukaryota
GeneTreeiENSGT00940000160052
InParanoidiP04180
OMAiWEDTKNL
OrthoDBi828056at2759
PhylomeDBiP04180
TreeFamiTF313258

Enzyme and pathway databases

BRENDAi2.3.1.43, 2681
PathwayCommonsiP04180
ReactomeiR-HSA-8964058, HDL remodeling
SABIO-RKiP04180
SIGNORiP04180

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		3931, 7 hits in 996 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		LCAT, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Lecithin%E2%80%94cholesterol_acyltransferase

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		3931
PharosiP04180, Tbio

Protein Ontology

More...PROi		PR:P04180
RNActiP04180, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000213398, Expressed in right lobe of liver and 159 other tissues
ExpressionAtlasiP04180, baseline and differential
GenevisibleiP04180, HS

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR003386, LACT/PDAT_acylTrfase
PfamiView protein in Pfam
PF02450, LCAT, 1 hit
SUPFAMiSSF53474, SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00120, LIPASE_SER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLCAT_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P04180
Secondary accession number(s): Q53XQ3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: April 7, 2021
This is version 211 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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