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Entry version 175 (13 Nov 2019)
Sequence version 1 (01 Nov 1999)
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Protein

Angiopoietin-related protein 3

Gene

ANGPTL3

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

Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism (PubMed:11788823, PubMed:12909640, PubMed:23661675, PubMed:25495645). Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake (By similarity). Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity. The inhibition of LPL activity appears to be an indirect mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1 (PubMed:12097324, PubMed:19318355, PubMed:20581395). Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids (PubMed:17110602, PubMed:19028676). Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol (PubMed:12565906). Suppresses LPL specifically in oxidative tissues which is required to route very low density lipoprotein (VLDL)-TG to white adipose tissue (WAT) for storage in response to food; the function may involve cooperation with circulating, liver-derived ANGPTL8 and ANGPTL4 expression in WAT (By similarity). Contributes to lower plasma levels of low density lipoprotein (LDL)-cholesterol by a mechanism that is independent of the canonical pathway implicating APOE and LDLR. May stimulate hypothalamic LPL activity (By similarity).By similarity1 Publication10 Publications
ANGPTL3(17-221): In vitro inhibits LPL activity; not effective on GPIHBP1-stabilized LPL.1 Publication
Involved in angiogenesis. Binds to endothelial cells via integrin alpha-V/beta-3 (ITGAV:ITGB3), activates FAK, MAPK and Akt signaling pathways and induces cell adhesion and cell migration (PubMed:11877390). Secreted from podocytes, may modulate properties of glomerular endothelial cells involving integrin alpha-V/beta-3 and Akt signaling (PubMed:18535744). May increase the motility of podocytes. May induce actin filament rearrangements in podocytes implicating integrin alpha-V/beta-3 and Rac1 activation. Binds to hematopoietic stem cells (HSC) and is involved in the regulation of HSC activity probably implicating down-regulation of IKZF1/IKAROS (By similarity).By similarity2 Publications

Miscellaneous

Was suggested to inhibit LPL through a direct mechanism; however, the necessary concentration to achieve in vitro inhibition is at least 30-fold higher than ANGPTL3 plasma concentration.2 Publications

<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

GO - Biological processi

<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 functionHeparin-binding
Biological processAngiogenesis, Cell adhesion, Lipid metabolism

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-8963889 Assembly of active LPL and LIPC lipase complexes
R-HSA-9029558 NR1H2 & NR1H3 regulate gene expression linked to lipogenesis

<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_and_taxonomy_section">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:
Angiopoietin-related protein 3
Alternative name(s):
Angiopoietin-5
Short name:
ANG-5
Angiopoietin-like protein 3
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:ANGPTL3
Synonyms:ANGPT5
ORF Names:UNQ153/PRO179
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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 1

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:491 ANGPTL3

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
604774 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9Y5C1

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, 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

Hypobetalipoproteinemia, familial, 2 (FHBL2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of lipid metabolism characterized by less than 5th percentile age- and sex-specific levels of low density lipoproteins, and dietary fat malabsorption. Affected individuals present with combined hypolipidemia, consisting of extremely low plasma levels of LDL cholesterol, HDL cholesterol, and triglycerides.
Related information in OMIM
May be involved in atherosclerosis. Plasma levels are closely associated with arterial wall thickness.1 Publication
May be involved in nephrotic syndrome.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi62 – 63HK → IN: Abolishes effect on plasma triglyceride level; when associated with N-65. 1 Publication2
Mutagenesisi63K → N: Abolishes inhibitory effect on LIPG/EL phospholipase activity; when associated with N-65. 1 Publication1
Mutagenesisi65K → N: Abolishes effect on plasma triglyceride level; when associated with 62-I-N-63. 1 Publication1
Mutagenesisi65K → N: Abolishes inhibitory effect on LIPG/EL phospholipase activity; when associated with N-63. 1 Publication1
Mutagenesisi204 – 205RR → TT: Abolishes proteolytical cleavage and effect on plasma triglyceride levels, keeps in vitro inactivation of LPL activity; when associated with S-221; S-224 and S-235. 1 Publication2
Mutagenesisi221R → ST: Abolishes proteolytical cleavage and effect on plasma triglyceride levels, keeps in vitro inactivation of LPL activity; when associated with 204-T-T-205; S-224 and S-235. 1 Publication1
Mutagenesisi224R → S: Abolishes proteolytical cleavage and effect on plasma triglyceride levels, keeps in vitro inactivation of LPL activity; when associated with 204-T-T-205; S-221 and S-235. 1 Publication1
Mutagenesisi235R → T: Abolishes proteolytical cleavage and effect on plasma triglyceride levels, keeps in vitro inactivation of LPL activity; when associated with 204-T-T-205; S-221 and S-224. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
27329

MalaCards human disease database

More...
MalaCardsi
ANGPTL3
MIMi605019 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000132855

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

More...
Orphaneti
426 NON RARE IN EUROPE: Familial hypobetalipoproteinemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24796

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q9Y5C1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3710485

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ANGPTL3

Domain mapping of disease mutations (DMDM)

More...
DMDMi
25008126

<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 – 161 PublicationAdd BLAST16
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000912217 – 460Angiopoietin-related protein 3Add BLAST444
ChainiPRO_000043590317 – 224ANGPTL3(17-224)1 PublicationAdd BLAST208
ChainiPRO_000043590417 – 221ANGPTL3(17-221)1 PublicationAdd BLAST205

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi115N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi226O-linked (GalNAc) threonine1 Publication1
<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 bondi246 ↔ 274PROSITE-ProRule annotation
Glycosylationi296N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi357N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi394 ↔ 408PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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-glycosylated at Thr-226 by GALNT2; blocks processing and activation by proprotein convertases.2 Publications
In part proteolytically cleaved by proprotein convertases; proposed to be involved in activation.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q9Y5C1

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

More...
PaxDbi
Q9Y5C1

PeptideAtlas

More...
PeptideAtlasi
Q9Y5C1

PRoteomics IDEntifications database

More...
PRIDEi
Q9Y5C1

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
86339

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
1010

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9Y5C1

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

More...
PhosphoSitePlusi
Q9Y5C1

<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

Expressed principally in liver. Weakly expressed in kidney. Binds to adipocytes. Increased expression and colocalization with activated ITGB3 in glomeruli of patients with nephrotic syndrome showing effaced podocyte foot processes (at protein level).3 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated by insulin.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000132855 Expressed in 87 organ(s), highest expression level in liver

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9Y5C1 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA038097

<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_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with ANGPTL8.

Interacts with ITGB3 (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
118143, 5 interactors

Protein interaction database and analysis system

More...
IntActi
Q9Y5C1, 7 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000360170

<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

1460
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
Q9Y5C1

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini237 – 455Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST219

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni17 – 207Sufficient to inhibit LIPG/EL phospholipase activity1 PublicationAdd BLAST191
Regioni17 – 165Sufficient to inhibit LPL lipase activity1 PublicationAdd BLAST149
Regioni32 – 56Required for inhibition of LPL lipase activity1 PublicationAdd BLAST25

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili85 – 210Sequence analysisAdd BLAST126

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The fibrinogen C-terminal domain is sufficient to mediate endothelial cell adhesion.1 Publication

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2579 Eukaryota
ENOG410ZYS4 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156746

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000015386

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9Y5C1

KEGG Orthology (KO)

More...
KOi
K22288

Identification of Orthologs from Complete Genome Data

More...
OMAi
NRGEHTS

Database of Orthologous Groups

More...
OrthoDBi
357340at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9Y5C1

TreeFam database of animal gene trees

More...
TreeFami
TF336658

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00087 FReD, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036056 Fibrinogen-like_C
IPR002181 Fibrinogen_a/b/g_C_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00147 Fibrinogen_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00186 FBG, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56496 SSF56496, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51406 FIBRINOGEN_C_2, 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_length">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q9Y5C1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFTIKLLLFI VPLVISSRID QDNSSFDSLS PEPKSRFAML DDVKILANGL
60 70 80 90 100
LQLGHGLKDF VHKTKGQIND IFQKLNIFDQ SFYDLSLQTS EIKEEEKELR
110 120 130 140 150
RTTYKLQVKN EEVKNMSLEL NSKLESLLEE KILLQQKVKY LEEQLTNLIQ
160 170 180 190 200
NQPETPEHPE VTSLKTFVEK QDNSIKDLLQ TVEDQYKQLN QQHSQIKEIE
210 220 230 240 250
NQLRRTSIQE PTEISLSSKP RAPRTTPFLQ LNEIRNVKHD GIPAECTTIY
260 270 280 290 300
NRGEHTSGMY AIRPSNSQVF HVYCDVISGS PWTLIQHRID GSQNFNETWE
310 320 330 340 350
NYKYGFGRLD GEFWLGLEKI YSIVKQSNYV LRIELEDWKD NKHYIEYSFY
360 370 380 390 400
LGNHETNYTL HLVAITGNVP NAIPENKDLV FSTWDHKAKG HFNCPEGYSG
410 420 430 440 450
GWWWHDECGE NNLNGKYNKP RAKSKPERRR GLSWKSQNGR LYSIKSTKML
460
IHPTDSESFE
Length:460
Mass (Da):53,637
Last modified:November 1, 1999 - 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:i6279465FEEB91F56
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH07059 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

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 conflicti134L → P in BAG37708 (PubMed:14702039).Curated1

Natural variant

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_07567063K → T Associated with low plasma triglyceride level; fails to suppress LPL activity in vitro. 1 PublicationCorresponds to variant dbSNP:rs146749211Ensembl.1
Natural variantiVAR_07567191E → G Associated with low plasma triglyceride level; fails to suppress LPL activity in vitro. 1 PublicationCorresponds to variant dbSNP:rs139334976Ensembl.1
Natural variantiVAR_067283127L → F1 PublicationCorresponds to variant dbSNP:rs72649573EnsemblClinVar.1
Natural variantiVAR_075672164L → F Associated with low plasma triglyceride level; fails to suppress LPL activity in vitro. 1 PublicationCorresponds to variant dbSNP:rs775976787Ensembl.1
Natural variantiVAR_075673173N → S Associated with low plasma triglyceride level; fails to suppress LPL activity in vitro; no effect on protein secretion. 2 PublicationsCorresponds to variant dbSNP:rs149624466Ensembl.1
Natural variantiVAR_075674259M → T Common allele in African americans; associated with low plasma triglyceride level; fails to suppress LPL activity in vitro; no effect on protein folding. 2 PublicationsCorresponds to variant dbSNP:rs77871363Ensembl.1
Natural variantiVAR_075675288R → Q Abolishes protein secretion; associated with low plasma triglyceride level. 2 PublicationsCorresponds to variant dbSNP:rs763904695Ensembl.1
Natural variantiVAR_075676288Missing Abolishes protein secretion; associated with low plasma triglyceride level. 1 Publication1
Natural variantiVAR_075677292S → P Abolishes protein secretion; associated with low plasma triglyceride level. 2 PublicationsCorresponds to variant dbSNP:rs138899888Ensembl.1
Natural variantiVAR_075678344Y → S Abolishes protein secretion; associated with low plasma triglyceride level. 2 PublicationsCorresponds to variant dbSNP:rs1334979946Ensembl.1
Natural variantiVAR_075679375E → K Abolishes protein secretion; associated with low plasma triglyceride level. 3 PublicationsCorresponds to variant dbSNP:rs768802285Ensembl.1
Natural variantiVAR_075680417Y → C Abolishes protein secretion; associated with low plasma triglyceride level. 1 PublicationCorresponds to variant dbSNP:rs376210525Ensembl.1
Natural variantiVAR_049071418N → Y. Corresponds to variant dbSNP:rs4145257Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF152562 mRNA Translation: AAD34156.1
AY358273 mRNA Translation: AAQ88640.1
AK315304 mRNA Translation: BAG37708.1
AY569015 Genomic DNA Translation: AAS66984.1
FJ515851 Genomic DNA Translation: ACS13743.1
CH471059 Genomic DNA Translation: EAX06583.1
BC007059 mRNA Translation: AAH07059.1 Sequence problems.
BC058287 mRNA Translation: AAH58287.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS622.1

NCBI Reference Sequences

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RefSeqi
NP_055310.1, NM_014495.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000371129; ENSP00000360170; ENSG00000132855

Database of genes from NCBI RefSeq genomes

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GeneIDi
27329

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:27329

UCSC genome browser

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UCSCi
uc001das.3 human

Keywords - Coding sequence diversityi

Polymorphism

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF152562 mRNA Translation: AAD34156.1
AY358273 mRNA Translation: AAQ88640.1
AK315304 mRNA Translation: BAG37708.1
AY569015 Genomic DNA Translation: AAS66984.1
FJ515851 Genomic DNA Translation: ACS13743.1
CH471059 Genomic DNA Translation: EAX06583.1
BC007059 mRNA Translation: AAH07059.1 Sequence problems.
BC058287 mRNA Translation: AAH58287.1
CCDSiCCDS622.1
RefSeqiNP_055310.1, NM_014495.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6EUAX-ray2.10A/B/C242-460[»]
SMRiQ9Y5C1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi118143, 5 interactors
IntActiQ9Y5C1, 7 interactors
STRINGi9606.ENSP00000360170

Chemistry databases

ChEMBLiCHEMBL3710485

PTM databases

GlyConnecti1010
iPTMnetiQ9Y5C1
PhosphoSitePlusiQ9Y5C1

Polymorphism and mutation databases

BioMutaiANGPTL3
DMDMi25008126

Proteomic databases

MassIVEiQ9Y5C1
PaxDbiQ9Y5C1
PeptideAtlasiQ9Y5C1
PRIDEiQ9Y5C1
ProteomicsDBi86339

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
Q9Y5C1

The DNASU plasmid repository

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DNASUi
27329

Genome annotation databases

EnsembliENST00000371129; ENSP00000360170; ENSG00000132855
GeneIDi27329
KEGGihsa:27329
UCSCiuc001das.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
27329
DisGeNETi27329

GeneCards: human genes, protein and diseases

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GeneCardsi
ANGPTL3
HGNCiHGNC:491 ANGPTL3
HPAiHPA038097
MalaCardsiANGPTL3
MIMi604774 gene
605019 phenotype
neXtProtiNX_Q9Y5C1
OpenTargetsiENSG00000132855
Orphaneti426 NON RARE IN EUROPE: Familial hypobetalipoproteinemia
PharmGKBiPA24796

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2579 Eukaryota
ENOG410ZYS4 LUCA
GeneTreeiENSGT00940000156746
HOGENOMiHOG000015386
InParanoidiQ9Y5C1
KOiK22288
OMAiNRGEHTS
OrthoDBi357340at2759
PhylomeDBiQ9Y5C1
TreeFamiTF336658

Enzyme and pathway databases

ReactomeiR-HSA-8963889 Assembly of active LPL and LIPC lipase complexes
R-HSA-9029558 NR1H2 & NR1H3 regulate gene expression linked to lipogenesis

Miscellaneous databases

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

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ChiTaRSi
ANGPTL3 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
ANGPTL3

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

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GenomeRNAii
27329
PharosiQ9Y5C1

Protein Ontology

More...
PROi
PR:Q9Y5C1

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000132855 Expressed in 87 organ(s), highest expression level in liver
GenevisibleiQ9Y5C1 HS

Family and domain databases

CDDicd00087 FReD, 1 hit
InterProiView protein in InterPro
IPR036056 Fibrinogen-like_C
IPR002181 Fibrinogen_a/b/g_C_dom
PfamiView protein in Pfam
PF00147 Fibrinogen_C, 1 hit
SMARTiView protein in SMART
SM00186 FBG, 1 hit
SUPFAMiSSF56496 SSF56496, 1 hit
PROSITEiView protein in PROSITE
PS51406 FIBRINOGEN_C_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiANGL3_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: Q9Y5C1
Secondary accession number(s): A0JLS0, B1ALJ0, B2RCW1
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 1, 1999
Last modified: November 13, 2019
This is version 175 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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