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Entry version 152 (08 May 2019)
Sequence version 1 (01 May 1999)
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Protein

Angiopoietin-related protein 4

Gene

Angptl4

Organism
Mus musculus (Mouse)
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

Mediates inactivation of the lipoprotein lipase LPL, and thereby plays a role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism (PubMed:15837923, PubMed:17609370, PubMed:29899519). May also play a role in regulating glucose homeostasis and insulin sensitivity (PubMed:15837923, PubMed:29899519). Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage (PubMed:14583458, PubMed:17130448, PubMed:21832056). Upon heterologous expression, inhibits the adhesion of endothelial cell to the extracellular matrix (ECM), and inhibits the reorganization of the actin cytoskeleton, formation of actin stress fibers and focal adhesions in endothelial cells that have adhered to ANGPTL4-containing ECM (in vitro) (By similarity). Depending on context, may modulate tumor-related angiogenesis (Probable).By similarity2 Publications6 Publications
ANGPTL4 N-terminal chain: Mediates inactivation of the lipoprotein lipase LPL, and thereby plays an important role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. Has higher activity in LPL inactivation than the uncleaved protein.By similarity

Miscellaneous

Upon heterologous expression under the control of the keratinocyte promoter in the skin, inhibits tumor-associated angiogenesis and tumor growth (PubMed:14583458). In xenograft models, it inhibits both intra- and extravasation of tumor cells as well as vascular permeability leading to inhibition of metastases. Expression by tumor cells induces reorganization of the actin cytoskeleton through inhibition of actin stress fiber formation and vinculin localization at focal contacts. It might prevent the metastatic process by inhibiting vascular activity as well as tumor cell motility and invasiveness (PubMed:17130448).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

Biological processAngiogenesis, Lipid metabolism

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-8963889 Assembly of active LPL and LIPC lipase complexes

<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 4
Alternative name(s):
425O18-1
Angiopoietin-like protein 4
Fasting-induced adipose factor1 Publication
Hepatic fibrinogen/angiopoietin-related protein1 Publication
Short name:
HFARP1 Publication
Secreted protein Bk89
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:Angptl4
Synonyms:Farp, Fiaf1 Publication, Ng27
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 17

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1888999 Angptl4

<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

Extracellular matrix, 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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Pups are born at less than the expected Mendelian rate, indicative of significant embryonic lethality. No obvious phenotype after birth; mice are viable and fertile (PubMed:21832056). Mutant mice have reduced circulating triglyceride and cholesterol levels when fed a high-fat diet (PubMed:17609370, PubMed:29899519). Besides, they display 30% lower non-fasted blood glucose levels and improved glucose tolerance when fed a high-fat diet. In contrast, glucose levels and glucose tolerance are not different from wild-type when mice are kept on a normal diet (PubMed:29899519). The retinal vascular network displays subtle alterations, including a somewhat larger diameter of veins and capillaries. Pups display a delay in pericyte spreading on newly formed capillaries in the retina, and defects in the organization of endothelial cell tight junctions. In retinas from 17 day old animals, hypoxia-induced pathological neovascularization is strongly reduced (PubMed:21832056). Some studies observed decreased survival of suckling pups and of adults kept on a high-fat diet due to intestinal pathologies, with lipogranulomatous lesions of the intestines and their draining lymphatics and mesenteric lymph nodes (PubMed:17609370). Other studies observed no such effects (PubMed:29899519).3 Publications

<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 – 23Sequence analysisAdd BLAST23
<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_000000912524 – 410Angiopoietin-related protein 4Add BLAST387
ChainiPRO_000044686124 – 167ANGPTL4 N-terminal chainAdd BLAST144
ChainiPRO_0000446862168 – 410ANGPTL4 C-terminal chainAdd BLAST243

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>Glycosylationi181N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi192 ↔ 220PROSITE-ProRule annotation
Glycosylationi236N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi242N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi345 ↔ 358PROSITE-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

N-glycosylated.By similarity
ANGPTL4 N-terminal chain: Forms disulfide-linked dimers and tetramers.By similarity
Cleaved into a smaller N-terminal chain and a larger chain that contains the fibrinogen C-terminal domain; both cleaved and uncleaved forms are detected in the extracellular space. The cleaved form is not present within the cell.By similarity

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>Sitei168 – 169CleavageBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9Z1P8

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

More...
PaxDbi
Q9Z1P8

PRoteomics IDEntifications database

More...
PRIDEi
Q9Z1P8

PTM databases

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

More...
PhosphoSitePlusi
Q9Z1P8

<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 liver and kidney (PubMed:10698685, PubMed:17609370). Predominantly expressed in adipose tissue and is strongly up-regulated by fasting in white adipose tissue and liver.3 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Detected in endothelial cells in the capillary plexus, veins and arteries in the retina at 2, 12 and 17 days after birth (PubMed:21832056). Expressed at low levels in most organs and connective tissue at 13.5 dpc. Between 15.5 dpc and 18.5 dpc, strongest expression in brown fat.2 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

Induced in interstitial capillaries in response to hind leg ischemia (PubMed:17068295). Alterations in nutrition and leptin administration are found to modulate the expression in vivo.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000002289 Expressed in 223 organ(s), highest expression level in white adipose tissue

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9Z1P8 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9Z1P8 MM

<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

Homooligomer; disulfide-linked via Cys residues in the N-terminal part of the protein (PubMed:14583458). The homooligomer undergoes proteolytic processing to release the ANGPTL4 C-terminal chain, which circulates as a monomer. The homooligomer unprocessed form is able to interact with the extracellular matrix (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-61311N

Protein interaction database and analysis system

More...
IntActi
Q9Z1P8, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000002360

<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

3D structure databases

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

More...
SMRi
Q9Z1P8

Database of comparative protein structure models

More...
ModBasei
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>Domaini183 – 405Fibrinogen C-terminalPROSITE-ProRule annotationAdd BLAST223

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 coili104 – 152Sequence analysisAdd BLAST49

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2579 Eukaryota
ENOG410ZYS4 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159478

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000015386

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9Z1P8

KEGG Orthology (KO)

More...
KOi
K08767

Identification of Orthologs from Complete Genome Data

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OMAi
PKQRHQR

Database of Orthologous Groups

More...
OrthoDBi
357340at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9Z1P8

TreeFam database of animal gene trees

More...
TreeFami
TF329953

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
IPR028793 ANGPTL4
IPR036056 Fibrinogen-like_C
IPR002181 Fibrinogen_a/b/g_C_dom
IPR020837 Fibrinogen_CS

The PANTHER Classification System

More...
PANTHERi
PTHR19143:SF256 PTHR19143:SF256, 2 hits

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
PS00514 FIBRINOGEN_C_1, 1 hit
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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q9Z1P8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRCAPTAGAA LVLCAATAGL LSAQGRPAQP EPPRFASWDE MNLLAHGLLQ
60 70 80 90 100
LGHGLREHVE RTRGQLGALE RRMAACGNAC QGPKGKDAPF KDSEDRVPEG
110 120 130 140 150
QTPETLQSLQ TQLKAQNSKI QQLFQKVAQQ QRYLSKQNLR IQNLQSQIDL
160 170 180 190 200
LAPTHLDNGV DKTSRGKRLP KMTQLIGLTP NATHLHRPPR DCQELFQEGE
210 220 230 240 250
RHSGLFQIQP LGSPPFLVNC EMTSDGGWTV IQRRLNGSVD FNQSWEAYKD
260 270 280 290 300
GFGDPQGEFW LGLEKMHSIT GNRGSQLAVQ LQDWDGNAKL LQFPIHLGGE
310 320 330 340 350
DTAYSLQLTE PTANELGATN VSPNGLSLPF STWDQDHDLR GDLNCAKSLS
360 370 380 390 400
GGWWFGTCSH SNLNGQYFHS IPRQRQERKK GIFWKTWKGR YYPLQATTLL
410
IQPMEATAAS
Length:410
Mass (Da):45,538
Last modified:May 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:iBCEE2259921D6D81
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3UWT7G3UWT7_MOUSE
Angiopoietin-related protein 4
Angptl4
154Annotation 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 conflicti168 – 170RLP → KLS in AAF42969 (PubMed:10866690).Curated3
Sequence conflicti180P → S in AAF42969 (PubMed:10866690).Curated1
Sequence conflicti189P → A in AAF42969 (PubMed:10866690).Curated1
Sequence conflicti272N → D in AAF86342 (PubMed:10862772).Curated1
Sequence conflicti272N → D in AAF42969 (PubMed:10866690).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF169313 mRNA Translation: AAF62869.1
AF278699 mRNA Translation: AAF86342.1
AB054540 mRNA Translation: BAB83079.1
AF123261 mRNA Translation: AAF42969.1
AK014564 mRNA Translation: BAB29431.1
AK132761 mRNA Translation: BAE21342.1
AF528162 Genomic DNA Translation: AAO17378.1
AF110520 Genomic DNA Translation: AAC97965.1
BC006611 mRNA Translation: AAH06611.1
BC021343 mRNA Translation: AAH21343.1
BC025797 mRNA Translation: AAH25797.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS28629.1

NCBI Reference Sequences

More...
RefSeqi
NP_065606.2, NM_020581.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000002360; ENSMUSP00000002360; ENSMUSG00000002289

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
57875

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:57875

UCSC genome browser

More...
UCSCi
uc008bzp.2 mouse

<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
AF169313 mRNA Translation: AAF62869.1
AF278699 mRNA Translation: AAF86342.1
AB054540 mRNA Translation: BAB83079.1
AF123261 mRNA Translation: AAF42969.1
AK014564 mRNA Translation: BAB29431.1
AK132761 mRNA Translation: BAE21342.1
AF528162 Genomic DNA Translation: AAO17378.1
AF110520 Genomic DNA Translation: AAC97965.1
BC006611 mRNA Translation: AAH06611.1
BC021343 mRNA Translation: AAH21343.1
BC025797 mRNA Translation: AAH25797.1
CCDSiCCDS28629.1
RefSeqiNP_065606.2, NM_020581.2

3D structure databases

SMRiQ9Z1P8
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-61311N
IntActiQ9Z1P8, 1 interactor
STRINGi10090.ENSMUSP00000002360

PTM databases

PhosphoSitePlusiQ9Z1P8

Proteomic databases

MaxQBiQ9Z1P8
PaxDbiQ9Z1P8
PRIDEiQ9Z1P8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002360; ENSMUSP00000002360; ENSMUSG00000002289
GeneIDi57875
KEGGimmu:57875
UCSCiuc008bzp.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
51129
MGIiMGI:1888999 Angptl4

Phylogenomic databases

eggNOGiKOG2579 Eukaryota
ENOG410ZYS4 LUCA
GeneTreeiENSGT00940000159478
HOGENOMiHOG000015386
InParanoidiQ9Z1P8
KOiK08767
OMAiPKQRHQR
OrthoDBi357340at2759
PhylomeDBiQ9Z1P8
TreeFamiTF329953

Enzyme and pathway databases

ReactomeiR-MMU-8963889 Assembly of active LPL and LIPC lipase complexes

Miscellaneous databases

Protein Ontology

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PROi
PR:Q9Z1P8

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000002289 Expressed in 223 organ(s), highest expression level in white adipose tissue
ExpressionAtlasiQ9Z1P8 baseline and differential
GenevisibleiQ9Z1P8 MM

Family and domain databases

CDDicd00087 FReD, 1 hit
InterProiView protein in InterPro
IPR028793 ANGPTL4
IPR036056 Fibrinogen-like_C
IPR002181 Fibrinogen_a/b/g_C_dom
IPR020837 Fibrinogen_CS
PANTHERiPTHR19143:SF256 PTHR19143:SF256, 2 hits
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
PS00514 FIBRINOGEN_C_1, 1 hit
PS51406 FIBRINOGEN_C_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiANGL4_MOUSE
<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: Q9Z1P8
Secondary accession number(s): Q78ZJ9, Q9JHX7, Q9JLX7
<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: May 1, 1999
Last modified: May 8, 2019
This is version 152 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

<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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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