Angptl4
entrez
57875
canonical
uniprot
Q9Z1P8
canonical
ensembl
ENSMUSG00000002289
resolver
ensp
ENSMUSP00000002360
resolver
enst
ENSMUST00000002360
resolver
genesymbol
Angptl4
resolver
genesymbol_syn
Farp
resolver
genesymbol_syn
Fiaf
resolver
genesymbol_syn
Ng27
resolver
uniprot
Q78ZJ9
resolver
uniprot
Q9JHX7
resolver
uniprot
Q9JLX7
resolver
uniprot_entry
ANGL4_MOUSE
resolver
uniprot_sec
Q78ZJ9
resolver
uniprot_sec
Q9JHX7
resolver
uniprot_sec
Q9JLX7
resolver
amino_acid_sequence
MRCAPTAGAALVLCAATAGLLSAQGRPAQPEPPRFASWDEMNLLAHGLLQLGHGLREHVERTRGQLGALERRMAACGNACQGPKGKDAPFKDSEDRVPEGQTPETLQSLQTQLKAQNSKIQQLFQKVAQQQRYLSKQNLRIQNLQSQIDLLAPTHLDNGVDKTSRGKRLPKMTQLIGLTPNATHLHRPPRDCQELFQEGERHSGLFQIQPLGSPPFLVNCEMTSDGGWTVIQRRLNGSVDFNQSWEAYKDGFGDPQGEFWLGLEKMHSITGNRGSQLAVQLQDWDGNAKLLQFPIHLGGEDTAYSLQLTEPTANELGATNVSPNGLSLPFSTWDQDHDLRGDLNCAKSLSGGWWFGTCSHSNLNGQYFHSIPRQRQERKKGIFWKTWKGRYYPLQATTLLIQPMEATAAS
uniprot
proteins
function
FUNCTION: 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). {ECO:0000250|UniProtKB:Q9BY76, ECO:0000269|PubMed:14583458, ECO:0000269|PubMed:15837923, ECO:0000269|PubMed:17130448, ECO:0000269|PubMed:17609370, ECO:0000269|PubMed:21832056, ECO:0000269|PubMed:29899519, ECO:0000305|PubMed:14583458, ECO:0000305|PubMed:17130448}.; FUNCTION: [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. {ECO:0000250|UniProtKB:Q9BY76}.
uniprot
proteins
mass_dalton
45538
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9BY76}.; PTM: [ANGPTL4 N-terminal chain]: Forms disulfide-linked dimers and tetramers. {ECO:0000250|UniProtKB:Q9BY76}.; PTM: 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. {ECO:0000250|UniProtKB:Q9BY76}.
uniprot
proteins
pubmed
10698685
uniprot
proteins
pubmed
10862772
uniprot
proteins
pubmed
10866690
uniprot
proteins
pubmed
14583458
uniprot
proteins
pubmed
14656967
uniprot
proteins
pubmed
15112104
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15837923
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17068295
uniprot
proteins
pubmed
17130448
uniprot
proteins
pubmed
17609370
uniprot
proteins
pubmed
21832056
uniprot
proteins
pubmed
27834691
uniprot
proteins
pubmed
29899519
uniprot
proteins
sequence_length
410
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14583458, ECO:0000269|PubMed:15837923}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9BY76}. Note=The unprocessed form interacts with the extracellular matrix. This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4. {ECO:0000250|UniProtKB:Q9BY76}.
uniprot
proteins