Angptl4
entrez
362850
canonical
uniprot
Q6TMA8
canonical
ensembl
ENSRNOG00000007545
resolver
ensembl
ENSRNOG00055031838
resolver
ensembl
ENSRNOG00060024266
resolver
ensembl
ENSRNOG00065021047
resolver
ensp
ENSRNOP00000010031
resolver
ensp
ENSRNOP00055045545
resolver
ensp
ENSRNOP00060034814
resolver
ensp
ENSRNOP00065028827
resolver
enst
ENSRNOT00000010031
resolver
enst
ENSRNOT00055055101
resolver
enst
ENSRNOT00060041979
resolver
enst
ENSRNOT00065035766
resolver
genesymbol
Angptl4
resolver
uniprot_entry
ANGL4_RAT
resolver
amino_acid_sequence
MRCAPTAGAALVLCAATAGLLSAQGRPAQPEPPRFASWDEMNLLAHGLLQLGHGLREHVERTRGQLGALERRMAACGNACQGPKGTDPKDRVPEGQAPETLQSLQTQLKAQNSKIQQLFQKVAQQQRYLSKQNLRIQNLQSQIDLLTPTHLDNGVDKTSRGKRLPKMAQLIGLTPNATRLHRPPRDCQELFQEGERHSGLFQIQPLGSPPFLVNCEMTSDGGWTVIQRRLNGSVDFNQSWEAYKDGFGDPQGEFWLGLEKMHSITGDRGSQLAVQLQDWDGNAKLLQFPIHLGGEDTAYSLQLTEPTANELGATNVSPNGLSLPFSTWDQDHDLRGDLNCAKSLSGGWWFGTCSHSNLNGQYFHSIPRQRQQRKKGIFWKTWKGRYYPLQATTLLIQPMEATAAS
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. May also play a role in regulating glucose homeostasis and insulin sensitivity. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q9BY76, ECO:0000250|UniProtKB:Q9Z1P8}.; 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
44951
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:14570927}.; PTM: [ANGPTL4 N-terminal chain]: Forms disulfide-linked dimers and tetramers. {ECO:0000269|PubMed:14570927}.; 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:0000305|PubMed:14570927}.
uniprot
proteins
pubmed
14570927
uniprot
proteins
pubmed
15489334
uniprot
proteins
sequence_length
405
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14570927}. 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