ANGPTL4
entrez
51129
canonical
uniprot
Q9BY76
canonical
ensembl
ENSG00000167772
resolver
ensp
ENSP00000301455
resolver
ensp
ENSP00000377534
resolver
genesymbol
ANGPTL4
resolver
genesymbol_syn
ARP4
resolver
genesymbol_syn
HFARP
resolver
genesymbol_syn
PGAR
resolver
hgnc
HGNC:16039
resolver
uniprot
A8MY84
resolver
uniprot
B4E089
resolver
uniprot
D6W670
resolver
uniprot
F5H0I2
resolver
uniprot
Q53HQ6
resolver
uniprot
Q53HU1
resolver
uniprot
Q6UXN0
resolver
uniprot
Q9HBV4
resolver
uniprot
Q9NZU4
resolver
uniprot
Q9Y5B3
resolver
uniprot_entry
ANGL4_HUMAN
resolver
uniprot_sec
A8MY84
resolver
uniprot_sec
B4E089
resolver
uniprot_sec
D6W670
resolver
uniprot_sec
F5H0I2
resolver
uniprot_sec
Q53HQ6
resolver
uniprot_sec
Q53HU1
resolver
uniprot_sec
Q6UXN0
resolver
uniprot_sec
Q9HBV4
resolver
uniprot_sec
Q9NZU4
resolver
uniprot_sec
Q9Y5B3
resolver
amino_acid_sequence
MSGAPTAGAALMLCAATAVLLSAQGGPVQSKSPRFASWDEMNVLAHGLLQLGQGLREHAERTRSQLSALERRLSACGSACQGTEGSTDLPLAPESRVDPEVLHSLQTQLKAQNSRIQQLFHKVAQQQRHLEKQHLRIQHLQSQFGLLDHKHLDHEVAKPARRKRLPEMAQPVDPAHNVSRLHRLPRDCQELFQVGERQSGLFEIQPQGSPPFLVNCKMTSDGGWTVIQRRHDGSVDFNRPWEAYKAGFGDPHGEFWLGLEKVHSITGDRNSRLAVQLRDWDGNAELLQFSVHLGGEDTAYSLQLTAPVAGQLGATTVPPSGLSVPFSTWDQDHDLRRDKNCAKSLSGGWWFGTCSHSNLNGQYFRSIPQQRQKLKKGIFWKTWRGRYYPLQATTMLIQPMAAEAAS
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:19270337, PubMed:21398697, PubMed:27929370, PubMed:29899144). May also play a role in regulating glucose homeostasis and insulin sensitivity (Probable). Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage (PubMed:14583458, PubMed:17068295). 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) (PubMed:17068295). Depending on context, may modulate tumor-related angiogenesis (By similarity). {ECO:0000250|UniProtKB:Q9Z1P8, ECO:0000269|PubMed:14583458, ECO:0000269|PubMed:17068295, ECO:0000269|PubMed:19270337, ECO:0000269|PubMed:21398697, ECO:0000269|PubMed:27929370, ECO:0000269|PubMed:29899144, ECO:0000305|PubMed:29899519}.; 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 (PubMed:19270337, PubMed:21398697, PubMed:27929370, PubMed:29899144). Has higher activity in LPL inactivation than the uncleaved protein (PubMed:19270337, PubMed:21398697). {ECO:0000269|PubMed:19270337, ECO:0000269|PubMed:21398697, ECO:0000269|PubMed:27929370, ECO:0000269|PubMed:29899144}.
uniprot
proteins
mass_dalton
45214
uniprot
proteins
mutagenesis
MUTAGEN 40; /note="E->A: Loss of inactivation of lipoprotein lipase LPL."; /evidence="ECO:0000269|PubMed:19270337"; MUTAGEN 40; /note="E->D: Decreased inactivation of lipoprotein lipase LPL."; /evidence="ECO:0000269|PubMed:19270337"; MUTAGEN 76; /note="C->A: No effect on secretion and proteolytic cleavage. Loss of oligomerization; when associated with A-80."; /evidence="ECO:0000269|PubMed:19270337"; MUTAGEN 80; /note="C->A: No effect on secretion and proteolytic cleavage. Loss of oligomerization; when associated with A-76."; /evidence="ECO:0000269|PubMed:19270337"; MUTAGEN 161..164; /note="RRKR->GSGS: Loss of proteolytic cleavage. No effect on the ability to inactivate lipoprotein lipase LPL."; /evidence="ECO:0000269|PubMed:19270337"; MUTAGEN 161; /note="R->A: Loss of proteolytic cleavage. Decreased ability to inactivate lipoprotein lipase LPL."; /evidence="ECO:0000269|PubMed:21398697"; MUTAGEN 164; /note="R->A: Loss of proteolytic cleavage."; /evidence="ECO:0000269|PubMed:21398697"; MUTAGEN 223; /note="G->R: Impaired protein folding."; /evidence="ECO:0000269|PubMed:29713054
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:10698685}.; PTM: [ANGPTL4 N-terminal chain]: Forms disulfide-linked dimers and tetramers. {ECO:0000269|PubMed:19270337}.; 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:0000269|PubMed:17068295, ECO:0000269|PubMed:19270337, ECO:0000269|PubMed:21398697}.
uniprot
proteins
pubmed
10698685
uniprot
proteins
pubmed
10866690
uniprot
proteins
pubmed
11953136
uniprot
proteins
pubmed
12015030
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14583458
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17068295
uniprot
proteins
pubmed
17322881
uniprot
proteins
pubmed
19270337
uniprot
proteins
pubmed
21398697
uniprot
proteins
pubmed
27929370
uniprot
proteins
pubmed
29713054
uniprot
proteins
pubmed
29899144
uniprot
proteins
pubmed
29899519
uniprot
proteins
sequence_length
406
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10698685, ECO:0000269|PubMed:14583458, ECO:0000269|PubMed:17068295, ECO:0000269|PubMed:19270337, ECO:0000269|PubMed:21398697, ECO:0000269|PubMed:29899519}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17068295, ECO:0000269|PubMed:21398697}. Note=The unprocessed form interacts with the extracellular matrix (PubMed:17068295, PubMed:21398697). This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4 (Probable). {ECO:0000269|PubMed:17068295, ECO:0000269|PubMed:21398697, ECO:0000305|PubMed:17068295}.
uniprot
proteins