Primary Information |
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BoMiProt ID | Bomi3885 |
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Protein Name | Angiopoietin-related protein 4/Angiopoietin-like protein 4 |
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Organism | Bos taurus |
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Uniprot ID | Q2KJ51 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001039508.1 |
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Aminoacid Length | 410 |
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Molecular Weight | 45553 |
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FASTA Sequence |
Download |
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Gene Name | ANGPTL4 |
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Gene ID | 509963 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | inhibitor of LPL that regulates circulating TG levels and lipid distributions across different tissues.induction of hyperpermeability.Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage.important role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. |
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Biochemical Properties | Homooligomer; disulfide-linked via Cys residues in the N-terminal part of the protein.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.Forms disulfide-linked dimers and tetramers. |
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Significance in milk | regulate the glucose and fatty acid metabolisms during the periparturient period. |
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PTMs | N-glycosylated.Proteolysis |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q2KJ51|ANGL4_BOVIN Angiopoietin-related protein 4 OS=Bos taurus OX=9913 GN=ANGPTL4 PE=2 SV=1
MRCAPTAGAALMLCAATAGLLSAQGRPEPPETPRFASWDEVNVLAHGLLQLGHGLREHVE
RTRGQLGELERRLGACGAACKDPEGSAAPPRAQANLVNPGGGDASPETLRSLKTQLEAQN
SRIQQLFQKVAQQQRHLEKQQLRIQNLQSQMDHLAPRHLGHEMAKPARRKRLPKMAQLAG
PAHN*184ISRLHRLPRDCQELFEEGERESGLFQIQPQGSPPFLVNCKMTSDGGWTVIQRRQDG
SVDFNQPWEAYKDGFGDPQGEFWLGLEKVHHILGDRGSRLAVQLQDWEGNAESLQFPIHL
GGEDTAYSLQLTPPVASKLGATTFSPSGLSLPFSTWDQDHDLRGDKNCARSLSGGWWFGT
CSHSNLNGQYFHSIPRQRQQRKKGIFWKTWRGRYYPLQATTILVQPTAAS
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Predicted Disorder Regions | 4 predicted disordered segments; (22-36), (82-91), (119-134), (160-180) |
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DisProt Annotation | |
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TM Helix Prediction | 1TMH; (7-25) |
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Significance of PTMs | Forms disulfide-linked dimers and tetramers.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. |
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Bibliography | Aryal B, Price NL, Suarez Y, Fernández-Hernando C. ANGPTL4 in Metabolic and Cardiovascular Disease. Trends Mol Med. 2019 Aug;25(8):723-734. doi: 10.1016/j.molmed.2019.05.010. Epub 2019 Jun 21. PMID: 31235370; PMCID: PMC6779329. |