UniProt functional annotation for P08519



	UniProt functional annotation for P08519

UniProt code: P08519.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330. {ECO:0000269|PubMed:2531657}.

Subunit: Disulfide-linked to apo-B100. Binds to fibronectin and decorin.

Ptm: N- and O-glycosylated. The N-glycans are complex biantennary structures present in either a mono- or disialylated state. The O- glycans are mostly (80%) represented by the monosialylated core type I structure, NeuNAcalpha2-3Galbeta1-3GalNAc, with smaller amounts of disialylated and non-sialylated O-glycans also detected. {ECO:0000269|PubMed:11294842}.

Polymorphism: LPA genetic variants, including variations in the number of Kringle domains, define the lipoprotein(a) quantitative trait locus (LPAQTL) and influence lipoprotein(a) levels in plasma [MIM:618807]. The reference genome sequence encodes a variant that contains 16 Kringle domains and that lack residues 533 to 3040. Depending on the individual, the encoded protein contains 2-43 copies of kringle-type domains. The allele represented here contains 38 copies of the kringle- type repeats. {ECO:0000269|PubMed:3670400}.

Miscellaneous: Apo(a) is known to be proteolytically cleaved, leading to the formation of the so-called mini-Lp(a). Apo(a) fragments accumulate in atherosclerotic lesions, where they may promote thrombogenesis. O-glycosylation may limit the extent of proteolytic fragmentation. Homology with plasminogen kringles IV and V is thought to underlie the atherogenicity of the protein, because the fragments are competing with plasminogen for fibrin(ogen) binding.

Similarity: Belongs to the peptidase S1 family. Plasminogen subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330. {ECO:0000269\|PubMed:2531657}.


Subunit:		Disulfide-linked to apo-B100. Binds to fibronectin and decorin.
Ptm:		N- and O-glycosylated. The N-glycans are complex biantennary structures present in either a mono- or disialylated state. The O- glycans are mostly (80%) represented by the monosialylated core type I structure, NeuNAcalpha2-3Galbeta1-3GalNAc, with smaller amounts of disialylated and non-sialylated O-glycans also detected. {ECO:0000269\|PubMed:11294842}.
Polymorphism:		LPA genetic variants, including variations in the number of Kringle domains, define the lipoprotein(a) quantitative trait locus (LPAQTL) and influence lipoprotein(a) levels in plasma [MIM:618807]. The reference genome sequence encodes a variant that contains 16 Kringle domains and that lack residues 533 to 3040. Depending on the individual, the encoded protein contains 2-43 copies of kringle-type domains. The allele represented here contains 38 copies of the kringle- type repeats. {ECO:0000269\|PubMed:3670400}.
Miscellaneous:		Apo(a) is known to be proteolytically cleaved, leading to the formation of the so-called mini-Lp(a). Apo(a) fragments accumulate in atherosclerotic lesions, where they may promote thrombogenesis. O-glycosylation may limit the extent of proteolytic fragmentation. Homology with plasminogen kringles IV and V is thought to underlie the atherogenicity of the protein, because the fragments are competing with plasminogen for fibrin(ogen) binding.
Similarity:		Belongs to the peptidase S1 family. Plasminogen subfamily. {ECO:0000255\|PROSITE-ProRule:PRU00274}.