UniProt functional annotation for P19999



	UniProt functional annotation for P19999

UniProt code: P19999.

Organism: Rattus norvegicus (Rat).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.

Function: Calcium-dependent lectin (PubMed:1436090, PubMed:9033386, PubMed:11850428). Plays a role in the innate immune response by binding mannose, fucose and N-acetylglucosamine moieties on different microorganisms and mediating activation of the lectin complement pathway (PubMed:3584121). Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages (By similarity). {ECO:0000250, ECO:0000269|PubMed:11850428, ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:3584121, ECO:0000269|PubMed:9033386}.

Subunit: Homotrimer (PubMed:7704532, PubMed:9033386, PubMed:11850428, PubMed:25419660). Forms higher oligomeric complexes formed by the association of two, three or more homotrimers (PubMed:10903744, PubMed:25419660). Oligomerization occurs in the endoplasmic reticulum (By similarity). Interacts with MASP1 and MASP2 (PubMed:10913141). {ECO:0000250, ECO:0000269|PubMed:10903744, ECO:0000269|PubMed:10913141, ECO:0000269|PubMed:11850428, ECO:0000269|PubMed:25419660, ECO:0000269|PubMed:7704532, ECO:0000269|PubMed:9033386}.

Subcellular location: Secreted {ECO:0000269|PubMed:10903744, ECO:0000269|PubMed:25419660, ECO:0000269|PubMed:3584121}. Note=According to PubMed:10903744, long retention times in the endoplasmic reticulum and the Golgi apparatus that have been observed in former studies may reflect the abnormal physiology of the hepatoma cells used.

Tissue specificity: Detected in blood serum (at protein level). {ECO:0000269|PubMed:3584121}.

Domain: The helical collagen-like domains from three protein chains assemble into a coiled coil and mediate trimerization. {ECO:0000269|PubMed:11850428, ECO:0000269|PubMed:7704532, ECO:0000269|PubMed:9033386}.

Ptm: Hydroxylated on lysine and proline residues within the collagen- like domain. {ECO:0000269|PubMed:10903744, ECO:0000269|PubMed:25419660}.

Ptm: O-glycosylated. O-linked glycans on hydroxylysine residues consist of Glc-Gal disaccharides bound to the oxygen atom of post- translationally added hydroxyl groups. {ECO:0000269|PubMed:10903744, ECO:0000269|PubMed:25419660}.

Annotations taken from UniProtKB at the EBI.


Organism:		Rattus norvegicus (Rat).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.



Function:		Calcium-dependent lectin (PubMed:1436090, PubMed:9033386, PubMed:11850428). Plays a role in the innate immune response by binding mannose, fucose and N-acetylglucosamine moieties on different microorganisms and mediating activation of the lectin complement pathway (PubMed:3584121). Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages (By similarity). {ECO:0000250, ECO:0000269\|PubMed:11850428, ECO:0000269\|PubMed:1436090, ECO:0000269\|PubMed:3584121, ECO:0000269\|PubMed:9033386}.


Subunit:		Homotrimer (PubMed:7704532, PubMed:9033386, PubMed:11850428, PubMed:25419660). Forms higher oligomeric complexes formed by the association of two, three or more homotrimers (PubMed:10903744, PubMed:25419660). Oligomerization occurs in the endoplasmic reticulum (By similarity). Interacts with MASP1 and MASP2 (PubMed:10913141). {ECO:0000250, ECO:0000269\|PubMed:10903744, ECO:0000269\|PubMed:10913141, ECO:0000269\|PubMed:11850428, ECO:0000269\|PubMed:25419660, ECO:0000269\|PubMed:7704532, ECO:0000269\|PubMed:9033386}.
Subcellular location:		Secreted {ECO:0000269\|PubMed:10903744, ECO:0000269\|PubMed:25419660, ECO:0000269\|PubMed:3584121}. Note=According to PubMed:10903744, long retention times in the endoplasmic reticulum and the Golgi apparatus that have been observed in former studies may reflect the abnormal physiology of the hepatoma cells used.
Tissue specificity:		Detected in blood serum (at protein level). {ECO:0000269\|PubMed:3584121}.
Domain:		The helical collagen-like domains from three protein chains assemble into a coiled coil and mediate trimerization. {ECO:0000269\|PubMed:11850428, ECO:0000269\|PubMed:7704532, ECO:0000269\|PubMed:9033386}.
Ptm:		Hydroxylated on lysine and proline residues within the collagen- like domain. {ECO:0000269\|PubMed:10903744, ECO:0000269\|PubMed:25419660}.
Ptm:		O-glycosylated. O-linked glycans on hydroxylysine residues consist of Glc-Gal disaccharides bound to the oxygen atom of post- translationally added hydroxyl groups. {ECO:0000269\|PubMed:10903744, ECO:0000269\|PubMed:25419660}.