UniProt functional annotation for Q9UBG0



	UniProt functional annotation for Q9UBG0

UniProt code: Q9UBG0.

Organism: Homo sapiens (Human).

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

Function: May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). {ECO:0000269|PubMed:10683150, ECO:0000269|PubMed:12972549}.

Subunit: Interacts with C-terminal region of type I collagen/COL1A1 (By similarity). Interacts directly with PLAUR/UPAR and PLAU/pro-UPA to form a tri-molecular complex. Interacts with collagen V. {ECO:0000250, ECO:0000269|PubMed:10636902}.

Subcellular location: Membrane; Single-pass type I membrane protein.

Tissue specificity: Ubiquitous with low expression in brain, placenta, lung, kidney, pancreas, spleen, thymus and colon. Expressed in endothelial cells, fibroblasts and macrophages. Highly expressed in fetal lung and kidney. {ECO:0000269|PubMed:10683150, ECO:0000269|PubMed:8702911}.

Domain: C-type lectin domains 3 to 8 are not required for calcium- dependent binding of mannose, fucose and N-acetylglucosamine. C-type lectin domain 2 is responsible for sugar-binding in a calcium-dependent manner.

Domain: Fibronectin type-II domain mediates collagen-binding.

Domain: Ricin B-type lectin domain contacts with the second C-type lectin domain. {ECO:0000250}.

Ptm: N-glycosylated. {ECO:0000269|PubMed:10683150, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218}.

Sequence caution: Sequence=BAA31684.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};

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:		May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). {ECO:0000269\|PubMed:10683150, ECO:0000269\|PubMed:12972549}.


Subunit:		Interacts with C-terminal region of type I collagen/COL1A1 (By similarity). Interacts directly with PLAUR/UPAR and PLAU/pro-UPA to form a tri-molecular complex. Interacts with collagen V. {ECO:0000250, ECO:0000269\|PubMed:10636902}.
Subcellular location:		Membrane; Single-pass type I membrane protein.
Tissue specificity:		Ubiquitous with low expression in brain, placenta, lung, kidney, pancreas, spleen, thymus and colon. Expressed in endothelial cells, fibroblasts and macrophages. Highly expressed in fetal lung and kidney. {ECO:0000269\|PubMed:10683150, ECO:0000269\|PubMed:8702911}.
Domain:		C-type lectin domains 3 to 8 are not required for calcium- dependent binding of mannose, fucose and N-acetylglucosamine. C-type lectin domain 2 is responsible for sugar-binding in a calcium-dependent manner.
Domain:		Fibronectin type-II domain mediates collagen-binding.
Domain:		Ricin B-type lectin domain contacts with the second C-type lectin domain. {ECO:0000250}.
Ptm:		N-glycosylated. {ECO:0000269\|PubMed:10683150, ECO:0000269\|PubMed:19139490, ECO:0000269\|PubMed:19159218}.
Sequence caution:		Sequence=BAA31684.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};