UniProt functional annotation for P04004



	UniProt functional annotation for P04004

UniProt code: P04004.

Organism: Homo sapiens (Human).

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

Function: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.

Function: Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.

Subunit: Exists in two forms: a single chain 75 kDa form (V75) and a clipped form composed of two chains (65 kDa and 10 kDa) (V65+V10) which are held together by a disulfide bond. Interacts with SERPINE1/PAI1, insulin and C1QBP. {ECO:0000269|PubMed:12808446, ECO:0000269|PubMed:1704366, ECO:0000269|PubMed:1709100, ECO:0000269|PubMed:7522053, ECO:0000269|PubMed:8900153}.

Subunit: (Microbial infection) Interacts (via hemopexin repeat 2) with P.falciparum (isolate CDC / Honduras) SERA5 P47 (via C-terminus); may form heterotetramers of two VTN and SERA5 P47 heterodimers; the interaction may protect merozoites from phagocytosis by host monocytes; VTN glycosylation appears to be dispensable for the interaction. {ECO:0000269|PubMed:29567995}.

Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:2448300, ECO:0000269|PubMed:29567995}.

Subcellular location: Parasitophorous vacuole {ECO:0000269|PubMed:29567995}. Note=(Microbial infection) In P.falciparum-infected red blood cells, VTN internalization is detected at the early trophozoite stage (PubMed:29567995). Colocalizes with SERA5 at the schizont stage and with SERA5 P47 at the merozoite surface (PubMed:29567995). {ECO:0000269|PubMed:29567995}.

Tissue specificity: Expressed in the retina pigment epithelium (at protein level) (PubMed:25136834). Expressed in plasma (at protein level) (PubMed:2448300). Expressed in serum (at protein level) (PubMed:29567995). {ECO:0000269|PubMed:2448300, ECO:0000269|PubMed:25136834, ECO:0000269|PubMed:29567995}.

Domain: The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin.

Ptm: Sulfated on tyrosine residues. {ECO:0000269|PubMed:17558413, ECO:0000269|PubMed:2479556, ECO:0000269|PubMed:25136834}.

Ptm: N- and O-glycosylated. {ECO:0000250}.

Ptm: Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading. {ECO:0000269|PubMed:9733784}.

Ptm: It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.

Ptm: Phosphorylation sites are present in the extracellular medium.

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:		Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.



Function:		Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.


Subunit:		Exists in two forms: a single chain 75 kDa form (V75) and a clipped form composed of two chains (65 kDa and 10 kDa) (V65+V10) which are held together by a disulfide bond. Interacts with SERPINE1/PAI1, insulin and C1QBP. {ECO:0000269\|PubMed:12808446, ECO:0000269\|PubMed:1704366, ECO:0000269\|PubMed:1709100, ECO:0000269\|PubMed:7522053, ECO:0000269\|PubMed:8900153}.
Subunit:		(Microbial infection) Interacts (via hemopexin repeat 2) with P.falciparum (isolate CDC / Honduras) SERA5 P47 (via C-terminus); may form heterotetramers of two VTN and SERA5 P47 heterodimers; the interaction may protect merozoites from phagocytosis by host monocytes; VTN glycosylation appears to be dispensable for the interaction. {ECO:0000269\|PubMed:29567995}.
Subcellular location:		Secreted, extracellular space {ECO:0000269\|PubMed:2448300, ECO:0000269\|PubMed:29567995}.
Subcellular location:		Parasitophorous vacuole {ECO:0000269\|PubMed:29567995}. Note=(Microbial infection) In P.falciparum-infected red blood cells, VTN internalization is detected at the early trophozoite stage (PubMed:29567995). Colocalizes with SERA5 at the schizont stage and with SERA5 P47 at the merozoite surface (PubMed:29567995). {ECO:0000269\|PubMed:29567995}.
Tissue specificity:		Expressed in the retina pigment epithelium (at protein level) (PubMed:25136834). Expressed in plasma (at protein level) (PubMed:2448300). Expressed in serum (at protein level) (PubMed:29567995). {ECO:0000269\|PubMed:2448300, ECO:0000269\|PubMed:25136834, ECO:0000269\|PubMed:29567995}.
Domain:		The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin.
Ptm:		Sulfated on tyrosine residues. {ECO:0000269\|PubMed:17558413, ECO:0000269\|PubMed:2479556, ECO:0000269\|PubMed:25136834}.
Ptm:		N- and O-glycosylated. {ECO:0000250}.
Ptm:		Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading. {ECO:0000269\|PubMed:9733784}.
Ptm:		It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.
Ptm:		Phosphorylation sites are present in the extracellular medium.