UniProt functional annotation for Q7SIB3



	UniProt functional annotation for Q7SIB3

UniProt code: Q7SIB3.

Organism: Bos taurus (Bovine).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.

Function: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Potently inhibits angiogenesis and tumor growth (By similarity). {ECO:0000250}.

Subunit: There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network. Interacts with EFEMP2 (By similarity). {ECO:0000250|UniProtKB:P08122}.

Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane.

Domain: Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.

Ptm: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Ptm: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.

Ptm: The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues. {ECO:0000250}.

Similarity: Belongs to the type IV collagen family. {ECO:0000255|PROSITE-ProRule:PRU00736}.

Annotations taken from UniProtKB at the EBI.


Organism:		Bos taurus (Bovine).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.



Function:		Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. Potently inhibits angiogenesis and tumor growth (By similarity). {ECO:0000250}.


Subunit:		There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network. Interacts with EFEMP2 (By similarity). {ECO:0000250\|UniProtKB:P08122}.
Subcellular location:		Secreted, extracellular space, extracellular matrix, basement membrane.
Domain:		Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.
Ptm:		Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Ptm:		Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.
Ptm:		The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues. {ECO:0000250}.
Similarity:		Belongs to the type IV collagen family. {ECO:0000255\|PROSITE-ProRule:PRU00736}.