UniProt functional annotation for Q7SIB2



	UniProt functional annotation for Q7SIB2

UniProt code: Q7SIB2.

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. {ECO:0000250|UniProtKB:P02463}.

Function: Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. {ECO:0000250|UniProtKB:P02462}.

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:P02463, ECO:0000305|PubMed:11970952}.

Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:P02463}.

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. {ECO:0000305}.

Ptm: Lysines at the third position of the tripeptide repeating unit (G- X-Y) are hydroxylated in all cases. The modified lysines can be O- glycosylated. {ECO:0000250|UniProtKB:P02462}.

Ptm: Contains 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P02462}.

Ptm: Contains 3-hydroxyproline (PubMed:24368846). This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline (By similarity). {ECO:0000250|UniProtKB:P02463, ECO:0000269|PubMed:24368846}.

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. {ECO:0000250|UniProtKB:P02462}.

Ptm: The trimeric structure of the NC1 domains is stabilized by covalent bonds (sulfilimine cross-links) between Lys and Met residues (PubMed:19729652). These cross-links are important for the mechanical stability of the basement membrane (By similarity). {ECO:0000250|UniProtKB:P02463, ECO:0000269|PubMed:19729652}.

Ptm: Proteolytic processing produces the C-terminal NC1 peptide, arresten. {ECO:0000250|UniProtKB:P02462}.

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. {ECO:0000250\|UniProtKB:P02463}.



Function:		Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. {ECO:0000250\|UniProtKB:P02462}.


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:P02463, ECO:0000305\|PubMed:11970952}.
Subcellular location:		Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250\|UniProtKB:P02463}.
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. {ECO:0000305}.
Ptm:		Lysines at the third position of the tripeptide repeating unit (G- X-Y) are hydroxylated in all cases. The modified lysines can be O- glycosylated. {ECO:0000250\|UniProtKB:P02462}.
Ptm:		Contains 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250\|UniProtKB:P02462}.
Ptm:		Contains 3-hydroxyproline (PubMed:24368846). This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline (By similarity). {ECO:0000250\|UniProtKB:P02463, ECO:0000269\|PubMed:24368846}.
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. {ECO:0000250\|UniProtKB:P02462}.
Ptm:		The trimeric structure of the NC1 domains is stabilized by covalent bonds (sulfilimine cross-links) between Lys and Met residues (PubMed:19729652). These cross-links are important for the mechanical stability of the basement membrane (By similarity). {ECO:0000250\|UniProtKB:P02463, ECO:0000269\|PubMed:19729652}.
Ptm:		Proteolytic processing produces the C-terminal NC1 peptide, arresten. {ECO:0000250\|UniProtKB:P02462}.
Similarity:		Belongs to the type IV collagen family. {ECO:0000255\|PROSITE-ProRule:PRU00736}.