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InterPro: IPR008160 Collagen triple helix repeat

Protein matches Help

UniProtKB

Matches:

3719 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR008160 Collagen

Secondary

IPR000087

Type

Repeat

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01391	Collagen	3719
Signatures in BioMart

InterPro Relationships Help

Found in

IPR017095 Transforming, StpC

InterPro annotation

Entry Details in BioMart

Abstract

Members of this family belong to the collagen superfamily [1]. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The sequence is predominantly repeats of the G-X-Y and the polypeptide chains form a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxyproline. Collagens are post-translationally modified by proline hydroxylase to form the hydroxyproline residues. Defective hydroxylation is the cause of scurvy.

Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure.

Structural links Help

PDB - click here

SCOP: h.1.1.1 , k.3.1.1

CATH: 1.20.5.360

Database links Help

PANDIT: PF01391

Blocks: IPB008160

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR008160

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

B4YNE6 Collagen-like protein V6

B7Z0K8 Collagen alpha chain CG42342

O00602 Ficolin-1

O35206 Collagen alpha-1(XV) chain

O76368 Putative cuticle collagen 99

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR014716	Fibrinogen, alpha/beta/gamma chain, C-terminal globular, subdomain 1
IPR010515	Collagenase NC10/endostatin
IPR020837	Fibrinogen, conserved site
IPR001791	Laminin G
IPR002181	Fibrinogen, alpha/beta/gamma chain, C-terminal globular
IPR016187	C-type lectin fold
IPR016186	C-type lectin-like
IPR008160	Collagen triple helix repeat
IPR003129	Laminin G, thrombospondin-type, N-terminal
IPR008985	Concanavalin A-like lectin/glucanase
IPR012680	Laminin G, subdomain 2
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Mayne R, Brewton RG. New members of the collagen superfamily. Curr. Opin. Cell Biol. 5 883-90 1993 [PubMed: 8240831] http://dx.doi.org/10.1016/0955-0674(93)90039-S

Additional Reading Open in usermanual
	Crouch E, McDonald B, Smith K, Roberts M, Mealy T, Seaton B, Head J. Critical role of Arg/Lys343 in the species-dependent recognition of phosphatidylinositol by pulmonary surfactant protein D. Biochemistry 46 2007 5160-9 [PubMed: 17417879] http://dx.doi.org/10.1021/bi700037x
	Wang L, Brauner JW, Mao G, Crouch E, Seaton B, Head J, Smith K, Flach CR, Mendelsohn R. Interaction of recombinant surfactant protein D with lipopolysaccharide: conformation and orientation of bound protein by IRRAS and simulations. Biochemistry 47 2008 8103-13 [PubMed: 18620419] http://dx.doi.org/10.1021/bi800626h
	Wang H, Head J, Kosma P, Brade H, Muller-Loennies S, Sheikh S, McDonald B, Smith K, Cafarella T, Seaton B, Crouch E. Recognition of heptoses and the inner core of bacterial lipopolysaccharides by surfactant protein d. Biochemistry 47 2008 710-20 [PubMed: 18092821] http://dx.doi.org/10.1021/bi7020553
	Emsley J, Knight CG, Farndale RW, Barnes MJ. Structure of the integrin alpha2beta1-binding collagen peptide. J. Mol. Biol. 335 2004 1019-28 [PubMed: 14698296] http://dx.doi.org/10.1016/j.jmb.2003.11.030
	Crouch E, McDonald B, Smith K, Cafarella T, Seaton B, Head J. Contributions of phenylalanine 335 to ligand recognition by human surfactant protein D: ring interactions with SP-D ligands. J. Biol. Chem. 281 2006 18008-14 [PubMed: 16636058] http://dx.doi.org/10.1074/jbc.M601749200

InterPro 23.1