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InterPro: IPR018248 EF-Hand domain

Protein matches Help

UniProtKB

Matches:

10681 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

IPR018248 EF_Hand_dom

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00036	efhand	10681
Signatures in BioMart

InterPro Relationships Help

Parent

IPR002048 Calcium-binding EF-hand

Found in

IPR000261 EPS15 homology (EH)
IPR001125 Recoverin
IPR003299 Flagellar calcium-binding protein (calflagin)
IPR008080 Parvalbumin
IPR011992 EF-hand-like domain
IPR012008 Serine/threonine protein phosphatase, EF-hand-containing
IPR015754 Calcium binding protein
IPR015756 Guanylate cyclase activating protein 2
IPR015757 Calcineurin B protein
IPR016688 Membrane protein, At2g17000, predicted
IPR020639 Calcyphosin-like
IPR020642 Calcium-dependent protein kinase

Contains

IPR001751 S100/CaBP-9k-type, calcium binding
IPR018247 EF-Hand 1, calcium-binding site

InterPro annotation

Entry Details in BioMart

Abstract

Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. This type of domain consists of a twelve residue loop flanked on both side by a twelve residue alpha-helical domain. In an EF-hand loop the calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X and -Z. The invariant Glu or Asp at position 12 provides two oxygens for liganding Ca (bidentate ligand).

Structural links Help

PDB - click here

SCOP: a.39.1.1 , a.39.1.10 , a.39.1.2 , a.39.1.4 , a.39.1.5 , a.39.1.6 , a.39.1.8

CATH: 1.10.238.10

Database links Help

Pfam Clan: CL0220.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018248

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O14815 Calpain-9

O16305 Calmodulin

P06704 Cell division control protein 31

P12815 Programmed cell death protein 6

P13395 Spectrin alpha chain

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011992	EF-hand-like domain
IPR002048	Calcium-binding EF-hand
IPR001452	Src homology-3 domain
IPR001300	Peptidase C2, calpain
IPR018159	Spectrin/alpha-actinin
IPR018247	EF-Hand 1, calcium-binding site
IPR018249	EF-HAND 2
IPR018248	EF-Hand domain
IPR000169	Peptidase, cysteine peptidase active site
IPR013315	Spectrin alpha chain, SH3 domain
IPR014837	EF-hand, Ca insensitive
IPR020473	Src homology-3, region
IPR002017	Spectrin repeat
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Finn BE, Forsen S. The evolving model of calmodulin structure, function and activation. Structure 3 1995 7-11 [PubMed: 7743133] http://dx.doi.org/10.1016/S0969-2126(01)00130-7
	Zhukov I, Ejchart A, Bierzynski A. Structural and motional changes induced in apo-S100A1 protein by the disulfide formation between its Cys 85 residue and beta-mercaptoethanol. Biochemistry 47 2008 640-50 [PubMed: 18088104] http://dx.doi.org/10.1021/bi701762v
	Lee YT, Dimitrova YN, Schneider G, Ridenour WB, Bhattacharya S, Soss SE, Caprioli RM, Filipek A, Chazin WJ. Structure of the S100A6 complex with a fragment from the C-terminal domain of Siah-1 interacting protein: a novel mode for S100 protein target recognition. Biochemistry 47 2008 10921-32 [PubMed: 18803400] http://dx.doi.org/10.1021/bi801233z
	Hogue CW, MacManus JP, Banville D, Szabo AG. Comparison of terbium (III) luminescence enhancement in mutants of EF hand calcium binding proteins. J. Biol. Chem. 267 1992 13340-7 [PubMed: 1618836] http://intl.jbc.org/cgi/reprint/267/19/13340.pdf
	Bairoch A, Cox JA. EF-hand motifs in inositol phospholipid-specific phospholipase C. FEBS Lett. 269 1990 454-6 [PubMed: 2401372] http://dx.doi.org/10.1016/0014-5793(90)81214-9
	Nakayama S, Moncrief ND, Kretsinger RH. Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories. J. Mol. Evol. 34 1992 416-48 [PubMed: 1602495] http://dx.doi.org/10.1007/BF00162998
	Ishida H, Borman MA, Ostrander J, Vogel HJ, MacDonald JA. Solution structure of the calponin homology (CH) domain from the smoothelin-like 1 protein: a unique apocalmodulin-binding mode and the possible role of the C-terminal type-2 CH-domain in smooth muscle relaxation. J. Biol. Chem. 283 2008 20569-78 [PubMed: 18477568] http://dx.doi.org/10.1074/jbc.M800627200
	Gsponer J, Christodoulou J, Cavalli A, Bui JM, Richter B, Dobson CM, Vendruscolo M. A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction. Structure 16 2008 736-46 [PubMed: 18462678] http://dx.doi.org/10.1016/j.str.2008.02.017
	Halling DB, Georgiou DK, Black DJ, Yang G, Fallon JL, Quiocho FA, Pedersen SE, Hamilton SL. Determinants in CaV1 channels that regulate the Ca2+ sensitivity of bound calmodulin. J. Biol. Chem. 284 2009 20041-51 [PubMed: 19473981] http://dx.doi.org/10.1074/jbc.M109.013326

InterPro 23.1