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InterPro: IPR002048 Calcium-binding EF-hand

Protein matches Help

UniProtKB

Matches:

11184 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

IPR002048 EF_hand_Ca_bd

Type

Repeat

Signatures Help

Database	ID	Name	Proteins
SMART	SM00054	EFh	11184
Signatures in BioMart

InterPro Relationships Help

Parent

IPR018249 EF-HAND 2

Children

IPR018248 EF-Hand domain

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
IPR015070 Domain of unknown function DUF1880
IPR015754 Calcium binding protein
IPR015756 Guanylate cyclase activating protein 2
IPR015757 Calcineurin B protein
IPR020639 Calcyphosin-like
IPR020642 Calcium-dependent protein kinase

Contains

IPR018247 EF-Hand 1, calcium-binding site

GO Term annotation Help

Function

GO:0005509 calcium ion binding

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.39.1.10 , a.39.1.4 , a.39.1.5 , a.39.1.6 , a.39.1.7 , a.39.1.8 , a.39.1.9

CATH: 1.10.238.10 , 1.10.238.110

Database links Help

PDBe-motif: PS00018

PROSITE doc: PDOC00018

PANDIT: PF00036

COMe: PRX000900

Interactions Help

This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002048

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
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
	Henzl MT, Tanner JJ. Solution structure of Ca2+-free rat alpha-parvalbumin. Protein Sci. 17 2008 431-8 [PubMed: 18218708] http://dx.doi.org/10.1110/ps.073318308
	Verdino P, Barderas R, Villalba M, Westritschnig K, Valenta R, Rodriguez R, Keller W. Three-dimensional structure of the cross-reactive pollen allergen Che a 3: visualizing cross-reactivity on the molecular surfaces of weed, grass, and tree pollen allergens. J. Immunol. 180 2008 2313-21 [PubMed: 18250440]
	Jung YS, Kim KS, Kim KD, Lim JS, Kim JW, Kim E. Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells. Biochem. Biophys. Res. Commun. 288 2001 420-6 [PubMed: 11606059] http://dx.doi.org/10.1006/bbrc.2001.5769
	Stepanyuk GA, Liu ZJ, Markova SS, Frank LA, Lee J, Vysotski ES, Wang BC. Crystal structure of coelenterazine-binding protein from Renilla muelleri at 1.7 A: why it is not a calcium-regulated photoprotein. Photochem. Photobiol. Sci. 7 2008 442-7 [PubMed: 18385886] http://dx.doi.org/10.1039/b716535h
	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
	Menetrey J, Llinas P, Cicolari J, Squires G, Liu X, Li A, Sweeney HL, Houdusse A. The post-rigor structure of myosin VI and implications for the recovery stroke. EMBO J. 27 2008 244-52 [PubMed: 18046460] http://dx.doi.org/10.1038/sj.emboj.7601937

InterPro 24.0