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InterPro: IPR018249 EF-HAND 2

Protein matches Help

UniProtKB

Matches:

16119 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

IPR018249 EF_HAND_2

Type

Repeat

Signatures Help

Database	ID	Name	Proteins
PROSITE profile	PS50222	EF_HAND_2	16119
Signatures in BioMart

InterPro Relationships Help

Children

IPR002048 Calcium-binding EF-hand

Found in

IPR000261 EPS15 homology (EH)
IPR001125 Recoverin
IPR003299 Flagellar calcium-binding protein (calflagin)
IPR005447 Voltage-dependent calcium channel, N-type, alpha-1 subunit
IPR005449 Voltage-dependent calcium channel, R-type, alpha-1 subunit
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
IPR016359 SPARC-like protein 1
IPR016688 Membrane protein, At2g17000, predicted
IPR020639 Calcyphosin-like
IPR020642 Calcium-dependent protein kinase

Contains

IPR001751 S100/Calbindin-D9k, conserved site
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.39.1.7 , a.39.1.8 , a.39.1.9 , b.55.1.1

CATH: 1.10.238.10 , 1.10.238.110

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018249

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O14815 Calpain-9

O16305 Calmodulin

O70200 Allograft inflammatory factor 1

P06704 Cell division control protein 31

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
	Akaboshi M, Hashimoto H, Ishida H, Saijo S, Koizumi N, Sato M, Shimizu T. The crystal structure of plant-specific calcium-binding protein AtCBL2 in complex with the regulatory domain of AtCIPK14. J. Mol. Biol. 377 2008 246-57 [PubMed: 18237745] http://dx.doi.org/10.1016/j.jmb.2008.01.006
	Strynadka NC, James MN. Crystal structures of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 58 1989 951-98 [PubMed: 2673026] http://dx.doi.org/10.1146/annurev.bi.58.070189.004511
	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
	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
	Chauvaux S, Beguin P, Aubert JP, Bhat KM, Gow LA, Wood TM, Bairoch A. Calcium-binding affinity and calcium-enhanced activity of Clostridium thermocellum endoglucanase D. Biochem. J. 265 1990 261-5 [PubMed: 2302168] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=2302168
	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
	Kretsinger RH. Calcium coordination and the calmodulin fold: divergent versus convergent evolution. Cold Spring Harb. Symp. Quant. Biol. 52 1987 499-510 [PubMed: 3454274]
	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
	Heizmann CW, Hunziker W. Intracellular calcium-binding proteins: more sites than insights. Trends Biochem. Sci. 16 1991 98-103 [PubMed: 2058003] http://dx.doi.org/10.1016/0968-0004(91)90041-S
	Gingras AR, Basran J, Prescott A, Kriajevska M, Bagshaw CR, Barsukov IL. Crystal structure of the Ca(2+)-form and Ca(2+)-binding kinetics of metastasis-associated protein, S100A4. FEBS Lett. 582 2008 1651-6 [PubMed: 18435928] http://dx.doi.org/10.1016/j.febslet.2008.04.017
	Kawasaki H, Kretsinger RH. Calcium-binding proteins 1: EF-hands. 2 1995 297-490 [PubMed: 7553064]
	Moncrief ND, Kretsinger RH, Goodman M. Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences. J. Mol. Evol. 30 1990 522-62 [PubMed: 2115931] http://dx.doi.org/10.1007/BF02101108
	Kligman D, Hilt DC. The S100 protein family. Trends Biochem. Sci. 13 1988 437-43 [PubMed: 3075365] http://dx.doi.org/10.1016/0968-0004(88)90218-6
	Pathuri P, Vogeley L, Luecke H. Crystal structure of metastasis-associated protein S100A4 in the active calcium-bound form. J. Mol. Biol. 383 2008 62-77 [PubMed: 18783790] http://dx.doi.org/10.1016/j.jmb.2008.04.076
	Haiech J, Sallantin J. Computer search of calcium binding sites in a gene data bank: use of learning techniques to build an expert system. Biochimie 67 1985 555-60 [PubMed: 3839696] http://dx.doi.org/10.1016/S0300-9084(85)80276-5

InterPro 24.0