Protein Domain : IPR001715

Type:  Domain Name:  Calponin homology domain
Description:  A number of actin-binding proteins, including spectrin, alpha-actinin and fimbrin, contain a 250 amino acid stretch called the actin binding domain(ABD). The ABD has probably arisen from duplication of a domain which is also found in a single copy in a number of other proteins like calponin or the vavproto-oncogene and has been called calponin homology (CH) domain [, ].A detailed analysis of The CH domain-containing proteins has shown that they can be divided in three groups []:The fimbrin family of monomeric actin cross-linking molecules containing two ABDsDimeric cross-linking proteins (alpha-actinin, beta-spectrin, filamin, etc.) and monomeric F-actin binding proteins (dystrophin, utrophin) each containing one ABDProteins containing only a single amino terminal CH domain. Each single ABD, comprising two CH domains, is able to bind one actin monomer in the filament. The amino terminal CH domain has the intrinsic ability tobind actin, albeit with lower affinity than the complete ABD, whereas the carboxy terminal CH bind actin extremely weakly or not at all. Neverthelessboth CH domains are required for a fully functional ABD; the C-terminal CH domain contributing to the overall stability of the complete ABD throughinter-domain helix-helix interactions []. Some of the proteins containing asingle CH domain also bind to actin, although this has not been shown to be via the single CH domain alone []. In addition, the CH domain occurs also ina number of proteins not known to bind actin, a notable example being the vav protooncogene.The resolution of the 3D structure of various CH domains has shown that the conserved core consist of four major alpha-helices [].Proteins containing a calponin domain include: Calponin, which is involved in the regulation of contractility and organisation of the actin cytoskeleton in smooth muscle cells [].Beta-spectrin, a major component of a submembrane cytoskeletal network connecting actin filaments to integral plasma membrane proteins [].The actin-cross-linking domain of the fimbrin/plastin family of actin filament bundling or cross-linking proteins [].Utrophin,a close homologue of dystrophin [].Dystrophin, the protein found to be defective in Duchenne muscular dystrophy; this protein contains a tandem repeat of two CH domains [].Actin-binding domain of plectin, a large and widely expressed cytolinker protein [].The N-terminal microtubule-binding domain of microtubule-associated protein eb1 (end-binding protein), a member of a conserved family of proteins that localise to the plus-ends of microtubules [].Ras GTPase-activating-like protein rng2, an IQGAP protein that is essential for the assembly of an actomyosin ring during cytokinesis [].Transgelin, which suppresses androgen receptor transactivation []. Short Name:  CH-domain

2 Child Features

DB identifier Type Name
IPR010441 Domain CH-like domain in sperm protein
IPR022613 Domain Calmodulin-regulated spectrin-associated protein, CH domain

1 Contains

DB identifier Type Name
IPR001589 Conserved_site Actinin-type actin-binding domain, conserved site

5 Cross Referencess

Identifier
PF00307
PS50021
SM00033
G3DSA:1.10.418.10
SSF47576

5 Found Ins

DB identifier Type Name
IPR003096 Family Smooth muscle protein/calponin
IPR016344 Family Dystrophin
IPR016343 Family Spectrin, beta subunit
IPR001061 Family Transgelin-2
IPR001997 Family Calponin/LIMCH1

1 GO Annotation

GO Term Gene Name
GO:0005515 IPR001715

1 Ontology Annotations

GO Term Gene Name
GO:0005515 IPR001715

0 Parent Features

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
412333 D8RKT7 PAC:15410802 Selaginella moellendorffii 200  
432244 D8TFE9 PAC:15402052 Selaginella moellendorffii 131  
57110 D8RTQ2 PAC:15401872 Selaginella moellendorffii 240  
404782 D8QXC1 PAC:15412605 Selaginella moellendorffii 1838  
233006 D8S323 PAC:15419445 Selaginella moellendorffii 660  
109778 D8S6C5 PAC:15406589 Selaginella moellendorffii 660  
66631 D8R0M6 PAC:15410042 Selaginella moellendorffii 263  
419634 D8S9J6 PAC:15411245 Selaginella moellendorffii 1459  
156878 D8SN93 PAC:15412326 Selaginella moellendorffii 638  
423909 D8SN72 PAC:15402984 Selaginella moellendorffii 176  
423931 D8SN95 PAC:15403038 Selaginella moellendorffii 179  
423927 D8SN91 PAC:15403024 Selaginella moellendorffii 309  
423908 D8SN71 PAC:15402982 Selaginella moellendorffii 144  
7821 D8SN90 PAC:15405218 Selaginella moellendorffii 86  
446038 D8SN73 PAC:15419400 Selaginella moellendorffii 247  
446318 D8SQE4 PAC:15421549 Selaginella moellendorffii 396  
424886 D8SRB6 PAC:15405323 Selaginella moellendorffii 189  
424859 D8SR88 PAC:15405272 Selaginella moellendorffii 328  
424858 D8SR87 PAC:15405271 Selaginella moellendorffii 126  
424862 D8SR92 PAC:15405284 Selaginella moellendorffii 234  
425231 D8SSF6 PAC:15403504 Selaginella moellendorffii 564  
124154 D8ST30 PAC:15401744 Selaginella moellendorffii 633  
48832 D8SSS5 PAC:15402939 Selaginella moellendorffii 118  
169724 D8RAS4 PAC:15404970 Selaginella moellendorffii 724  
429928 D8T7S0 PAC:15420642 Selaginella moellendorffii 434  
429462 D8T698 PAC:15416940 Selaginella moellendorffii 291  
evm.TU.contig_48088.1 PAC:16432496 Carica papaya 84  
evm.model.supercontig_12.224 PAC:16406775 Carica papaya 688  
evm.model.supercontig_12.99 PAC:16406943 Carica papaya 1149  
evm.model.supercontig_151.38 PAC:16409556 Carica papaya 812  

10 Publications

First Author Title Year Journal Volume Pages PubMed ID
            17082327
            9708889
            9887274
            10801490
            11839310
            15272162
            12857735
            15128297
            9302997
            17121810