second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 186 QRKAIKALLAWVQRKTRKYGVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALENSTRENLEKAFSIAQDALHIPRLLE 265
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                          90       100
                  ....*....|....*....|....*.
gi 2462541597 266 PEDIMVDTPDEQSIMTYVAQFLERFP 291
Cdd:cd21245    81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106

second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 186 QRKAIKALLAWVQRKTRKYGVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALENSTRENLEKAFSIAQDALHIPRLLE 265
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                          90       100
                  ....*....|....*....|....*.
gi 2462541597 266 PEDIMVDTPDEQSIMTYVAQFLERFP 291
Cdd:cd21245    81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 191 KALLAWVQRKTRKYG--VAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQ--ALENSTRENLEKAFSIAQDALHIPR-LLE 265
Cdd:pfam00307   5 KELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlnKSEFDKLENINLALDVAEKKLGVPKvLIE 84

                          90       100
                  ....*....|....*....|....*.
gi 2462541597 266 PEDImVDtPDEQSIMTYVAQFLERFP 291
Cdd:pfam00307  85 PEDL-VE-GDNKSVLTYLASLFRRFQ 108

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597   36 RTFTRWINLHLEKcNPPLEVKDLFVDIQDGKILMALLEVLSGR-NLLHEYKSSSHRIFRLNNIAKALKFLEDSNVKLVSI 114
Cdd:smart00033   1 KTLLRWVNSLLAE-YDKPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79

                           90       100
                   ....*....|....*....|...
gi 2462541597  115 DAAEIADGNPsLVLGLIWNIILF 137
Cdd:smart00033  80 EPEDLVEGPK-LILGVIWTLISL 101

second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 186 QRKAIKALLAWVQRKTRKYGVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALENSTRENLEKAFSIAQDALHIPRLLE 265
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                          90       100
                  ....*....|....*....|....*.
gi 2462541597 266 PEDIMVDTPDEQSIMTYVAQFLERFP 291
Cdd:cd21245    81 PEDVMVDSPDEQSIMTYVAQFLEHFP 106

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597  29 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462541597 109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21241    81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597  22 RVQNLQVERENVQKRTFTRWINLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21193     5 RIRALQEERINIQKKTFTKWINSFLEKAN--LEIGDLFTDLSDGKLLLKLLEIISGEKLGKPNRGRL-RVQKIENVNKAL 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462541597 102 KFLEdSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21193    82 AFLK-TKVRLENIGAEDIVDGNPRLILGLIWTIIL 115

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597  32 NVQKRTFTRWINLHLEKCNPPLeVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSshRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21186     1 DVQKKTFTKWINSQLSKANKPP-IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRM--RVHHLNNVNRALQVLEQNNVKL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462541597 112 VSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21186    78 VNISSNDIVDGNPKLTLGLVWSIILHWQVK 107

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597  22 RVQNLQVERENVQKRTFTRWINLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21246     5 RIKALADEREAVQKKTFTKWVNSHLARVG--CRINDLYTDLRDGRMLIKLLEVLSGERLPKPTKGKM-RIHCLENVDKAL 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462541597 102 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21246    82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597  33 VQKRTFTRWINLHLEKCNPPleVKDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSNVKLV 112
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRE--RGRMRFHRLQNVQTALDFLKYRKIKLV 78

                          90       100
                  ....*....|....*....|....*..
gi 2462541597 113 SIDAAEIADGNPSLVLGLIWNIILFFQ 139
Cdd:cd21188    79 NIRAEDIVDGNPKLTLGLIWTIILHFQ 105

second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 187 RKAIKALLAWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALENSTRENLEKAFSIAQDALHIPRLLE 265
Cdd:cd21194     1 KSAKDALLLWCQRKTAGYpGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLD 80

                          90       100
                  ....*....|....*....|....*
gi 2462541597 266 PEDIMVDTPDEQSIMTYVAQFLERF 290
Cdd:cd21194    81 AEDVDVARPDEKSIMTYVASYYHYF 105

second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 189 AIKALLAWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALENSTRENLEKAFSIAQDALHIPRLLEPE 267
Cdd:cd21189     2 AKEALLLWARRTTEGYpGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDPE 81

                          90       100
                  ....*....|....*....|....
gi 2462541597 268 DIMVDTPDEQSIMTYVAQFLERFP 291
Cdd:cd21189    82 DVDVPEPDEKSIITYVSSLYDVFP 105

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597  29 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21236    13 ERDKVQKKTFTKWINQHLMKVRK--HVNDLYEDLRDGHNLISLLEVLSGDTLPRE--KGRMRFHRLQNVQIALDYLKRRQ 88

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462541597 109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKEL 143
Cdd:cd21236    89 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597  22 RVQNLQVERENVQKRTFTRWINLHLEKCnpPLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21318    27 RIKALADEREAVQKKTFTKWVNSHLARV--PCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRM-RIHSLENVDKAL 103

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462541597 102 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21318   104 QFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138

second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 181 ISVkDQRKAIKALLAWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALENSTRENLEKAFSIAQDALH 259
Cdd:cd21216     4 ISV-EELSAKEGLLLWCQRKTAPYkNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLD 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462541597 260 IPRLLEPEDIM-VDTPDEQSIMTYVAQFLERF 290
Cdd:cd21216    83 IPKMLDAEDIVnTPRPDERSVMTYVSCYYHAF 114

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597  22 RVQNLQVERENVQKRTFTRWINLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21317    20 RIKALADEREAVQKKTFTKWVNSHLARVT--CRIGDLYTDLRDGRMLIRLLEVLSGEQLPKPTKGRM-RIHCLENVDKAL 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462541597 102 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21317    97 QFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131

first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597  32 NVQKRTFTRWINLHLEKCNPPlEVKDLFVDIQDGKILMALLEVLSGRNLLHEYKSSshRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKP-PIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGST--RVHALNNVNRVLQVLHQNNVEL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462541597 112 VSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21232    78 VNIGGTDIVDGNHKLTLGLLWSIILHWQVK 107

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597  33 VQKRTFTRWINLHLEKCNPPLEvkDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLE-DSNVKL 111
Cdd:cd21311    15 IQQNTFTRWANEHLKTANKHIA--DLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFRSQKLENVSVALKFLEeDEGIKI 92

                          90       100
                  ....*....|....*....|....*....
gi 2462541597 112 VSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21311    93 VNIDSSDIVDGKLKLILGLIWTLILHYSI 121

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 184 KDQRKAIKALLAWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALENSTRENLEKAFSIAQDALHIPR 262
Cdd:cd21319     1 RETRSAKDALLLWCQMKTAGYpNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462541597 263 LLEPEDIMVDTPDEQSIMTYVAQFLERFPELE 294
Cdd:cd21319    81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKMK 112

second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 189 AIKALLAWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALENSTRENLEKAFSIAQDALHIPRLLEPE 267
Cdd:cd21291    11 AKEGLLLWCQRKTAGYdEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLDVE 90

                          90       100
                  ....*....|....*....|....
gi 2462541597 268 DIM-VDTPDEQSIMTYVAQFLERF 290
Cdd:cd21291    91 DVCdVAKPDERSIMTYVAYYFHAF 114

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 184 KDQRKAIKALLAWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALENSTRENLEKAFSIAQDALHIPR 262
Cdd:cd21321     1 KEKKSAKDALLLWCQMKTAGYpNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462541597 263 LLEPEDIMVDTPDEQSIMTYVAQFLERFPELEA 295
Cdd:cd21321    81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKA 113

calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 188 KAIKALLAWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALENSTRENLEKAFSIAQDALHIPRLLEP 266
Cdd:cd21253     1 AGIKALQQWCRQQTEGYrDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80

                          90       100
                  ....*....|....*....|....*.
gi 2462541597 267 EDiMVD--TPDEQSIMTYVAQFLERF 290
Cdd:cd21253    81 ED-MVAlkVPDKLSILTYVSQYYNYF 105

second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 189 AIKALLAWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALENSTRENLEKAFSIAQDaLHIPRLLEPE 267
Cdd:cd21239     2 AKERLLLWSQQMTEGYtGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDPE 80

                          90       100
                  ....*....|....*....|....
gi 2462541597 268 DIMVDTPDEQSIMTYVAQFLERFP 291
Cdd:cd21239    81 DVDVSSPDEKSVITYVSSLYDVFP 104

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 184 KDQRKAIKALLAWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALENSTRENLEKAFSIAQDALHIPR 262
Cdd:cd21322    13 RETRSAKDALLLWCQMKTAGYpEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLTK 92

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462541597 263 LLEPEDIMVDTPDEQSIMTYVAQFLERFPELEA 295
Cdd:cd21322    93 LLDPEDVNMEAPDEKSIITYVVSFYHYFSKMKA 125

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462541597 191 KALLAWVQRKTRKYG--VAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQ--ALENSTRENLEKAFSIAQDALHIPR-LLE 265
Cdd:pfam00307   5 KELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlnKSEFDKLENINLALDVAEKKLGVPKvLIE 84

                          90       100
                  ....*....|....*....|....*.
gi 2462541597 266 PEDImVDtPDEQSIMTYVAQFLERFP 291
Cdd:pfam00307  85 PEDL-VE-GDNKSVLTYLASLFRRFQ 108