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 100816903  186 QRKAIKTLLSWVQRKTRKYGVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLE 265
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                          90       100
                  ....*....|....*....|....*.
gi 100816903  266 PEDIMVDMPDEQSIVTYVAQFLERFP 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 100816903  186 QRKAIKTLLSWVQRKTRKYGVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLE 265
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                          90       100
                  ....*....|....*....|....*.
gi 100816903  266 PEDIMVDMPDEQSIVTYVAQFLERFP 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 100816903    32 NVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGrNLLHEYKSSSHRIFRLNNIAKALKFLEDS-NVK 110
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAP-GLVDKKKLNKSEFDKLENINLALDVAEKKlGVP 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 100816903   111 LVSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:pfam00307   80 KVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109

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 100816903     36 RTFTRWINLHLEKcDPPLEVTDLFVDIQDGKILMALLEVLSGR-NLLHEYKSSSHRIFRLNNIAKALKFLEDSNVKLVSI 114
Cdd:smart00033    1 KTLLRWVNSLLAE-YDKPPVTNFSSDLKDGVALCALLNSLSPGlVDKKKVAASLSRFKKIENINLALSFAEKLGGKVVLF 79

                            90       100
                    ....*....|....*....|...
gi 100816903    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 100816903  186 QRKAIKTLLSWVQRKTRKYGVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLE 265
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKYGVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLE 80

                          90       100
                  ....*....|....*....|....*.
gi 100816903  266 PEDIMVDMPDEQSIVTYVAQFLERFP 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 100816903   29 ERENVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLKRVHFLSNINTALKFLESKK 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 100816903  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21241    81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. 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) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. 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. 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 100816903   29 ERENVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVLQRAHKLSNIRNALDFLTKRC 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 100816903  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21190    81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113

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 100816903   32 NVQKRTFTRWINLHLEKCDPPLeVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSshRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21186     1 DVQKKTFTKWINSQLSKANKPP-IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRM--RVHHLNNVNRALQVLEQNNVKL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 100816903  112 VSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21186    78 VNISSNDIVDGNPKLTLGLVWSIILHWQVK 107

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 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-2 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 100816903  189 AIKTLLSWVQRKTRKYG-VAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPE 267
Cdd:cd21244     6 ARKALLLWAQEQCAKVGsISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEPE 85

                          90       100
                  ....*....|....*....|.
gi 100816903  268 DIMVDMPDEQSIVTYVAQFLE 288
Cdd:cd21244    86 DVDVVNPDEKSIMTYVAQFLQ 106

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 100816903   33 VQKRTFTRWINLHLEKCDPPleVTDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSNVKLV 112
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRE--RGRMRFHRLQNVQTALDFLKYRKIKLV 78

                          90       100
                  ....*....|....*....|....*..
gi 100816903  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 100816903  187 RKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLE 265
Cdd:cd21194     1 KSAKDALLLWCQRKTAGYpGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLD 80

                          90       100
                  ....*....|....*....|....*
gi 100816903  266 PEDIMVDMPDEQSIVTYVAQFLERF 290
Cdd:cd21194    81 AEDVDVARPDEKSIMTYVASYYHYF 105

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816903   31 ENVQKRTFTRWINLHLEKCDPPLEvtDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKALKFLEDSNVK 110
Cdd:cd21214     3 EKQQRKTFTAWCNSHLRKAGTQIE--NIEEDFRDGLKLMLLLEVISGERLPKPERGKM-RFHKIANVNKALDFIASKGVK 79

                          90       100
                  ....*....|....*....|....*.
gi 100816903  111 LVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21214    80 LVSIGAEEIVDGNLKMTLGMIWTIIL 105

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 100816903   22 RVQNLQVERENVQKRTFTRWINLHLEKCdpPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSShRIFRLNNIAKAL 101
Cdd:cd21318    27 RIKALADEREAVQKKTFTKWVNSHLARV--PCRINDLYTDLRDGYVLTRLLEVLSGEQLPKPTRGRM-RIHSLENVDKAL 103

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 100816903  102 KFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIIL 136
Cdd:cd21318   104 QFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138

first calponin homology (CH) domain found in plectin and similar proteins; 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 can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin 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 100816903   29 ERENVQKRTFTRWINLHLEKCDPplEVTDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21235     2 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 100816903  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKEL 143
Cdd:cd21235    78 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDI 112

first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816903   31 ENVQKRTFTRWINLHLEKCDppLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSNVK 110
Cdd:cd21215     2 VDVQKKTFTKWLNTKLSSRG--LSITDLVTDLSDGVRLIQLLEIIGDESLGRYNKNPKMRVQKLENVNKALEFIKSRGVK 79

                          90       100
                  ....*....|....*....|....*...
gi 100816903  111 LVSIDAAEIADGNPSLVLGLIWNIILFF 138
Cdd:cd21215    80 LTNIGAEDIVDGNLKLILGLLWTLILRF 107

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The 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 100816903   33 VQKRTFTRWINLHLEKCDppLEVTDLFVDIQDGKILMALLEVLSGRNLLHEY-KSSSHRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21228     4 IQQNTFTRWCNEHLKCVN--KRIYNLETDLSDGLRLIALLEVLSQKRMYKKYnKRPTFRQMKLENVSVALEFLERESIKL 81

                          90       100
                  ....*....|....*....|....*..
gi 100816903  112 VSIDAAEIADGNPSLVLGLIWNIILFF 138
Cdd:cd21228    82 VSIDSSAIVDGNLKLILGLIWTLILHY 108

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 100816903   32 NVQKRTFTRWINLHLEKCDPPlEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSshRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKP-PIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGST--RVHALNNVNRVLQVLHQNNVEL 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 100816903  112 VSIDAAEIADGNPSLVLGLIWNIILFFQIK 141
Cdd:cd21232    78 VNIGGTDIVDGNHKLTLGLLWSIILHWQVK 107

second 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 link 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 100816903  191 KTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDI 269
Cdd:cd21187     3 KTLLAWCRQSTRGYeQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDV 82

                          90       100
                  ....*....|....*....|..
gi 100816903  270 MVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21187    83 NVEQPDKKSILMYVTSLFQVLP 104

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; 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. MACF1 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 100816903   29 ERENVQKRTFTRWINLHLEKCDPplEVTDLFVDIQDGKILMALLEVLSGRNLLHEykSSSHRIFRLNNIAKALKFLEDSN 108
Cdd:cd21237     2 ERDRVQKKTFTKWVNKHLMKVRK--HINDLYEDLRDGHNLISLLEVLSGVKLPRE--KGRMRFHRLQNVQIALDFLKQRQ 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 100816903  109 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKEL 143
Cdd:cd21237    78 VKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 112

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other 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 100816903   33 VQKRTFTRWINLHLEKCDppLEVTDLFVDIQDGKILMALLEVLSGRNLLHEY-KSSSHRIFRLNNIAKALKFLEDSNVKL 111
Cdd:cd21183     4 IQANTFTRWCNEHLKERG--MQIHDLATDFSDGLCLIALLENLSTRPLKRSYnRRPAFQQHYLENVSTALKFIEADHIKL 81

                          90       100
                  ....*....|....*....|....*..
gi 100816903  112 VSIDAAEIADGNPSLVLGLIWNIILFF 138
Cdd:cd21183    82 VNIGSGDIVNGNIKLILGLIWTLILHY 108

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 100816903  184 KDQRKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPR 262
Cdd:cd21319     1 RETRSAKDALLLWCQMKTAGYpNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 100816903  263 LLEPEDIMVDMPDEQSIVTYVAQFLERFPELE 294
Cdd:cd21319    81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKMK 112

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) 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. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 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 100816903   16 GQISDIRVQNLQVERENVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLlheyKSSSHRIFR-- 93
Cdd:cd21247     3 TEYEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQL----PRPSRGKMRvh 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 100816903   94 -LNNIAKALKFLEdSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQI 140
Cdd:cd21247    79 fLENNSKAITFLK-TKVPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125

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 100816903  184 KDQRKAIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPR 262
Cdd:cd21321     1 KEKKSAKDALLLWCQMKTAGYpNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 100816903  263 LLEPEDIMVDMPDEQSIVTYVAQFLERFPELE 294
Cdd:cd21321    81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMK 112

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 100816903  189 AIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAhDSLHIPRLLEPE 267
Cdd:cd21239     2 AKERLLLWSQQMTEGYtGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVA-EKLGVTRLLDPE 80

                          90       100
                  ....*....|....*....|....
gi 100816903  268 DIMVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21239    81 DVDVSSPDEKSVITYVSSLYDVFP 104

second calponin homology (CH) domain found in plectin and similar proteins; 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 can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin 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 100816903  189 AIKTLLSWVQRKTRKY-GVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPE 267
Cdd:cd21238     3 AKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 82

                          90       100
                  ....*....|....*....|....
gi 100816903  268 DIMVDMPDEQSIVTYVAQFLERFP 291
Cdd:cd21238    83 DVDVPQPDEKSIITYVSSLYDAMP 106