first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. 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 22832611  91 KLQRILVDWINDELAEQRIIVQHLEEDMYDGQVLHKLWEKLTGKKLDVPEVTQSEQGQHEKLNIVLKAVNHTLGF-HQKI 169
Cdd:cd21304   1 ELIKVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEVAEVTQSEVGQKQKLRTVLDKINRILNLpRWSQ 80

                        90       100
                ....*....|....*....|....*..
gi 22832611 170 PKWSVASVHSKNIVAILHLLVALVRHF 196
Cdd:cd21304  81 QKWSVDSIHSKNLVAILHLLVALARHF 107

first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. 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 22832611  91 KLQRILVDWINDELAEQRIIVQHLEEDMYDGQVLHKLWEKLTGKKLDVPEVTQSEQGQHEKLNIVLKAVNHTLGF-HQKI 169
Cdd:cd21304   1 ELIKVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEVAEVTQSEVGQKQKLRTVLDKINRILNLpRWSQ 80

                        90       100
                ....*....|....*....|....*..
gi 22832611 170 PKWSVASVHSKNIVAILHLLVALVRHF 196
Cdd:cd21304  81 QKWSVDSIHSKNLVAILHLLVALARHF 107

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 22832611   257 AVVKKSLITFVNKHLAKL--NFEISDLNTDFRDGVYlcllmgllggffvpLHEF--HLTPQDVD---------QMVSNVA 323
Cdd:pfam00307   1 LELEKELLRWINSHLAEYgpGVRVTNFTTDLRDGLA--------------LCALlnKLAPGLVDkkklnksefDKLENIN 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 22832611   324 FAFDLMQ-DVGLPKPKARPEDIVNMDLKSTLRVLYSLFTMFR 364
Cdd:pfam00307  67 LALDVAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108

first calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. 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 22832611  91 KLQRILVDWINDELAEQRIIVQHLEEDMYDGQVLHKLWEKLTGKKLDVPEVTQSEQGQHEKLNIVLKAVNHTLGF-HQKI 169
Cdd:cd21304   1 ELIKVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEVAEVTQSEVGQKQKLRTVLDKINRILNLpRWSQ 80

                        90       100
                ....*....|....*....|....*..
gi 22832611 170 PKWSVASVHSKNIVAILHLLVALVRHF 196
Cdd:cd21304  81 QKWSVDSIHSKNLVAILHLLVALARHF 107

second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin 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 22832611 239 RCEKDAFDTLIDCAPDKLAVVKKSLITFVNKHLAKLNFEISDLNTDFRDGVYLCLLMGLLGGFFVPLHEFHLTPQDVDQM 318
Cdd:cd21337   1 RHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSFEQK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 22832611 319 VSNVAFAFDLMQDVGLPKPKARPEDIVNMDLKSTLRVLYSLFTMFRD 365
Cdd:cd21337  81 VLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYRN 127

first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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 22832611  91 KLQRILVDWINDELAEQRIIVQHLEEDMYDGQVLHKLWEKLTGKKLDVPEVTQSEQGQHEKLNIVLKAVNHTLGFHQKIP 170
Cdd:cd21221   1 ELVRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEVAQSEEGQKQKLAVVLACVNFLLGLEEDEA 80

                        90       100
                ....*....|....*....|....*.
gi 22832611 171 KWSVASVHSKNIVAILHLLVALVRHF 196
Cdd:cd21221  81 RWTVDGIYNKDLVSILHLLVALAHHY 106

first calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin 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 22832611  86 DPQVIKLQRILVDWINDELAEQRIIVQHLEEDMYDGQVLHKLWEKLTGKKLDVPEVTQSEQGQHEKLNIVLKAVNHTLGF 165
Cdd:cd21335   1 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLEKINETLKL 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 22832611 166 HQKIPKWSVASVHSKNIVAILHLLVALVRHFRAPV 200
Cdd:cd21335  81 PPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPI 115

first calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. It 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 22832611  91 KLQRILVDWINDELAEQRIIVQHLEEDMYDGQVLHKLWEKLTGKKLDVPEVTQSEQGQHEKLNIVLKAVNHTLGFHQKIP 170
Cdd:cd21305   1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLLVKLAGVKLEVEEIALTENAQKRKLTVILEAVNQSLQLEESQL 80

                        90       100
                ....*....|....*....|....*.
gi 22832611 171 KWSVASVHSKNIVAILHLLVALVRHF 196
Cdd:cd21305  81 KWSVELIHNKDLLATLHLLVAIAKHF 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 22832611   257 AVVKKSLITFVNKHLAKL--NFEISDLNTDFRDGVYlcllmgllggffvpLHEF--HLTPQDVD---------QMVSNVA 323
Cdd:pfam00307   1 LELEKELLRWINSHLAEYgpGVRVTNFTTDLRDGLA--------------LCALlnKLAPGLVDkkklnksefDKLENIN 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 22832611   324 FAFDLMQ-DVGLPKPKARPEDIVNMDLKSTLRVLYSLFTMFR 364
Cdd:pfam00307  67 LALDVAEkKLGVPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108

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 22832611 257 AVVKKSLITFVNKHLAKLNFEISDLNTDFRDGVYLCLLMGLLGGFFVP----LHEFHltpqdvdqMVSNVAFAFDLMQDV 332
Cdd:cd21188   2 AVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPrergRMRFH--------RLQNVQTALDFLKYR 73

                        90       100       110
                ....*....|....*....|....*....|..
gi 22832611 333 GLPKPKARPEDIVNMDLKSTLRVLYSLFTMFR 364
Cdd:cd21188  74 KIKLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105

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 22832611 257 AVVKKSLITFVNKHLAKLNFEISDLNTDFRDGVYLCLLMGLLGGffVPLHEFHLTPQDVDQMVSNVAFAFDLMQDVGLPK 336
Cdd:cd21215   3 DVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGD--ESLGRYNKNPKMRVQKLENVNKALEFIKSRGVKL 80

                        90       100
                ....*....|....*....|....*..
gi 22832611 337 PKARPEDIVNMDLKSTLRVLYSLFTMF 363
Cdd:cd21215  81 TNIGAEDIVDGNLKLILGLLWTLILRF 107

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22832611 264 ITFVNKHLAKL--NFEISDLNTDFRDGVYLCLLMGLLGGFFVPlhEFHLTPQDVDQMVSNVAFAFDLMQDVGLPKPKARP 341
Cdd:cd21213   6 VAWVNSQLKKRpgIRPVQDLRRDLRDGVALAQLIEILAGEKLP--GIDWNPTTDAERKENVEKVLQFMASKRIRMHQTSA 83

                        90
                ....*....|....*...
gi 22832611 342 EDIVNMDLKSTLRVLYSL 359
Cdd:cd21213  84 KDIVDGNLKAIMRLILAL 101

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22832611  93 QRILVDWINDELAEQRII-VQHLEEDMYDGQVLHKLWEKLTGKKLDVPEVTQSEQGQH-EKLNIVLKAVnHTLGFHqKIP 170
Cdd:cd00014   1 EEELLKWINEVLGEELPVsITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKrENINLFLNAC-KKLGLP-ELD 78

                        90       100
                ....*....|....*....|....*
gi 22832611 171 KWSVASVHS-KNIVAILHLLVALVR 194
Cdd:cd00014  79 LFEPEDLYEkGNLKKVLGTLWALAL 103

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
                ....*....|....*....|....*....|....*....|....*...
gi 22832611 241 EKDAFDTLIDcapDKLAVVKKSLITFVNKHLAKLNFEISDLNTDFRDG 288
Cdd:cd21317  17 ERSRIKALAD---EREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDG 61

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 22832611  88 QVIKLQRILVDWINDELAE--QRIIVQHLEEDMYDGQVLHKLWEKLTGKKLDVpevtqsEQGQHEKLNIVLKAVNHTLGF 165
Cdd:cd21190   2 QERVQKKTFTNWINSHLAKlsQPIVINDLFVDIKDGTALLRLLEVLSGQKLPI------ESGRVLQRAHKLSNIRNALDF 75

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 22832611 166 HQKiPKWSVASVHSKNIV-----AILHLLVALVRHFR 197
Cdd:cd21190  76 LTK-RCIKLVNINSTDIVdgkpsIVLGLIWTIILYFQ 111

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
                ....*....|....*....|....*....|....*....|.
gi 22832611  99 WINDELAEQRIIVQHLEEDMYDGQVLHKLWEKLTGKKLDVP 139
Cdd:cd21246  24 WVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKP 64

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 22832611  99 WINDELAEQRIIVQHLEEDMYDGQVLHKLWEKLTGKKLDVPevtqseqgQHEKLNI-VLKAVNHTLGF-HQKIPkwsVAS 176
Cdd:cd21193  24 WINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKP--------NRGRLRVqKIENVNKALAFlKTKVR---LEN 92

                ....*..
gi 22832611 177 VHSKNIV 183
Cdd:cd21193  93 IGAEDIV 99

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
                ....*....|....*....|....*....|....*....
gi 22832611  99 WINDELA-EQRIIVQHLEEDMYDGQVLHKLWEKLTGKKL 136
Cdd:cd21186  10 WINSQLSkANKPPIKDLFEDLRDGTRLLALLEVLTGKKL 48

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22832611  93 QRILVDWINDELAEQR--IIVQHLEEDMYDGQVLHKLWEKLTGKKLdvpevtQSEQGQHEKLNIVLKAVNHTLGF 165
Cdd:cd21241   7 KKTFTNWINSYLAKRKppMKVEDLFEDIKDGTKLLALLEVLSGEKL------PCEKGRRLKRVHFLSNINTALKF 75