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 1020405720 130 DRKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLERINDALKV 209
Cdd:cd21335     1 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLEKINETLKL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1020405720 210 STRSIKWNVDSVHAKSIVAILHLLVALSQHFRAPI 244
Cdd:cd21335    81 PPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPI 115

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 1020405720 130 DRKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLERINDALKV 209
Cdd:cd21335     1 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLEKINETLKL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1020405720 210 STRSIKWNVDSVHAKSIVAILHLLVALSQHFRAPI 244
Cdd:cd21335    81 PPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPI 115

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 1020405720 301 NVVKKTLITFVNKHLNKL--NLEVAELDTQFADGVYLVLLMGLLEGYFVPLYNffLTPENFDQkVHNVSFSFELMQDG-G 377
Cdd:pfam00307   1 LELEKELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK--LNKSEFDK-LENINLALDVAEKKlG 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1020405720 378 LERPKPRPEDIVNCDLKSTLRVLYNLFTRYR 408
Cdd:pfam00307  78 VPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020405720 287 DAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVAELDTQFADGVYLVLLMGLLEGYFVPLYNFFLTPENFDQKVHNV 366
Cdd:cd21306     1 DAFDTLFDHAPDKLNVVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPTSFEQKVHNV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1020405720 367 SFSFELMQDGGLERPKPRPEDIVNCDLKSTLRVLYNLFTRY 407
Cdd:cd21306    81 QFAFELMQDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121

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 1020405720 130 DRKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLERINDALKV 209
Cdd:cd21335     1 DPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLEKINETLKL 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1020405720 210 STRSIKWNVDSVHAKSIVAILHLLVALSQHFRAPI 244
Cdd:cd21335    81 PPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPI 115

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 1020405720 135 ELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLERINDALKVS-TRS 213
Cdd:cd21304     1 ELIKVLIEWINDELAEQRIIVKDIEEDLYDGQVLQKLLEKLTGVKLEVAEVTQSEVGQKQKLRTVLDKINRILNLPrWSQ 80

                          90       100
                  ....*....|....*....|....*..
gi 1020405720 214 IKWNVDSVHAKSIVAILHLLVALSQHF 240
Cdd:cd21304    81 QKWSVDSIHSKNLVAILHLLVALARHF 107

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020405720 287 DAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVAELDTQFADGVYLVLLMGLLEGYFVPLYNFFLTPENFDQKVHNV 366
Cdd:cd21307     1 DAIDELFKLGPDKVNTVKKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHLSEFFLTPSSTSEMLHNV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1020405720 367 SFSFELMQDGGLERPKPRPEDIVNCDLKSTLRVLYNLFTRYR 408
Cdd:cd21307    81 TLALELLKEGGLLNFPVNPEDIVNGDSKATIRVLYCLFSKYK 122

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 1020405720 135 ELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKLNVAEVTQSEIAQKQKLQTVLERINDALKVSTRSI 214
Cdd:cd21305     1 ELKEVLIDWINTTLKQEHIVVKSLEEDLYDGLVLHHLLVKLAGVKLEVEEIALTENAQKRKLTVILEAVNQSLQLEESQL 80

                          90       100
                  ....*....|....*....|....*.
gi 1020405720 215 KWNVDSVHAKSIVAILHLLVALSQHF 240
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 1020405720 301 NVVKKTLITFVNKHLNKL--NLEVAELDTQFADGVYLVLLMGLLEGYFVPLYNffLTPENFDQkVHNVSFSFELMQDG-G 377
Cdd:pfam00307   1 LELEKELLRWINSHLAEYgpGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKK--LNKSEFDK-LENINLALDVAEKKlG 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1020405720 378 LERPKPRPEDIVNCDLKSTLRVLYNLFTRYR 408
Cdd:pfam00307  78 VPKVLIEPEDLVEGDNKSVLTYLASLFRRFQ 108

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 1020405720 285 ERDafdtLFDHAPDKLnVVKKTLITFVNKHLNKLNLEVAELDTQFADGVYLVLLMGLLEGYFVPLYNffLTPENFDQKVH 364
Cdd:cd21311     3 ERD----LAEDAQWKR-IQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFN--KRPTFRSQKLE 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1020405720 365 NVSFSFELMQ-DGGLERPKPRPEDIVNCDLKSTLRVLYNLFTRY 407
Cdd:cd21311    76 NVSVALKFLEeDEGIKIVNIDSSDIVDGKLKLILGLIWTLILHY 119

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 1020405720 304 KKTLITFVNKHLNKLNLEVAELDTQFADGVYLVLLMGLLEGYFVPLynffltPENFDQKVH---NVSFSFELMQDGGLER 380
Cdd:cd21214     7 RKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPK------PERGKMRFHkiaNVNKALDFIASKGVKL 80

                          90
                  ....*....|....*..
gi 1020405720 381 PKPRPEDIVNCDLKSTL 397
Cdd:cd21214    81 VSIGAEEIVDGNLKMTL 97

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020405720 142 DWINDVLV--GERIIVKDLAEDLYDGQVLQKLFEKLEGEKlnVAEVTQSEIAQKQKlqtvLERINDALKVsTRSIKWNVD 219
Cdd:cd21212     7 DWANHYLEkgGHKRIITDLQKDLGDGLTLVNLIEAVAGEK--VPGIHSRPKTRAQK----LENIQACLQF-LAALGVDVQ 79

                          90       100
                  ....*....|....*....|....*.
gi 1020405720 220 SVHAKSIV-----AILHLLVALSQHF 240
Cdd:cd21212    80 GITAEDIVdgnlkAILGLFFSLSRYK 105

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 1020405720 302 VVKKTLITFVNKHLNKLNLEVAELDTQFADGVYLVLLMGLLEGYFVPLYNFFLtpeNFdQKVHNVSFSFELMQDGGLERP 381
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRM---RF-HRLQNVQTALDFLKYRKIKLV 78

                          90
                  ....*....|....*.
gi 1020405720 382 KPRPEDIVNCDLKSTL 397
Cdd:cd21188    79 NIRAEDIVDGNPKLTL 94

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 1020405720 304 KKTLITFVNKHLNKLNLEVAELDTQFADGVYLVLLMGLLEGYFV-PLYNffLTPENFDQKVHNVSFSFELMQDGGLERPK 382
Cdd:cd21183     6 ANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLkRSYN--RRPAFQQHYLENVSTALKFIEADHIKLVN 83

                          90       100
                  ....*....|....*....|....*
gi 1020405720 383 PRPEDIVNCDLKSTLRVLYNLFTRY 407
Cdd:cd21183    84 IGSGDIVNGNIKLILGLIWTLILHY 108

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 1020405720 296 APDKLNVVKKTLITFVNKHLNKLNLEVAELDTQFADGVYLVLLMGLLEGYFVPlynfflTPENFDQKVH---NVSFSFEL 372
Cdd:cd21318    32 ADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLP------KPTRGRMRIHsleNVDKALQF 105

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1020405720 373 MQDGGLERPKPRPEDIVNCDLKSTLRVLYNLFTR 406
Cdd:cd21318   106 LKEQRVHLENVGSHDIVDGNHRLTLGLIWTIILR 139

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 1020405720 304 KKTLITFVNKHLNKLNLEVAELDTQFADGVYLVLLMGLLEGYFVPlYNFFLTPENFDQKVHNVSFSFELMQDGGLERPKP 383
Cdd:cd21228     6 QNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMY-KKYNKRPTFRQMKLENVSVALEFLERESIKLVSI 84

                          90       100
                  ....*....|....*....|....
gi 1020405720 384 RPEDIVNCDLKSTLRVLYNLFTRY 407
Cdd:cd21228    85 DSSAIVDGNLKLILGLIWTLILHY 108

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
                  ....*....|....*....|....*....|....*....|....*.
gi 1020405720 298 DKLNVVKKTLITFVNKHLNKLNLEVAELDTQFADGvylVLLMGLLE 343
Cdd:cd21193    12 ERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDG---KLLLKLLE 54

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 1020405720 141 IDWINDVL---VGERIIVkDLAEDLYDGQVLQKLFEKLEGEKLN-VAEVTQSEIAQKQKLQTVLERindalkVSTRSIKw 216
Cdd:cd21213     6 VAWVNSQLkkrPGIRPVQ-DLRRDLRDGVALAQLIEILAGEKLPgIDWNPTTDAERKENVEKVLQF------MASKRIR- 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1020405720 217 nVDSVHAKSIV-----AILHLLVALSQHFR 241
Cdd:cd21213    78 -MHQTSAKDIVdgnlkAIMRLILALAAHFK 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 1020405720 138 KVLIDWINDVLVGER--IIVKDLAEDLYDGQVLQKLFEKLEGEKLnvaevtqsEIAQKQKLQTV--LERINDALK-VSTR 212
Cdd:cd21241     8 KTFTNWINSYLAKRKppMKVEDLFEDIKDGTKLLALLEVLSGEKL--------PCEKGRRLKRVhfLSNINTALKfLESK 79

                  ...
gi 1020405720 213 SIK 215
Cdd:cd21241    80 KIK 82

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and 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 1020405720 302 VVKKTLITFVNKHLNKLNLE-VAELDTQFADGVYLVLLMGLLEGYFVPlYNFFLTPENFDQKVHNVSFSFELMQDGGLER 380
Cdd:cd21225     4 VQIKAFTAWVNSVLEKRGIPkISDLATDLSDGVRLIFFLELVSGKKFP-KKFDLEPKNRIQMIQNLHLAMLFIEEDLKIR 82

                          90       100
                  ....*....|....*....|....*....
gi 1020405720 381 -PKPRPEDIVNCDLKSTLRVLYNLFTRYR 408
Cdd:cd21225    83 vQGIGAEDFVDNNKKLILGLLWTLYRKYR 111

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (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. FLN-C 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 1020405720 292 LFDHAPDKlNVVKKTLITFVNKHLNKLNLEVAELDTQFADGVYLVLLMGLLEGYfvPLYNFFLTPENFDQ-KVHNVSFSF 370
Cdd:cd21310     7 LAEDAPWK-KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQK--KMYRKYHPRPNFRQmKLENVSVAL 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1020405720 371 ELMQDGGLERPKPRPEDIVNCDLKSTLRVLYNLFTRY 407
Cdd:cd21310    84 EFLDREHIKLVSIDSKAIVDGNLKLILGLIWTLILHY 120

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
                  ....*....|....*....|....*....|....*....|....*
gi 1020405720 138 KVLIDWINDVLV-GERIIVKDLAEDLYDGQVLQKLFEKLEGEKLN 181
Cdd:cd21186     5 KTFTKWINSQLSkANKPPIKDLFEDLRDGTRLLALLEVLTGKKLK 49

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
                  ....*....|....*....|....*....|....*....|...
gi 1020405720 138 KVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLEGEKL 180
Cdd:cd21214     8 KTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERL 50