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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2517823329   1 LINKLQPGSVPKVNEPAQNWHKLENIGNFLR-AITRYGVKPHDIfEANDLFENtNHTQVQSTLIALAS 67
Cdd:pfam00307  40 LLNKLAPGLVDKKKLNKSEFDKLENINLALDvAEKKLGVPKVLI-EPEDLVEG-DNKSVLTYLASLFR 105

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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2517823329    1 LINKLQPGSVPKVNEPAQN--WHKLENIGNFLRAITRYGVKPhDIFEANDLFENTNHT-QVQSTLIAL 65
Cdd:smart00033  35 LLNSLSPGLVDKKKVAASLsrFKKIENINLALSFAEKLGGKV-VLFEPEDLVEGPKLIlGVIWTLISL 101

calponin homology (CH) domain found in the calponin family; Calponin is an actin filament-associated regulatory protein expressed in smooth muscle and many types of non-muscle cells. There are three calponin isoforms, calponin-1, -2, -3. All of them are actin-binding proteins with functions in inhibiting actin-activated myosin ATPase and stabilizing the actin cytoskeleton. Calponin-1 is specifically expressed in smooth muscle cells and plays a role in fine-tuning smooth muscle contractility. Calponin-2 is expressed in both smooth muscle and non-muscle cells and regulates multiple actin cytoskeleton-based functions. Calponin-3 is expressed in the brain and participates in actin cytoskeleton-based activities in embryonic development and myogenesis. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2517823329   1 LINKLQPGSVPKVNEPAQNWHKLENIGNFLRAITRYGVKPHDIFEANDLFENTNHTQVQSTLIALASQAKTK 72
Cdd:cd21211    37 LINKLQPGSVKKINESMQNWHQLENIGNFIKAIVSYGMKPHDIFEANDLFENGNMTQVQVTLLALAGKAKTK 108

calponin homology (CH) domain found in calponin-2; Calponin-2 (CNN2), also called neutral calponin, or smooth muscle calponin H2, is an actin cytoskeleton-associated regulatory protein that inhibits the activity of myosin-ATPase and cytoskeleton dynamics. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2517823329   1 LINKLQPGSVPKVNEPAQNWHKLENIGNFLRAITRYGVKPHDIFEANDLFENTNHTQVQSTLIALASQAKTKG 73
Cdd:cd21283    37 LMNKLQPGSVPKINRSMQNWHQLENLSNFIKAMVSYGMKPVDLFEANDLFESGNMTQVQVSLLALAGMAKTKG 109

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2517823329   1 LINKLQPGSVPKVNEPAQN-WHKLENIGNFLRAITRYGVKPHDIFEANDLFENTNHTQVQSTLIALAS 67
Cdd:cd00014    36 LINKLSPGSIPKINKKPKSpFKKRENINLFLNACKKLGLPELDLFEPEDLYEKGNLKKVLGTLWALAL 103

calponin homology (CH) domain found in Saccharomyces cerevisiae transgelin (SCP1) and similar proteins; The family includes transgelins from Saccharomyces cerevisiae and Schizosaccharomyces pombe, which are also called SCP1 and STG1, respectively. Transgelin, also called calponin homolog 1, has actin-binding and actin-bundling activity. It stabilizes actin filaments against disassembly. Transgelin contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2517823329   1 LINKLQPGSVPKVNEPAQNWHKLENIGNFLRAITRYGVKPHDIFEANDLFENTNHTQVQSTLIALA 66
Cdd:cd21210    35 LANRILPADIRKYKESKMPFVQMENISAFLNAARKLGVPENDLFQTVDLFERKNPAQVLQCLHALS 100

calponin homology (CH) domain found in transgelin-2; Transgelin-2, also called epididymis tissue protein Li 7e, or SM22-alpha homolog, acts as an actin-binding protein that induces actin gelation and regulates the actin cytoskeleton. It may participate in the development and progression of multiple cancers. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2517823329   1 LINKLQPGS---VPKVNEPAQNWHKLENIGNFLRAITRYGVKPHDIFEANDLFENTNHTQVQSTLIALASQAKTKGNNVG 77
Cdd:cd21280    48 LINSLYPKGqapVKKIQASTMAFKQMEQISQFLQAAERYGINTTDIFQTVDLWEGKNMASVQRTLMNLGGLAVTRDDGLF 127

                  ..
gi 2517823329  78 LG 79
Cdd:cd21280   128 VG 129

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2517823329   1 LINKLQPGSVPKVNEPAQNWHKLENIGNFLR-AITRYGVKPHDIfEANDLFENtNHTQVQSTLIALAS 67
Cdd:pfam00307  40 LLNKLAPGLVDKKKLNKSEFDKLENINLALDvAEKKLGVPKVLI-EPEDLVEG-DNKSVLTYLASLFR 105

calponin homology (CH) domain found in the Pak Interactive eXchange factor family; Pak Interactive eXchange factor (PIX) proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX family, alpha-PIX and beta-PIX. Alpha-PIX, also called Rho guanine nucleotide exchange factor 6 (ARHGEF6), is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX, also called Rho guanine nucleotide exchange factor 7 (ARHGEF7), plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. Both alpha-PIX and beta-PIX 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2517823329   1 LINKLQPGSVPKV-NEPAQNWHKLENIGNFLRAITRYGVKPHDIFEANDLFENTNHTQVQSTLIAL 65
Cdd:cd21202    43 LVNRLKPGTVEKIyDEPTTEEECLYNFESFLKACQELGILAEEIFDPNDLYSGGNFQKVLSTLERL 108

calponin homology (CH) domain found in alpha-Pak Interactive eXchange factor; Alpha-Pak Interactive eXchange factor (alpha-PIX), also called PAK-interacting exchange factor alpha, Rho guanine nucleotide exchange factor 6 (ARHGEF6), Rac/Cdc42 guanine nucleotide exchange factor 6, or Cool (Cloned out of Library)-2, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac1, and is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Alpha-PIX contains a single copy of the CH domain at its N-terminus. CH domains are actin filament (F-actin) binding motifs.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2517823329   1 LINKLQPGSVPKV-NEPAQNWHKLENIGNFLRAITRYGVkphDIFEANDLFENTNHTQVQSTLIAL 65
Cdd:cd21265    44 LIERLLPGSVEKYcLEPKTEADCIGNIKEFLKGCAALKV---ETFEPDDLYTGENFSKVLSTLLAV 106

calponin homology (CH) domain found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV proteins.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2517823329   1 LINKLQPGSVPKV----NEPAQNWHKLENIGNFLRAI-TRYGVKPHDIFEANDLFENTNHTQVQSTL 62
Cdd:cd21201    45 LLNRLSPGSVDDReinlRPQMSQFLCLKNIRTFLQACrTVFGLRSADLFEPEDLYDVTNFGKVIRTL 111

calponin homology (CH) domain found in LIM domain only protein 7 and similar proteins; This family includes LIM domain only protein 7 (LMO-7) and LIM and calponin homology domains-containing protein 1 (LIMCH1), and similar proteins. LMO-7, also called F-box only protein 20, or LOMP, is a transcription regulator for expression of many Emery-Dreifuss muscular dystrophy (EDMD)-relevant genes. It binds to alpha-actinin and AF6/afadin at adherens junctions for epithelial cell-cell adhesion. LIMCH1 acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. 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
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2517823329   1 LINKLQPGSVPKVNEPAQNWHKLENIGNFLRAITRYGVKPHDIFEANDLFENTN 54
Cdd:cd21208    35 LINAIKPGSIKKINRLPTPIAGLDNLNLFLKACEDLGLKDSQLFDPTDLQDLSN 88

calponin homology (CH) domain found in LIM and calponin homology domains-containing protein 1; LIM and calponin homology domains-containing protein 1 (LIMCH1) acts as an actin stress fiber-associated protein that activates the non-muscle myosin IIa complex by promoting the phosphorylation of its regulatory subunit MRLC/MYL9. It positively regulates actin stress fiber assembly and stabilizes focal adhesions, and therefore negatively regulates cell spreading and cell migration. LIMCH1 contains 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2517823329   1 LINKLQPGSVPKVNEPAQNWHKLENIGNFLRAITRYGVKPHDIFEANDLFENTNHTQVQST 61
Cdd:cd21278    35 LLNAIKPGLVKKINRLPTPIAGLDNITLFLRGCKELGLKESQLFDPGDLQDTSNRVTIKSS 95

Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2517823329    1 LINKLQPGSVPKV--NEPAQNWHKlENIGNFLRAITRYGVKPHDIFEANDLFENTNHTQVQSTLIALASQAKTKG 73
Cdd:COG5261     79 LTQRFNPDLTTVIfpADKLQFRHT-DNINAFLDLIEHVGLPESFHFELQDLYEKKNIPKVIYCIHALISMLSWPG 152

calponin homology (CH) domain found in VAV1 protein; VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. This model corresponds to the CH domain, an actin-binding domain which is present as a single copy in VAV1 protein.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2517823329   1 LINKLQPGSV--PKVNEPAQ--NWHKLENIGNFLRAIT-RYGVKPHDIFEANDLFENTNHTQVQSTLIALA 66
Cdd:cd21262    45 LLNNLLPHAVnlREINLRPQmsQFLCLKNIRTFLSTCCeKFGLRKSELFEAFDLFDVRDFGKVIDTLSILS 115

calponin homology (CH) domain found in VAV3 protein and similar proteins; VAV3 is ubiquitously expressed and functions as a phosphorylation-dependent guanine nucleotide exchange factor (GEF) for RhoA, RhoG, and Rac1. Its function has been implicated in the hematopoietic, bone, cerebellar, and cardiovascular systems. VAV3 is essential in axon guidance in neurons that control blood pressure and respiration. It is overexpressed in prostate cancer cells and it plays a role in regulating androgen receptor transcriptional activity. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The model corresponds to CH domain, an actin-binding domain which is present as a single copy in VAV3 protein.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2517823329   1 LINKLQPGSV--PKVNEPAQ--NWHKLENIGNFLRAITR-YGVKPHDIFEANDLFENTNHTQVQSTLIALA 66
Cdd:cd21264    45 LLNNLRPHSInlKEINLRPQmsQFLCLKNIRTFLSACCEtFGMRKSELFEAFDLFDVRDFGKVIETLSKLS 115