calponin homology (CH) domain found in transgelin-3; Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. 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 78214339  23 DADLENKLVDWIILQCAEDIEHPPPGRTHFQKWLMDGTVLCKLINSLYPPGQEPIPKISESKMAFKQMEQISQFLKAAEV 102
Cdd:cd21281   1 DPDLESRLVDWIIIQCGGDIERPQPGRQNFQKWLMDGTILCRLINSLYPPGKEPIKKISETKMAFKQMEKISQFLQAAEA 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 78214339 103 YGVRTTDIFQTVDLWEGKDMAAVQRTLMALGSVAVTKDD 141
Cdd:cd21281  81 YGVITTDIFQTVDLWEGKDMAAVQRTLMALGSVAVTKDD 119

calponin homology (CH) domain found in transgelin-3; Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. 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 78214339  23 DADLENKLVDWIILQCAEDIEHPPPGRTHFQKWLMDGTVLCKLINSLYPPGQEPIPKISESKMAFKQMEQISQFLKAAEV 102
Cdd:cd21281   1 DPDLESRLVDWIIIQCGGDIERPQPGRQNFQKWLMDGTILCRLINSLYPPGKEPIKKISETKMAFKQMEKISQFLQAAEA 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 78214339 103 YGVRTTDIFQTVDLWEGKDMAAVQRTLMALGSVAVTKDD 141
Cdd:cd21281  81 YGVITTDIFQTVDLWEGKDMAAVQRTLMALGSVAVTKDD 119

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 78214339    24 ADLENKLVDWIILQCAEDIEHPPpgRTHFQKWLMDGTVLCKLINSLYPPGqepIPKISESKMAFKQMEQISQFLKAAEV- 102
Cdd:pfam00307   1 LELEKELLRWINSHLAEYGPGVR--VTNFTTDLRDGLALCALLNKLAPGL---VDKKKLNKSEFDKLENINLALDVAEKk 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 78214339   103 YGVRTTDIfQTVDLWEGKDMaAVQRTLMALGSVAVT 138
Cdd:pfam00307  76 LGVPKVLI-EPEDLVEGDNK-SVLTYLASLFRRFQA 109

Calponin family repeat;

                          10        20
                  ....*....|....*....|....*
gi 78214339   174 IGLQMGSNKGASQAGMTGYGMPRQI 198
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25

calponin homology (CH) domain found in transgelin-3; Transgelin-3, also called neuronal protein 22 (NP22), or neuronal protein NP25, may have a role in alcohol-related adaptations and may mediate regulatory signal transduction pathways in neurons. 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 78214339  23 DADLENKLVDWIILQCAEDIEHPPPGRTHFQKWLMDGTVLCKLINSLYPPGQEPIPKISESKMAFKQMEQISQFLKAAEV 102
Cdd:cd21281   1 DPDLESRLVDWIIIQCGGDIERPQPGRQNFQKWLMDGTILCRLINSLYPPGKEPIKKISETKMAFKQMEKISQFLQAAEA 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 78214339 103 YGVRTTDIFQTVDLWEGKDMAAVQRTLMALGSVAVTKDD 141
Cdd:cd21281  81 YGVITTDIFQTVDLWEGKDMAAVQRTLMALGSVAVTKDD 119

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 78214339  18 IEQKYDADLENKLVDWIILQCAEDIEHPPPGRTHFQKWLMDGTVLCKLINSLYPPGQEPIPKISESKMAFKQMEQISQFL 97
Cdd:cd21280   1 IDKQYDADLEQILIQWITAQCGKQVGRPQPGRENFQNWLKDGTVLCHLINSLYPKGQAPVKKIQASTMAFKQMEQISQFL 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 78214339  98 KAAEVYGVRTTDIFQTVDLWEGKDMAAVQRTLMALGSVAVTKDDGCYRGEPSWFHRK 154
Cdd:cd21280  81 QAAERYGINTTDIFQTVDLWEGKNMASVQRTLMNLGGLAVTRDDGLFVGDPNWFPKK 137

calponin homology (CH) domain found in Drosophila melanogaster muscle-specific protein 20 (dMP20) and similar domains; This subfamily contains Drosophila melanogaster muscle-specific protein 20 (dMP20), Echinococcus granulosus myophilin, Dictyostelium discoideum Rac guanine nucleotide exchange factor B (also called Trix), and similar proteins. dMP20 is present only in the synchronous muscles of D. melanogaster. It may be involved in the system linking the nerve impulse with the contraction or the relaxation process. Trix is involved in the regulation of the late steps of the endocytic pathway. dMP20 contains a single copy of the CH domain, while Trix (triple CH-domain array exchange factor) contains three, two type 3 CH domains which are included in this model, and one type 1 CH domain that is not included in this subfamily, but is part of the superfamily. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78214339  21 KYDADLENKLVDWIilqcAEDIEHPPPGRTHFQKWLMDGTVLCKLINSLYPPGqepIPKISESKMAFKQMEQISQFLKAA 100
Cdd:cd21207   1 KRDPALEAEALDWI----EAVTGEKLDDGKDYEDVLKDGVILCKLINILKPGS---VKKINTSKMAFKLMENIENFLTAC 73

                        90       100       110
                ....*....|....*....|....*....|....
gi 78214339 101 EVYGVRTTDIFQTVDLWEGKDMAAVQRTLMALGS 134
Cdd:cd21207  74 KGYGVPKTDLFQTVDLYEKKNIPQVTNCLFALGR 107

calponin homology (CH) domain found in calponin-3; Calponin-3 (CNN3), also called acidic isoform calponin, is an F-actin-binding protein that is expressed in the brain and has been shown to control dendritic spine morphology, density, and plasticity by regulating actin cytoskeletal reorganization and 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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78214339  21 KYDADLENKLVDWIilqcaEDIEHPPPGRtHFQKWLMDGTVLCKLINSLYPpgqEPIPKISESKMAFKQMEQISQFLKAA 100
Cdd:cd21284   1 KYDPQKEEELRNWI-----EEVTGMSIGE-NFQKGLKDGVILCELINKLQP---GSIRKINESKLNWHQLENIGNFIKAI 71

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 78214339 101 EVYGVRTTDIFQTVDLWEGKDMAAVQRTLMALGSVAVTK 139
Cdd:cd21284  72 QAYGMKPHDIFEANDLFENGNMTQVQTTLLALAGLAKTK 110

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 78214339  27 ENKLVDWIILQCAEDIehpPPGRTHFQKWLMDGTVLCKLINSLYPpgqEPIPKI-SESKMAFKQMEQISQFLKAAEVYGV 105
Cdd:cd00014   1 EEELLKWINEVLGEEL---PVSITDLFESLRDGVLLCKLINKLSP---GSIPKInKKPKSPFKKRENINLFLNACKKLGL 74

                        90       100
                ....*....|....*....|....*....
gi 78214339 106 RTTDIFQTVDLWEGKDMAAVQRTLMALGS 134
Cdd:cd00014  75 PELDLFEPEDLYEKGNLKKVLGTLWALAL 103

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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78214339  52 FQKWLMDGTVLCKLINSLYPPGqepIPKISESKMAFKQMEQISQFLKAAEVYGVRTTDIFQTVDLWEGKDMAAVQRTLMA 131
Cdd:cd21211  24 FQKGLKDGIILCELINKLQPGS---VKKINESMQNWHQLENIGNFIKAIVSYGMKPHDIFEANDLFENGNMTQVQVTLLA 100

                ....*...
gi 78214339 132 LGSVAVTK 139
Cdd:cd21211 101 LAGKAKTK 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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78214339  52 FQKWLMDGTVLCKLINSLYPpgqEPIPKISESKMAFKQMEQISQFLKAAEVYGVRTTDIFQTVDLWEGKDMAAVQRTLMA 131
Cdd:cd21283  24 FQKGLKDGVILCELMNKLQP---GSVPKINRSMQNWHQLENLSNFIKAMVSYGMKPVDLFEANDLFESGNMTQVQVSLLA 100

                ....*...
gi 78214339 132 LGSVAVTK 139
Cdd:cd21283 101 LAGMAKTK 108

Calponin family repeat;

                          10        20
                  ....*....|....*....|....*
gi 78214339   174 IGLQMGSNKGASQAGMTGYGMPRQI 198
Cdd:pfam00402   1 IGLQMGTNKGASQSGMTAFGAVRHI 25

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        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78214339  56 LMDGTVLCKLINSLyPPGQEPIPKIS--ESKMAFKQMEQISQFLKAA-EVYGVRTTDIFQTVDLWEGKDMAAVQRTL 129
Cdd:cd21201  36 LRDGVLLCQLLNRL-SPGSVDDREINlrPQMSQFLCLKNIRTFLQACrTVFGLRSADLFEPEDLYDVTNFGKVIRTL 111

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        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78214339  56 LMDGTVLCKLINSLYPPGQEPI---PKISESKMafkqmEQISQFLKAAEVYGVRTTDIFQTVDLWEGKDMAAVQRTLMAL 132
Cdd:cd21202  34 LKNGVVLCRLVNRLKPGTVEKIydePTTEEECL-----YNFESFLKACQELGILAEEIFDPNDLYSGGNFQKVLSTLERL 108

                ....
gi 78214339 133 GSVA 136
Cdd:cd21202 109 EKVA 112

calponin homology (CH) domain found in the leucine-rich repeat and calponin homology domain-containing protein family; The leucine-rich repeat and calponin homology domain-containing protein (LRCH) family includes LRCH1-4. LRCH1, also called calponin homology domain-containing protein 1, or neuronal protein 81 (NP81), acts as a negative regulator of GTPase Cdc42 by sequestering Cdc42-guanine exchange factor DOCK8. LRCH2 may play a role in the organization of the cytoskeleton. LRCH3 is part of the DISP complex and may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. LRCH4, also called leucine-rich repeat neuronal protein 4, or leucine-rich neuronal protein, acts as a novel Toll-like receptor (TLR) accessory protein that regulates the innate immune response. Members of this family contain a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78214339  56 LMDGTVLCKLINSLYPPG----QEPIPKISESKMAfKQMEQISQFLKAAEVYGVRTTDIFQTVDLWEGKDMAAVQRTLMA 131
Cdd:cd21205  26 LMDGVVLCHLANHVRPRSvpsiHVPSPAVPKLSMA-KCRRNVENFLEACRKLGVPEERLCSPGDILEEKGLVRVAVTVQA 104

                ...
gi 78214339 132 LGS 134
Cdd:cd21205 105 LLQ 107

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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78214339  56 LMDGTVLCKLINSLYPP----GQEPI-PKISEskmaFKQMEQISQFLKA-AEVYGVRTTDIFQTVDLWEGKDMAAVQRTL 129
Cdd:cd21262  36 LRDGVLLCQLLNNLLPHavnlREINLrPQMSQ----FLCLKNIRTFLSTcCEKFGLRKSELFEAFDLFDVRDFGKVIDTL 111

                ...
gi 78214339 130 MAL 132
Cdd:cd21262 112 SIL 114

calponin homology (CH) domain found in beta-Pak Interactive eXchange factor; Beta-Pak Interactive eXchange factor (beta-PIX), also called PAK-interacting exchange factor beta, Rho guanine nucleotide exchange factor 7 (ARHGEF7), p85, or Cool (Cloned out of Library)-1, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac1, and plays important roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. Beta-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        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78214339  31 VDWII----LQCAEDIEHPPPGrtHFQKWLMDGTVLCKLINSLYPPGQEPIpkISESKMAFKQMEQISQFLKAAEVYGVR 106
Cdd:cd21266   6 VTWLItlgvLESPKKTISDPEG--FLQASLKDGVVLCRLLERLLPGSIDKV--YPEPRTESECLSNIREFLRGCGALRLE 81

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 78214339 107 TtdiFQTVDLWEGKDMAAVQRTLMALGSvaVTKDDG 142
Cdd:cd21266  82 T---FDANDLYQGQNFNKVLSSLVALNK--VTADIG 112

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four 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 78214339  31 VDWI--ILQCAEDIEH----PPPGRTHFQKwLMDGTVLCKLINSLYpPGQEPIPKISESKM--AFKQMEQISQFLKAAEV 102
Cdd:cd21217   7 VEHInsLLADDPDLKHllpiDPDGDDLFEA-LRDGVLLCKLINKIV-PGTIDERKLNKKKPknIFEATENLNLALNAAKK 84

                        90       100
                ....*....|....*....|
gi 78214339 103 YGVRTTDIfQTVDLWEGKDM 122
Cdd:cd21217  85 IGCKVVNI-GPQDILDGNPH 103

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 4; Leucine-rich repeat and calponin homology domain-containing protein 4 (LRCH4), also called leucine-rich repeat neuronal protein 4, or leucine-rich neuronal protein, acts as a novel Toll-like receptor (TLR) accessory protein that regulates the innate immune response. LRCH4 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78214339  56 LMDGTVLCKLINSLYPPG-------QEPIPKISeskmAFKQMEQISQFLKAAEVYGVRTTDIFQTVDLWEGKDmAAVQRT 128
Cdd:cd21273  29 LSNGAVLCQLANQLRPRSvsiihvpSPAVPKLS----KAKCRKNVENFIEACRKMGVPEVDLCSPSDVLLQGP-AAVLRT 103

                ....
gi 78214339 129 LMAL 132
Cdd:cd21273 104 VLAL 107

calponin homology (CH) domain found in leucine-rich repeat and calponin homology domain-containing protein 3; Leucine-rich repeat and calponin homology domain-containing protein 3 (LRCH3) is part of the DISP (DOCK7-Induced Septin disPlacement) complex. It may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. LRCH3 contains a single copy of the CH domain at the C-terminus. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78214339  56 LMDGTVLCKLINSLYP---PG-QEPIPKISESKMAfKQMEQISQFLKAAEVYGVRTTDIFQTVDLWEGKDMAAVQRTLMA 131
Cdd:cd21272  26 LTDGVVLCHLANHVRPrsvPSiHVPSPAVPKLTMA-KCRRNVENFLEACRRIGVPQEQLCLPLHILEEKGLSQVAVTVQA 104

                ....*
gi 78214339 132 LGSVA 136
Cdd:cd21272 105 LLELA 109

calponin homology (CH) domain found in VAV2 protein and similar proteins; VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others. It has been reported to associate with Nek3. 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 VAV2 protein.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78214339  56 LMDGTVLCKLINSLyPPGQEPIPKIS-ESKMA-FKQMEQISQFLKAA-EVYGVRTTDIFQTVDLWEGKDMAAV 125
Cdd:cd21263  36 LRDGVLLCQLLHNL-SPGSIDLKDINfRPQMSqFLCLKNIRTFLKVChDKFGLRNSELFDPFDLFDVRDFGKV 107