calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). 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 17553196 341 RRNVLLMWVQEKLELYSDqLTVSNFSSDWTDCRAFCALLYDLFPDTMPDVTVSPivgdciSRCRRTFQLleiPFdERALG 420
Cdd:cd21199   9 KRNALLKWCQEKTQGYKG-IDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNP------QDKRRNFTL---AF-KAAES 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17553196 421 ISSPTADSgADEdsssacSVITGLTDWRYIMNTVFMLYKR 460
Cdd:cd21199  78 VGIPTTLT-IDE------MVSMERPDWQSVMSYVTAIYKH 110

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 17553196 342 RNVLLMWVQEKLELYSDQLTVSNFSSDWTDCRAFCALLYDLFPDTM 387
Cdd:COG5069 127 HINLLLWCDEDTGGYKPEVDTFDFFRSWRDGLAFSALIHDSRPDTL 172

calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). 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 17553196 341 RRNVLLMWVQEKLELYSDqLTVSNFSSDWTDCRAFCALLYDLFPDTMPDVTVSPivgdciSRCRRTFQLleiPFdERALG 420
Cdd:cd21199   9 KRNALLKWCQEKTQGYKG-IDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNP------QDKRRNFTL---AF-KAAES 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17553196 421 ISSPTADSgADEdsssacSVITGLTDWRYIMNTVFMLYKR 460
Cdd:cd21199  78 VGIPTTLT-IDE------MVSMERPDWQSVMSYVTAIYKH 110

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 17553196   341 RRNVLLMWVQEKLELYSDQLTVSNFSSDWTDCRAFCALLYDLFPDTMPDVTVSPIVGDCISRCRRTFQLLeipfdERALG 420
Cdd:pfam00307   3 LEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKLENINLALDVA-----EKKLG 77

                  ..
gi 17553196   421 IS 422
Cdd:pfam00307  78 VP 79

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17553196 342 RNVLLMWVQEKLELYSdqltVSNFSSDWTDCRAFCALLYDLFPDTMPDvTVSPIVGDCISRCRRTFQLLeipfdERALGI 421
Cdd:cd21184   3 KSLLLEWVNSKIPEYK----VKNFTTDWNDGKALAALVDALKPGLIPD-NESLDKENPLENATKAMDIA-----EEELGI 72

                .
gi 17553196 422 S 422
Cdd:cd21184  73 P 73

calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. 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
                ....*....|....*....|....*....|....*....|....
gi 17553196 342 RNVLLMWVQEKLELYsDQLTVSNFSSDWTDCRAFCALLYDLFPD 385
Cdd:cd21200   3 KQMLLEWCQAKTRGY-EHVDITNFSSSWSDGMAFCALIHHFFPD 45

calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17553196 342 RNVLLMWVQEKLELYsDQLTVSNFSSDWTDCRAFCALLYDLFPDTMPDVTVSP 394
Cdd:cd21259   3 KQMLLDWCRAKTRGY-ENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSP 54

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

                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17553196 345 LLMWVQEKLELYsDQLTVSNFSSDWTDCRAFCALLYDLFPD 385
Cdd:cd21291  15 LLLWCQRKTAGY-DEVDVQDFTTSWTDGLAFCALIHRHRPD 54

calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 17553196 345 LLMWVQEKLELYSDqLTVSNFSSDWTDCRAFCALLYDLFPD 385
Cdd:cd22198   5 LLSWCQEQTEGYRG-VKVTDLTSSWRSGLALCAIIHRFRPD 44

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

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 17553196 345 LLMWVQEKLElysdQLTVSNFSSDWTDCRAFCALLYDLFPDTMPD 389
Cdd:cd21230   6 LLGWIQNKIP----QLPITNFTTDWNDGRALGALVDSCAPGLCPD 46

second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The 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 second CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17553196 342 RNVLLMWVQEKLELYSDqLTVSNFSSDWTDCRAFCALLYDLFPD--TMPDVTVSP 394
Cdd:cd21192   5 EKALLKWVQAEIGKYYG-IRVTDFDKSWRDGVAFLALIHAIRPDlvDMKTVKNRS 58

third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17553196 336 HKNTLRrnvllmWVQEKLElysdQLTVSNFSSDWTDCRAFCALLYDL------FPDTMPDvtvspivgDCISRCRRTF 407
Cdd:cd21185   3 YKATLR------WVRQLLP----DVDVNNFTTDWNDGRLLCGLVNALggsvpgWPNLDPE--------ESENNIQRGL 62

calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 17553196 345 LLMWVQEKLELYSDqLTVSNFSSDWTDCRAFCALLYDLFP 384
Cdd:cd21196   8 LLRWCQEQTAGYPG-VHVSDLSSSWADGLALCALVYRLQP 46

calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 17553196 345 LLMWVQEKLELYSDqLTVSNFSSDWTDCRAFCALLYDLFPDTM 387
Cdd:cd21255   6 LLEWCQEVTAGYRG-VRVTNFTTSWRNGLAFCAILHHFHPDLV 47

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

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 17553196 342 RNVLLMWVQEKLELYsDQLTVSNFSSDWTDCRAFCALLYDLFPD 385
Cdd:cd21248   4 KDALLLWCQMKTAGY-PNVNVRNFTTSWRDGLAFNALIHKHRPD 46

second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three 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 17553196 342 RNVLLMWVQEKLElysdQLTVSNFSSDWTDCRAFCALLYDLFPDTMPD-VTVSPivGDCISRCRRTFQL----LEIPFDE 416
Cdd:cd21229   5 KKLMLAWLQAVLP----ELKITNFSTDWNDGIALSALLDYCKPGLCPNwRKLDP--SNSLENCRRAMDLakreFNIPMVL 78

                        90
                ....*....|.
gi 17553196 417 RALGISSPTAD 427
Cdd:cd21229  79 SPEDLSSPHLD 89

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

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 17553196 345 LLMWVQEKLElysdQLTVSNFSSDWTDCRAFCALLYDLFPDTMPD 389
Cdd:cd21315  21 LLGWIQSKVP----DLPITNFTNDWNDGKAIGALVDALAPGLCPD 61

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 17553196 342 RNVLLMWVQEKLELYSDQLTVSNFSSDWTDCRAFCALLYDLFPDTM 387
Cdd:COG5069 127 HINLLLWCDEDTGGYKPEVDTFDFFRSWRDGLAFSALIHDSRPDTL 172

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

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 17553196 342 RNVLLMWVQEKLELYSdQLTVSNFSSDWTDCRAFCALLYDLFPDTM 387
Cdd:cd21322  19 KDALLLWCQMKTAGYP-EVNIQNFTTSWRDGLAFNALIHRHRPDLI 63