Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB7, also known as cardiovascular small heat shock protein (cvHsp), and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. HspB7 is a 25-kDa protein, preferentially expressed in heart and skeletal muscle. It binds the cytoskeleton protein alpha-filamin (also known as actin-binding protein 280). The expression of HspB7 is increased during rat muscle aging. Its expression is also modulated in obesity implicating this protein in this and related metabolic disorders. As the human gene encoding HspB7 is mapped to chromosome 1p36.23-p34.3 it is a positional candidate for several dystrophies and myopathies.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503301  67 GNIKTLGDAYEFAVDVRDFSPEDIIVTTSNNHIEVRAEKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSLTIRAR 146
Cdd:cd06479     1 GNVKTLGDTYQFAVDVSDFSPEDIIVTTSNNQIEVHAEKLASDGTVMNTFTHKCQLPEDVDPTSVSSSLGEDGTLTIKAR 80

                  .
gi 1167503301 147 R 147
Cdd:cd06479    81 R 81

Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB7, also known as cardiovascular small heat shock protein (cvHsp), and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. HspB7 is a 25-kDa protein, preferentially expressed in heart and skeletal muscle. It binds the cytoskeleton protein alpha-filamin (also known as actin-binding protein 280). The expression of HspB7 is increased during rat muscle aging. Its expression is also modulated in obesity implicating this protein in this and related metabolic disorders. As the human gene encoding HspB7 is mapped to chromosome 1p36.23-p34.3 it is a positional candidate for several dystrophies and myopathies.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503301  67 GNIKTLGDAYEFAVDVRDFSPEDIIVTTSNNHIEVRAEKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSLTIRAR 146
Cdd:cd06479     1 GNVKTLGDTYQFAVDVSDFSPEDIIVTTSNNQIEVHAEKLASDGTVMNTFTHKCQLPEDVDPTSVSSSLGEDGTLTIKAR 80

                  .
gi 1167503301 147 R 147
Cdd:cd06479    81 R 81

Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503301  68 NIKTLGDAYEFAVDVRDFSPEDIIVTTSNNHIEVRAEK----LAADGTVM------NTFAHKCQLPEDVDPTSVTSALrE 137
Cdd:COG0071     3 DIEETDDAYVITADLPGVDKEDIDVTVEGNVLTISGERkeeeEEEGENYLrrerryGSFERSFTLPDDVDVDKIEASY-E 81

                  ....*..
gi 1167503301 138 DGSLTIR 144
Cdd:COG0071    82 NGVLTIT 88

Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB7, also known as cardiovascular small heat shock protein (cvHsp), and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. HspB7 is a 25-kDa protein, preferentially expressed in heart and skeletal muscle. It binds the cytoskeleton protein alpha-filamin (also known as actin-binding protein 280). The expression of HspB7 is increased during rat muscle aging. Its expression is also modulated in obesity implicating this protein in this and related metabolic disorders. As the human gene encoding HspB7 is mapped to chromosome 1p36.23-p34.3 it is a positional candidate for several dystrophies and myopathies.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503301  67 GNIKTLGDAYEFAVDVRDFSPEDIIVTTSNNHIEVRAEKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSLTIRAR 146
Cdd:cd06479     1 GNVKTLGDTYQFAVDVSDFSPEDIIVTTSNNQIEVHAEKLASDGTVMNTFTHKCQLPEDVDPTSVSSSLGEDGTLTIKAR 80

                  .
gi 1167503301 147 R 147
Cdd:cd06479    81 R 81

Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503301  68 NIKTLGDAYEFAVDVRDFSPEDIIVTTSNNHIEVRAEKLAADGT---------VMNTFAHKCQLPEDVDPTSVTSALrED 138
Cdd:cd06464     1 DVYETDDAYVVEADLPGFKKEDIKVEVEDGVLTISGEREEEEEEeenylrrerSYGSFSRSFRLPEDVDPDKIKASL-EN 79

                  ....*....
gi 1167503301 139 GSLTIRARR 147
Cdd:cd06464    80 GVLTITLPK 88

Alpha crystallin domain (ACD) found in mammalian small (s)heat shock protein (Hsp)-27 (also denoted HspB1 in human) and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Hsp27 shows enhanced synthesis in response to stress. It is a molecular chaperone which interacts with a large number of different proteins. It is found in many types of human cells including breast, uterus, cervix, platelets and cancer cells. Hsp27 has diverse cellular functions including, chaperoning, regulation of actin polymerization, keratinocyte differentiation, regulation of inflammatory pathways in keratinocytes, and protection from oxidative stress through modulating glutathione levels. It is also a subunit of AUF1-containing protein complexes. It has been linked to several transduction pathways regulating cellular functions including differentiation, cell growth, development, and apoptosis. Its activity can be regulated by phosphorylation. Its unphosphorylated state is a high molecular weight aggregated form (100-800kDa) composed of up to 24 subunits, which forms as a result of multiple interactions within the ACD, and is required for chaperone function and resistance to oxidative stress. Upon phosphorylation these large aggregates rapidly disassociate to smaller oligomers and chaperone activity is modified. High constitutive levels of Hsp27 have been detected in various cancer cells, in particular those of carcinoma origin. Over-expression of Hsp27 has a protective effect against various diseases-processes, including Huntington's disease. Mutations in Hsp27 have been associated with a form of distal hereditary motor neuropathy type II and Charcot-Marie-Tooth disease type 2.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503301  69 IKTLGDAYEFAVDVRDFSPEDIIVTTSNNHIEVRA---EKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSLTIRA 145
Cdd:cd06475     5 IRQTADRWKVSLDVNHFAPEELVVKTKDGVVEITGkheEKQDEHGFVSRCFTRKYTLPPGVDPTAVTSSLSPDGILTVEA 84

Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaB-crystallin (HspB5, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. HspB4 does not belong to this group. HspB5 shows increased synthesis in response to stress. HspB5 is also expressed constitutively in other tissues including brain, heart, and type I and type IIa skeletal muscle fibers, and in several cancers including gliomas, renal cell carcinomas, basal-like and metaplastic breast carcinomas, and head and neck cancer. Its functions include effects on the apoptotic pathway and on metastasis. Phosphorylation of HspB5 reduces its oligomerization and anti-apoptotic activities. HspB5 is protective in demyelinating disease such as multiple sclerosis (MS), being a negative regulator of inflammation. In early active MS lesions it is the most abundant gene transcript and an autoantigen, the immune response against it would disrupt its function and worsen inflammation and demyelination. Given as therapy for ongoing demyelinating disease it may counteract this effect. It is an autoantigen in the pathogenesis of various other inflammatory disorders including Lens-associated uveitis (LAU), and Behcet's disease. Mutations in HspB5 have been associated with diseases including dominant cataract and desmin-related myopathy.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1167503301  74 DAYEFAVDVRDFSPEDIIVTTSNNHIEVRA---EKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSLTIRARR 147
Cdd:cd06498     7 DKFSVNLDVKHFSPEELKVKVLGDFIEIHGkheERQDEHGFISREFQRKYRIPADVDPLTITSSLSPDGVLTVCGPR 83

Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and prokaryotes but they have also now been shown to occur in cyanobacterial phages as well as their bacterial hosts.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503301  69 IKTLGDAYEFAVDVRDFSPEDIIVTTSNNHIEVRA--EKLAADGTV------MNTFAHKCQLPEDVDPTSVTSALrEDGS 140
Cdd:pfam00011   2 IKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGehEEEKEDDHGlrsersYGSFSRKFTLPENADPDKVKASL-KDGV 80

                  ....*
gi 1167503301 141 LTIRA 145
Cdd:pfam00011  81 LTVTV 85

Alpha crystallin domain (ACD) found in mammalian small heat shock protein (sHsp) HspB2/heat shock 27kDa protein 2 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. HspB2 is preferentially and constitutively expressed in skeletal muscle and heart. HspB2 shows homooligomeric activity and forms aggregates in muscle cytosol. Although its expression is not induced by heat shock, it redistributes to the insoluble fraction in response to heat shock. In the mouse heart, HspB2 plays a role in maintaining energetic balance, by protecting cardiac energetics during ischemia/reperfusion, and allowing for increased work during acute inotropic challenge. hHspB2 [previously also known as myotonic dystrophy protein kinase (DMPK) binding protein (MKBP)] is selectively up-regulated in skeletal muscles from myotonic dystrophy patients. The ACD of hHspB2 binds the DMPK kinase domain. In vitro, hHspB2 enhances the kinase activity of DMPK and confers thermoresistance. The hHspB2 gene lies less than 1kb from the 5 prime end of the related alphaB (HspB4)-crystallin gene, with the opposite transcription direction. These two genes may share regulatory elements for their expression.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503301  71 TLGDAYEFAVDVRDFSPEDIIVTTSNNHIEVRA---EKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSLTIRARR 147
Cdd:cd06476     4 SEDDKYQVFLDVCHFTPDEITVRTVDNLLEVSArhpQRMDRHGFVSREFTRTYILPMDVDPLLVRASLSHDGILCIQAPR 83

Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167503301  68 NIKTLGDAYEFAVDVRDFSPEDIIVTTSNNHIEVRAEK----LAADGTVM------NTFAHKCQLPEDVDPTSVTSALrE 137
Cdd:COG0071     3 DIEETDDAYVITADLPGVDKEDIDVTVEGNVLTISGERkeeeEEEGENYLrrerryGSFERSFTLPDDVDVDKIEASY-E 81

                  ....*..
gi 1167503301 138 DGSLTIR 144
Cdd:COG0071    82 NGVLTIT 88