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 31542970  72 GNIKTLGDAYEFTVDMRDFSPEDIIVTTFNNHIEVRAEKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSLTIRAR 151
Cdd:cd06479   1 GNVKTLGDTYQFAVDVSDFSPEDIIVTTSNNQIEVHAEKLASDGTVMNTFTHKCQLPEDVDPTSVSSSLGEDGTLTIKAR 80

                .
gi 31542970 152 R 152
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 31542970  72 GNIKTLGDAYEFTVDMRDFSPEDIIVTTFNNHIEVRAEKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSLTIRAR 151
Cdd:cd06479   1 GNVKTLGDTYQFAVDVSDFSPEDIIVTTSNNQIEVHAEKLASDGTVMNTFTHKCQLPEDVDPTSVSSSLGEDGTLTIKAR 80

                .
gi 31542970 152 R 152
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 31542970  73 NIKTLGDAYEFTVDMRDFSPEDIIVTTFNNHIEVRAEK----LAADGTVM------NTFAHKCQLPEDVDPTSVTSALrE 142
Cdd:COG0071   3 DIEETDDAYVITADLPGVDKEDIDVTVEGNVLTISGERkeeeEEEGENYLrrerryGSFERSFTLPDDVDVDKIEASY-E 81

                ....*..
gi 31542970 143 DGSLTIR 149
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 31542970  72 GNIKTLGDAYEFTVDMRDFSPEDIIVTTFNNHIEVRAEKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSLTIRAR 151
Cdd:cd06479   1 GNVKTLGDTYQFAVDVSDFSPEDIIVTTSNNQIEVHAEKLASDGTVMNTFTHKCQLPEDVDPTSVSSSLGEDGTLTIKAR 80

                .
gi 31542970 152 R 152
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 31542970  73 NIKTLGDAYEFTVDMRDFSPEDIIVTTFNNHIEVRAEKLAADGT---------VMNTFAHKCQLPEDVDPTSVTSALrED 143
Cdd:cd06464   1 DVYETDDAYVVEADLPGFKKEDIKVEVEDGVLTISGEREEEEEEeenylrrerSYGSFSRSFRLPEDVDPDKIKASL-EN 79

                ....*....
gi 31542970 144 GSLTIRARR 152
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 31542970  70 GQGNIKTLGDAYEFTVDMRDFSPEDIIVTTFNNHIEVRA---EKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSL 146
Cdd:cd06475   1 GMSEIRQTADRWKVSLDVNHFAPEELVVKTKDGVVEITGkheEKQDEHGFVSRCFTRKYTLPPGVDPTAVTSSLSPDGIL 80

                ....
gi 31542970 147 TIRA 150
Cdd:cd06475  81 TVEA 84

Alpha-crystallin domain found in alphaA-crystallin (HspB4), alphaB-crystallin (HspB5), and the small heat shock protein (sHsp) HspB6, also known as Hsp20. 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. Only trace amounts of HspB4 are found in tissues other than the lens. HspB5 on the other hand 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. HspB5's 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. Mutations in HspB4 have been associated with Autosomal Dominant Congenital Cataract (ADCC). HspB6 (Hsp20) is ubiquitous and is involved in diverse functions including regulation of glucose transport and contraction of smooth muscle, in platelet aggregation, in cardioprotection, and in the prevention of apoptosis. It interacts with the universal scaffolding and adaptor protein 14-3-3, and also with the proapoptotic protein Bax.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31542970  79 DAYEFTVDMRDFSPEDIIVTTFNNHIEVRA---EKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSLTIRARR 152
Cdd:cd06478   7 DRFSVNLDVKHFSPEELSVKVLGDFVEIHGkheERQDEHGFISREFHRRYRLPPGVDPAAITSSLSADGVLTISGPR 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 31542970    74 IKTLGDAYEFTVDMRDFSPEDIIVTTFNNHIEVRA--EKLAADGTV------MNTFAHKCQLPEDVDPTSVTSALrEDGS 145
Cdd:pfam00011   2 IKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGehEEEKEDDHGlrsersYGSFSRKFTLPENADPDKVKASL-KDGV 80

                  ....*
gi 31542970   146 LTIRA 150
Cdd:pfam00011  81 LTVTV 85

Alpha-crystallin domain (ACD) found in mammalian 21.6 KDa small heat shock protein (sHsp) HspB8, also denoted as Hsp22 in humans, 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. A chaperone complex formed of HspB8 and Bag3 stimulates degradation of protein complexes by macroautophagy. HspB8 also forms complexes with Hsp27 (HspB1), MKBP (HspB2), HspB3, alphaB-crystallin (HspB5), Hsp20 (HspB6), and cvHsp (HspB7). These latter interactions may depend on phosphorylation of the respective partner sHsp. HspB8 may participate in the regulation of cell proliferation, cardiac hypertrophy, apoptosis, and carcinogenesis. Point mutations in HspB8 have been correlated with the development of several congenital neurological diseases, including Charcot Marie tooth disease and distal motor neuropathy type II.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542970  68 PGGQGNIKTLGDAYEFTVDMRDFSPEDIIVTTFNNHIEVRA---EKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDG 144
Cdd:cd06480   4 PEPRNPPPNSSEPWKVCVNVHSFKPEELTVKTKDGFVEVSGkheEQQKEGGIVSKNFTKKIQLPPEVDPVTVFASLSPEG 83

                ....*...
gi 31542970 145 SLTIRARR 152
Cdd:cd06480  84 LLIIEAPQ 91

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31542970  73 NIKTLGDAYEFTVDMRDFSPEDIIVTTFNNHIEVRAEK----LAADGTVM------NTFAHKCQLPEDVDPTSVTSALrE 142
Cdd:COG0071   3 DIEETDDAYVITADLPGVDKEDIDVTVEGNVLTISGERkeeeEEEGENYLrrerryGSFERSFTLPDDVDVDKIEASY-E 81

                ....*..
gi 31542970 143 DGSLTIR 149
Cdd:COG0071  82 NGVLTIT 88