SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) proteins (also known as SANS) is a putative protein-protein interaction domain. Members of this group have an N-terminal ankyrin repeat region and C-terminal SAM domain. USH1G is expressed in the hair bundles of the inner ear sensory cells. It can form a functional network with USH1B (myosin VIIa), USH1C (harmonin b), USH1F (protocadherin-related 15), and USH1D (cadherin 23). The SAM domain of the USH1G protein is involved in synergetic interactions with the PDZ domain of harmonin. Such interactions contribute to the stability of harmonin. The network is required for the correct cohesion of the hair bundle. Mutations in the ush1g gene lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767993490 285 ETSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQAMERP 350
Cdd:cd09586    1 DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRRRQTIERP 66

SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) proteins (also known as SANS) is a putative protein-protein interaction domain. Members of this group have an N-terminal ankyrin repeat region and C-terminal SAM domain. USH1G is expressed in the hair bundles of the inner ear sensory cells. It can form a functional network with USH1B (myosin VIIa), USH1C (harmonin b), USH1F (protocadherin-related 15), and USH1D (cadherin 23). The SAM domain of the USH1G protein is involved in synergetic interactions with the PDZ domain of harmonin. Such interactions contribute to the stability of harmonin. The network is required for the correct cohesion of the hair bundle. Mutations in the ush1g gene lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767993490 285 ETSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQAMERP 350
Cdd:cd09586    1 DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRRRQTIERP 66

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.

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                  ....*....|....*....|....*....|....*....|....*....|....
gi 767993490  292 FLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISV-PLGPRKKILGAVRRRR 344
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVtLLGHRKKILYAIQRLK 64

SAM domain of USH1G; SAM (sterile alpha motif) domain of USH1G (Usher syndrome type-1G protein) proteins (also known as SANS) is a putative protein-protein interaction domain. Members of this group have an N-terminal ankyrin repeat region and C-terminal SAM domain. USH1G is expressed in the hair bundles of the inner ear sensory cells. It can form a functional network with USH1B (myosin VIIa), USH1C (harmonin b), USH1F (protocadherin-related 15), and USH1D (cadherin 23). The SAM domain of the USH1G protein is involved in synergetic interactions with the PDZ domain of harmonin. Such interactions contribute to the stability of harmonin. The network is required for the correct cohesion of the hair bundle. Mutations in the ush1g gene lead to Usher syndrome type 1G. This syndrome is the cause of deaf-blindness in humans.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767993490 285 ETSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRRQAMERP 350
Cdd:cd09586    1 DTSPLEVFLASLSMEEFIAILKREKIDLDALLLCSDNDLKSIHIPLGPRKKILDACQRRRQTIERP 66

central domain found in usher syndrome type-1G protein; Usher syndrome type-1G protein (USH1G), also called scaffold protein containing ankyrin repeats and SAM domain (Sans), is an anchoring/scaffolding protein that is part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A, that mediates mechanotransduction in cochlear hair cells. It is required for normal development and maintenance of cochlear hair cell bundles, as well as for normal hearing. USH1G consists of four N-terminal ANK repeats, a central region, and a sterile alpha motif (SAM) followed by a C-terminal type I PDZ binding motif (PBM). This model corresponds to the central region (CEN) of USH1G, which contains the conserved regions CEN1 and CEN2. CEN is directly responsible for binding to the MYO7A MyTH4-FERM tandem.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993490 193 EVSTDSGHDSLFTRPGLGTMVFRRNYLSSGLHGLGREDggldgvgaprgrlqsspsldddslgsanslqdrscgEELPWD 272
Cdd:cd21803    1 EVSTDSGHDSLFNRPGLGTMVFRRNYVSSGLFGLGRED------------------------------------EELPWD 44

                         90
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gi 767993490 273 ELDLGLDEDLEPE 285
Cdd:cd21803   45 EVDLGLDDDDEPD 57

SAM domain of sec23ip-like subfamily; SAM (sterile alpha motif) domain of Sec23ip-like (Sec23 interacting protein) subfamily is a potential protein-protein interaction domain. This group of proteins includes Sec23ip and DDHD2 proteins. All of them contain at least two domains: a SAM domain and a predicted metal-binding domain. For mammalian DDHD2 members of this group, phospholipase activity has been demonstrated. Sec23ip proteins of this group interact with Sec23 proteins via an N-terminal proline-rich region. Members of this subfamily are involved in organization of ER/Golgi intermediate compartment.

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gi 767993490 280 EDLEPETSPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISVPLGPRKKILGAVRRRR 344
Cdd:cd09516    3 VEEQEEPLTLEEDLEKLGLSEYFDTFEKEKIDMESLLLCSESDLKEMGIPMGPRKKLLGFLKDQK 67

central domain found in usher syndrome type-1G protein, ankyrin repeat and SAM domain-containing protein 4B, and similar proteins; The family includes usher syndrome type-1G protein (USH1G), ankyrin repeat and SAM domain-containing protein 4B (ANKS4B), and similar proteins. USH1G, also called scaffold protein containing ankyrin repeats and SAM domain (Sans), is an anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A, that mediates mechanotransduction in cochlear hair cells. It is required for normal development and maintenance of cochlear hair cell bundles, as well as for normal hearing. ANKS4B, also called Harmonin-interacting ankyrin repeat-containing protein (Harp), is highly expressed in intestine and is essential for intermicrovillar adhesion. As part of the intermicrovillar adhesion complex (IMAC), ANKS4B plays a role in epithelial brush border differentiation, controlling microvilli organization and length. It may be involved in cellular response to endoplasmic reticulum stress. Both USH1G and ANKS4B contain four N-terminal ANK repeats, a central region, and a sterile alpha motif (SAM) followed by a C-terminal type I PDZ binding motif (PBM). This model corresponds to the central region (CEN), which contains the conserved regions CEN1 and CEN2. CEN is directly responsible for USH1G binding to the MYO7A MyTH4-FERM tandem, as well as for ANKS4B binding to the N-terminal MyTH4-FERM-SH3 supramodule of MYO7B.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767993490 193 EVSTDSGHDSLFTRPGLGTMVFRRNYlssglhglgredggldgvgaprgrlqsspsldddslgsanslqdrscgEELPWD 272
Cdd:cd21764    1 EESTDSGHESIFNRPGLGNIVFRRNL------------------------------------------------EELPWD 32

                 ....*....
gi 767993490 273 ELDLGLDED 281
Cdd:cd21764   33 EEELEWDEE 41

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.

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                  ....*....|....*....|....*....|....*....|....*....|....
gi 767993490  292 FLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISV-PLGPRKKILGAVRRRR 344
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVtLLGHRKKILYAIQRLK 64

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.

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                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767993490   292 FLASLHMEDFAALLRQEKIDLEALMLCSDL-DLRSISV-PLGPRKKILGAVRRRRQ 345
Cdd:smart00454  12 WLESIGLEQYADNFRKNGIDGALLLLLTSEeDLKELGItKLGHRKKILKAIQKLKE 67

SAM domain of BICC1 (bicaudal) subfamily; SAM (sterile alpha motif) domain of BICC1 (bicaudal) subfamily is a protein-protein interaction domain. Proteins of this group have N-terminal K homology RNA-binding vigilin-like repeats and a C-terminal SAM domain. BICC1 is involved in the regulation of embryonic differentiation. It plays a role in the regulation of Dvl (Dishevelled) signaling, particularly in the correct cilia orientation and nodal flow generation. In Drosophila, disruption of BICC1 can disturb the normal migration direction of the anterior follicle cell of oocytes; the specific function of SAM is to recruit whole protein to the periphery of P-bodies. In mammals, mutations in this gene are associated with polycystic kidney disease and it was suggested that the BICC1 protein can indirectly interact with ANKS6 protein (ANKS6 is also associated with polycystic kidney disease) through some protein and RNA intermediates.

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                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767993490 287 SPLETFLASLHMEDFAALLRQEKIDLEALMLCSDLDLRSISV-PLGPRKKILGAV 340
Cdd:cd09520    5 SDLPELLAKLGLEKYIDLFAQQEIDLQTFLTLTDQDLKELGItAFGARRKMLLAI 59