EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156630438  36 LLQDLRPILNTLWSSGESTISLAQEDVQQHLEELFRSISPELPDQAVTEATDQTTRLLFKLFDRGQTGVILLRSVEAALI 115
Cdd:cd16243    1 DLRLIKPILNSLGGSIERTISLSVEEVSQALERLFQSASQEVPGQVSAEATEQTCRLLFRLYDREQTGFVSLRSVEAALI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156630438 116 ALCGDTLSAKQRALFRLAESysgNQESDRGSISRSALRVLLEDLSQVPAVVQENHVFGHAETAVSSCFNGVISAGVTEEH 195
Cdd:cd16243   81 ALSGDTLSAKYRALFQLYES---GQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFGNVETAVRSCFSGVLTASISEEH 157

                 ....*.
gi 156630438 196 FIWWLQ 201
Cdd:cd16243  158 FLSWLQ 163

EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156630438  36 LLQDLRPILNTLWSSGESTISLAQEDVQQHLEELFRSISPELPDQAVTEATDQTTRLLFKLFDRGQTGVILLRSVEAALI 115
Cdd:cd16243    1 DLRLIKPILNSLGGSIERTISLSVEEVSQALERLFQSASQEVPGQVSAEATEQTCRLLFRLYDREQTGFVSLRSVEAALI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156630438 116 ALCGDTLSAKQRALFRLAESysgNQESDRGSISRSALRVLLEDLSQVPAVVQENHVFGHAETAVSSCFNGVISAGVTEEH 195
Cdd:cd16243   81 ALSGDTLSAKYRALFQLYES---GQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFGNVETAVRSCFSGVLTASISEEH 157

                 ....*.
gi 156630438 196 FIWWLQ 201
Cdd:cd16243  158 FLSWLQ 163

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 156630438 226 VHCHACKAFPITGLRYRCLKCLNVHLCQSCFLTERRSRKHKPSHSVLEY 274
Cdd:cd02334    1 AKCNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSHKNSHPMKEY 49

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 156630438  224 HRVHCHACKAFPITGLRYRCLKCLNVHLCQSCFLTeRRSRKHKP 267
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45

EF-hand-like motif found in dystrotelin and similar proteins; Dystrotelin is the vertebrate orthologue of Drosophila DAH, which is involved in the synchronised cellularization of thousands of nuclei in the syncytial early fly embryo (a specialised form of cytokinesis). Dystrotelin is mainly expressed in the developing central nervous system (CNS) and adult nervous and muscular tissues. Heterologously expressed dystrotelin protein localizes spontaneously to the cytoplasmic membrane, and possibly to the endoplasmic reticulum (ER). Dystrotelin is not critical for mammalian development. It may be involved in other forms of cytokinesis. Its N-terminal region contains a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. The C-terminal region is extremely divergent. Unlike other superfamily members, dystrophin or dystrobrevin, the residues directly involved in beta-dystroglycan binding are not conserved in dystrotelin, which makes it unlikely that dystrotelin interacts with this ligand. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156630438  36 LLQDLRPILNTLWSSGESTISLAQEDVQQHLEELFRSISPELPDQAVTEATDQTTRLLFKLFDRGQTGVILLRSVEAALI 115
Cdd:cd16243    1 DLRLIKPILNSLGGSIERTISLSVEEVSQALERLFQSASQEVPGQVSAEATEQTCRLLFRLYDREQTGFVSLRSVEAALI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156630438 116 ALCGDTLSAKQRALFRLAESysgNQESDRGSISRSALRVLLEDLSQVPAVVQENHVFGHAETAVSSCFNGVISAGVTEEH 195
Cdd:cd16243   81 ALSGDTLSAKYRALFQLYES---GQGGSSGSITRSGLRVLLQDLSQIPAVVQESHVFGNVETAVRSCFSGVLTASISEEH 157

                 ....*.
gi 156630438 196 FIWWLQ 201
Cdd:cd16243  158 FLSWLQ 163

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156630438  47 LWSSGESTISLaqEDVQQHLEELFRSISPELPDQAVTE-ATDQTTRLLFKLFDRGQTGVILLRSVEAALIALCGDTLSAK 125
Cdd:cd15901   14 LSGSQDSVLDC--EELETILTELYIKLNKRRPDLIDVPrASDLLLNWLLNLYDRNRTGCIRLLSVKIALITLCAASLLDK 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156630438 126 QRALFRLAESYSgnqesdrGSISRSALRVLLEDLSQVPAVVQENHVFG--HAETAVSSCFNGVIS-AGVTEEHFIWWLQ 201
Cdd:cd15901   92 YRYLFGQLADSS-------GFISRERLTQFLQDLLQIPDLIGESPAFGghNVEAAVESCFQLARSrVGVSEDTFLSWLL 163

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 156630438   222 VQHRVHCHACKAfPITGLRYRCLKCLNVHLCQSCFLTERRSRKHK 266
Cdd:smart00291   1 VHHSYSCDTCGK-PIVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 156630438  224 HRVHCHACKAFPITGLRYRCLKCLNVHLCQSCFLTeRRSRKHKP 267
Cdd:pfam00569   3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQT-HKGGNHQM 45

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 156630438 228 CHACKAfPITGLRYRCLKCLNVHLCQSCFLTERrsRKHKPSHSVLEY 274
Cdd:cd02249    3 CDGCLK-PIVGVRYHCLVCEDFDLCSSCYAKGK--KGHPPDHSFTEI 46

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 156630438 228 CHACKAFPITGLRYRCLKCLNVHLCQSCFLTErrsrKHKPSHSVLEY 274
Cdd:cd02339    3 CDTCRKQGIIGIRWKCAECPNYDLCTTCYHGD----KHDLEHRFYRY 45

EF-hand-like motif found in the dystrophins subfamily; This dystrophins subfamily includes dystrophin and its two paralogs, utrophin and DRP-2. Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin also involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. DRP-2 is mainly expressed in the vertebrate central nervous system (CNS). It is associated with brain membrane fractions and highly enriched in the postsynaptic density. DRP-2 plays a role in the organization of central cholinergic synapses. It interacts with dystroglycan and L-Periaxin to form a transmembrane complex, which plays a role in Schwann cell-basal lamina interactions and in the regulation of the terminal stages of myelination. The dystrophins subfamily has been characterized by a compact cluster of domains comprising a WW domain, four EF-hand-like motifs and a ZZ-domain, followed by two syntrophin binding sites (SBSs) and a looser region with two coiled-coils.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156630438  66 LEELFRSISPELPD-QAVTEATDQTTRLLFKLFDRGQTGVILLRSVEAALIALCGDTLSAKQRALFRLAesysgnqeSDR 144
Cdd:cd16242   31 LTTIYEALEEEHPTlVNVPLCVDLCLNWLLNVYDSGRSGKIRVLSFKVGLVLLCNAHLEEKYRYLFSLI--------ADP 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156630438 145 -GSISRSALRVLLEDLSQVPAVVQENHVFG--HAETAVSSCFNGV-ISAGVTEEHFIWWLQ 201
Cdd:cd16242  103 nGCVDQRRLGLLLHDCIQIPRQLGEVAAFGgsNIEPSVRSCFEKAgEKPEISAAHFLDWLK 163

Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 156630438 227 HCHACKAFPITGLRYRCLKCLNVHLCQSCFLTERRSRKHKPSHS 270
Cdd:cd02335    2 HCDYCSKDITGTIRIKCAECPDFDLCLECFSAGAEIGKHRNDHN 45

EF-hand-like motif found in dystrophin; Dystrophin is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscle. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It involves in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated abnormal cerebral diffusion and perfusion, acute Trypanosoma cruzi infection.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156630438  87 DQTTRLLFKLFDRGQTGVILLRSVEAALIALCGDTLSAKQRALFRLAESYSGNQESDRgsisrsaLRVLLEDLSQVPAVV 166
Cdd:cd16246   52 DMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASSTGFCDQRR-------LGLLLHDAIQIPRQL 124

                         90
                 ....*....|....*....
gi 156630438 167 QENHVFG--HAETAVSSCF 183
Cdd:cd16246  125 GEVASFGgsNIEPSVRSCF 143

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.

                         10        20        30
                 ....*....|....*....|....*....|
gi 156630438 226 VHCHACKAfPITGLRYRCLKCLNVHLCQSC 255
Cdd:cd02340    1 VICDGCQG-PIVGVRYKCLVCPDYDLCESC 29

EF-hand-like motif found in alpha-dystrobrevin; Alpha-dystrobrevin, also termed dystrobrevin alpha (DTN-A), or dystrophin-related protein 3 (DRP-3), is the mammalian ortholog of the Torpedo 87 kDa postsynaptic protein that tightly associates with dystrophin. It is a cytoplasmic protein expressed predominantly in skeletal muscle, heart, lung, and brain. Alpha-dystrobrevin has been implicated in the regulation of acetylcholine receptor (AChR) aggregate density and patterning. It is also essential in the pathogenesis of dystrophin-dependent muscular dystrophies. It plays a critical role in the full functionality of dystrophin through increasing dystrophin's binding to the dystrophin-glycoprotein complex (DGC), and provides protection during cardiac stress. Alpha-dystrobrevin binds to the intermediate filament proteins syncoilin and beta-synemin, thereby linking the dystrophin-associated protein complex (DAPC) to the intermediate filament network. Moreover, alpha-dystrobrevin involves in cell signaling via interaction with other proteins such as syntrophin, a modular adaptor protein that coordinates the assembly of the signaling proteins nitric oxide synthase, stress-activated protein kinase-3, and Grb2 to the DAPC. Furthermore, alpha-dystrobrevin plays an important role in muscle function, as well as in nuclear morphology maintenance through specific interaction with the nuclear lamina component lamin B1. In addition, alpha-dystrobrevin is required in dystrophin-associated protein scaffolding in brain. Absence of glial alpha-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. Alpha-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, alpha-dystrobrevin contain two syntrophin binding sites (SBSs).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156630438  39 DLRPILNTLWSSGESTISLAQEDVQQHLEELFRSISPELPDQAVTE---ATDQTTRLLFKL----FDRGQTGVILLRSVE 111
Cdd:cd16249    1 DIWNIIEALRENALNNLDPNTELNVARLEAVLSTIFYQLNKRMPTThqiNVEQSISLLLNFllaaFDPEGHGKISVFAVK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156630438 112 AALIALCGDTLSAKQRALFrlaesysgNQESD-RGSISRSALRVLLEDLSQVPAVVQENHVFGHAETAVSSCF 183
Cdd:cd16249   81 MALATLCGGKIMDKLRYIF--------SMISDsNGVMVYGRYDQFLREVLKLPTAVFEGPSFGYTEQSARSCF 145

EF-hand-like motif found in beta-dystrobrevin; Beta-dystrobrevin, also termed dystrobrevin beta (DTN-B), is a dystrophin-related protein that is restricted to non-muscle tissues and is abundantly expressed in brain, lung, kidney, and liver. It may be involved in regulating chromatin dynamics, possibly playing a role in neuronal differentiation, through the interactions with the high mobility group HMG20 proteins iBRAF/HMG20a and BRAF35 /HMG20b. It also binds to and represses the promoter of synapsin I, a neuronal differentiation gene. Moreover, beta-dystrobrevin functions as a kinesin-binding receptor involved in brain development via the association with the extracellular matrix components pancortins. Furthermore, beta-dystrobrevin binds directly to dystrophin and is a cytoplasmic component of the dystrophin-associated glycoprotein complex, a multimeric protein complex that links the extracellular matrix to the cortical actin cytoskeleton and acts as a scaffold for signaling proteins such as protein kinase A. Absence of alpha- and beta-dystrobrevin causes cerebellar synaptic defects and abnormal motor behavior. Beta-dystrobrevin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, beta-dystrobrevin contain two syntrophin binding sites (SBSs).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156630438  44 LNTLWSSGESTISLAQEDVQQHLEELFRSIsPELPDQAVTEATDQTTRLLFKLFDRGQTGVILLRSVEAALIALCGDTLS 123
Cdd:cd16250   14 LNTLDHSTEISVSRLETIISSIYYQLNKRL-PSTHQISVEQSISLLLNFMIAAYDSEGHGKLTVFSVKAMLATMCGGKIL 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156630438 124 AKQRALFrlaesysgNQESD-RGSISRSALRVLLEDLSQVPAVVQENHVFGHAETAVSSCF 183
Cdd:cd16250   93 DKLRYTF--------SQMSDsNGLMIFLKFDQFLREVLKLPTAVFEGPSFGYTEHSVRTCF 145