Regulator of G protein signaling (RGS) domain found in the RGS7 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS7 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Other members of the R7 subfamily (Neuronal RGS) include: RGS6, RGS9, and RGS11, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. R7 RGS proteins are key modulators of the pharmacological effects of drugs involved in the development of tolerance and addiction. In addition, RGS7 was found to bind a component of the synaptic fusion complex, snapin, and some other proteins outside of G protein signaling pathways.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 233 RVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIKEVPSRVQEIWQEFLAPGAPSAINLDSKSYD 312
Cdd:cd08738     1 RVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIREVPSRVQEIWQEFLAPGAPSAINLDSKSYD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1765945278 313 KTTQNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 353
Cdd:cd08738    81 KTTQNVKDPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 121

Regulator of G-protein signalling DHEX domain; This domain is found in RGS9 (Class C) regulator of G-protein signalling (RGS) protein present in Mus musculus. RGS proteins attenuate heterotrimeric G-protein signalling by enhancing the intrinsic GTPase activity of G-alpha subunits and are vital for proper signal transduction kinetics. The domain is referred to as DEP helical extension (DHEX) because it is located next to N-terminal Dishevelled/Egl-10/Pleckstrin homology (DEP) domain. Both the DEP and DHEX domains are necessary, but not sufficient, to bind anchoring proteins such as RGS9 anchor protein. DHEX has no close structural homologs. This domain is also found in regulator of G-protein signaling 7 (RGS7), the crystal structure of which has been solved.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1765945278  71 FSCKQKHKQSEslVDKKRDKIERKILDSQERAFWDVHRPVPGCVNTTEVDI 121
Cdd:pfam18148  52 FIIMQAEEQYK--VGKERNKADRYILDSQERAFWLVHRPPPGQVNVLEYGI 100

Regulator of G protein signaling (RGS) domain found in the RGS7 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS7 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Other members of the R7 subfamily (Neuronal RGS) include: RGS6, RGS9, and RGS11, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. R7 RGS proteins are key modulators of the pharmacological effects of drugs involved in the development of tolerance and addiction. In addition, RGS7 was found to bind a component of the synaptic fusion complex, snapin, and some other proteins outside of G protein signaling pathways.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 233 RVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIKEVPSRVQEIWQEFLAPGAPSAINLDSKSYD 312
Cdd:cd08738     1 RVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIREVPSRVQEIWQEFLAPGAPSAINLDSKSYD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1765945278 313 KTTQNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 353
Cdd:cd08738    81 KTTQNVKDPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 121

Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278  242 DEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKK-RPIKEVPSRVQEIWQEFLAPGAPSAINLDSKSYDKTTQNVK- 319
Cdd:smart00315   3 ESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKKaEDDEERIAKAREIYDKFLSPNAPKEVNLDSDLREKIEENLEs 82

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1765945278  320 -EPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQEL 354
Cdd:smart00315  83 eEPPPDLFDEAQREVYELLEKDSFPRFLESDYYLRF 118

GGL domain; G-protein gamma like domains (GGL) are found in the gamma subunit of the heterotrimeric G protein complex and in regulators of G protein signaling (RGS) proteins. It is also found fused to an inactive Galpha in the Dictyostelium protein gbqA. G-gamma likely shares a common origin with the helical N-terminal unit of G-beta. All organizms that posses a G-beta possess a G-gamma.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765945278 163 DELQQQIKYWQIQLDRHRLKMSKVADSLLSYTEQYLEYDPFL----LPPDPSNPWLSDDTTFWEL 223
Cdd:pfam00631   5 LKLKREIEQLREELKRERIKVSKACEELIDYCEQRSTKDPLLpgvwGPPAGENPWREDDGCCWIL 69

Regulator of G-protein signalling DHEX domain; This domain is found in RGS9 (Class C) regulator of G-protein signalling (RGS) protein present in Mus musculus. RGS proteins attenuate heterotrimeric G-protein signalling by enhancing the intrinsic GTPase activity of G-alpha subunits and are vital for proper signal transduction kinetics. The domain is referred to as DEP helical extension (DHEX) because it is located next to N-terminal Dishevelled/Egl-10/Pleckstrin homology (DEP) domain. Both the DEP and DHEX domains are necessary, but not sufficient, to bind anchoring proteins such as RGS9 anchor protein. DHEX has no close structural homologs. This domain is also found in regulator of G-protein signaling 7 (RGS7), the crystal structure of which has been solved.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1765945278  71 FSCKQKHKQSEslVDKKRDKIERKILDSQERAFWDVHRPVPGCVNTTEVDI 121
Cdd:pfam18148  52 FIIMQAEEQYK--VGKERNKADRYILDSQERAFWLVHRPPPGQVNVLEYGI 100

Regulator of G protein signaling (RGS) domain found in the RGS7 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS7 protein, a member of R7 subfamily of the RGS protein family. RGS is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Other members of the R7 subfamily (Neuronal RGS) include: RGS6, RGS9, and RGS11, all of which are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes such as vision and motor control. Additionally they have been implicated in many neurological conditions such as anxiety, schizophrenia, and drug dependence. R7 RGS proteins are key modulators of the pharmacological effects of drugs involved in the development of tolerance and addiction. In addition, RGS7 was found to bind a component of the synaptic fusion complex, snapin, and some other proteins outside of G protein signaling pathways.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 233 RVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIKEVPSRVQEIWQEFLAPGAPSAINLDSKSYD 312
Cdd:cd08738     1 RVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIREVPSRVQEIWQEFLAPGAPSAINLDSKSYD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1765945278 313 KTTQNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 353
Cdd:cd08738    81 KTTQNVKDPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 121

Regulator of G protein signaling (RGS) domain found in the R7 subfamily of proteins; The RGS (Regulator of G-protein Signaling) domain is an essential part of the R7 (Neuronal RGS) protein subfamily of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The R7 subfamily includes RGS6, RGS7, RGS9, and RGS11, all of which, in humans, are expressed predominantly in the nervous system, form an obligatory complex with G-beta-5, and play important roles in the regulation of crucial neuronal processes. In addition, R7 proteins were found to bind many other proteins outside of the G protein signaling pathways including: m-opioid receptor, beta-arrestin, alpha-actinin-2, NMDAR, polycystin, spinophilin, guanylyl cyclase, among others.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 233 RVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIKEVPSRVQEIWQEFLAPGAPSAINLDSKSYD 312
Cdd:cd08705     1 RVKRWGFSFSELLKDPVGREQFLKFLEKEFSGENLRFWEACQDLKYGPQSQVPEKVQEIYQEFLAPGAPSWINIDSKTME 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1765945278 313 KTTQNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 353
Cdd:cd08705    81 ITLKNLKDPHRYTFDAAQEHIYMLMKKDSYPRFLRSDIYKE 121

Regulator of G protein signaling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 242 DEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKK-RPIKEVPSRVQEIWQEFLAPGAPSAINLDSKSYDKTTQNV-K 319
Cdd:pfam00615   3 DSLLEDQPGRRLFRQFLESEFSEENLEFWLACEEFKKaDPDEERLKKAKEIYNEFLAPGSPKEINLDSDLREEIRENLeK 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1765945278 320 EPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQEL 354
Cdd:pfam00615  83 EPTRDLFDEAQAEVYELMEKDSYPRFLKSPLYLRL 117

Regulator of G protein signalling domain; RGS family members are GTPase-activating proteins for heterotrimeric G-protein alpha-subunits.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278  242 DEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKK-RPIKEVPSRVQEIWQEFLAPGAPSAINLDSKSYDKTTQNVK- 319
Cdd:smart00315   3 ESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKKaEDDEERIAKAREIYDKFLSPNAPKEVNLDSDLREKIEENLEs 82

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1765945278  320 -EPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQEL 354
Cdd:smart00315  83 eEPPPDLFDEAQREVYELLEKDSFPRFLESDYYLRF 118

Regulator of G protein signaling (RGS) domain found in the RGS20 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS20 protein (also known as RGSZ1), a member of the RZ subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of G-protein signaling is controlled by the RGS domain, which accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP resulting in reassociation of the alpha-subunit with the beta-gamma-dimer and inhibition of downstream activity. As a major G-protein regulator, the RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The RZ subfamily of RGS proteins include RGS17, RGS19 (former GAIP), and the splice variant of RGS20, Ret-RGS. RGS20 is expressed exclusively in brain, with the highest concentrations in the temporal lobe and the caudate nucleus and may play a role in signaling regulation in these brain regions. RGS20 acts as a GAP of both G-alpha-z and G-alpha-I and controls signaling in the mu opioid receptor pathway.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 224 EASKEPSQQRVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIKEV-PSRVQEIWQEFLAPGAPS 302
Cdd:cd08746    37 EESPKPTLEEVCAWGQSFDKLMLTPAGRNAFREFLRTEFSEENMLFWMACEELKKEANKSViEEKARIIYEDYISILSPK 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1765945278 303 AINLDSKSYDKTTQNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 353
Cdd:cd08746   117 EVSLDSRVREVINRNMLEPSQHTFDDAQLQIYTLMHRDSYPRFMNSAIYKN 167

Regulator of G protein signaling (RGS) domain found in the RGS19 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS19 protein (also known as GAIP), a member of the RZ subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of G-protein signaling is controlled by RGS domains, which accelerate GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, resulting in a reassociation of the alpha-subunit with the beta-gamma-dimer and an inhibition of downstream activity. As a major G-protein regulator, the RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The RZ subfamily of RGS proteins includes RGS17, RGS20, and its splice variant Ret-RGS. RGS19 participates in regulation of dopamine receptor D2R and D3R, as well as beta-adrenergic receptors .

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 237 WGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIKE-VPSRVQEIWQEFLAPGAPSAINLDSKSYDKTT 315
Cdd:cd08745     1 WAQSFDKLMKSPAGRNVFREFLRTEYSEENMLFWLACEELKAEANKHvIDEKARLIYEDYISILSPKEVSLDSRVREGIN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1765945278 316 QNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQ 352
Cdd:cd08745    81 RKMQEPSSHTFDDAQLQIYTLMHRDSYPRFLNSPIYK 117

Regulator of G protein signaling (RGS) domain found in the RGS5 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS5 protein. RGS5 is member of the R4/RGS subfamily of the RGS family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G-alpha subunit which leads to G protein deactivation and promotes desensitization. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. Two splice isoforms of RGS5 has been found: RGS5L (long) which is expressed in smooth muscle cells (pericytes) and heart and RGS5S (short) which is highly expressed in the ciliary body of the eye, kidney, brain, spleen, skeletal muscle, and small intestine. Outside of the GPCR pathway, RGS5 interacts with the 14-3-3 protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 241 MDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKK--RPIKeVPSRVQEIWQEFLAPGAPSAINLDSKSYDKTTQNV 318
Cdd:cd08717     1 LDKLLQNSYGLASFKSFLKSEFSEENIEFWEACEDYKKtkSPLK-MATKAKKIYEEFIQTEAPKEVNIDHFTKDVTMKNL 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1765945278 319 KEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 353
Cdd:cd08717    80 VEPSSSSFDLAQKRIFALMEKDSLPRFVRSEFYQE 114

Regulator of G protein signaling (RGS) domain found in the RGS21 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part RGS21 protein, a member of RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, apoptosis, and cell proliferation, as well as modulation of cardiac development. RGS21 is a member of the R4/RGS subfamily and its mRNA was detected only in sensory taste cells that express sweet taste receptors and the taste G-alpha subunit, gustducin, suggesting a potential role in regulating taste transduction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 245 LKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIK-EVPSRVQEIWQEFLAPGAPSAINLDSKSYDKTTQNVKEPGR 323
Cdd:cd08723     2 LANQAGLDAFRTFLKSEFSEENVEFWLACEDFKKTKSStEIALKAQMIYSEFIQADAPKEINIDFHTRDLISQNISEPTL 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1765945278 324 YTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 353
Cdd:cd08723    82 KCFDEAQSLIYCLMAKDSFPRFLKSEVYKK 111

Regulator of G protein signaling (RGS) domain found in the RZ protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RZ subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of G-protein signaling is controlled by RGS domains, which accelerate GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in reassociation of the alpha-subunit with the beta-gamma-dimer and inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The RZ subfamily of RGS proteins includes RGS17, RGS19 (former GAIP), RGS20, and its splice variant Ret-RGS.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 237 WGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIKE-VPSRVQEIWQEFLAPGAPSAINLDSKSYDKTT 315
Cdd:cd08718     1 WAQSFDKLMKSPAGRNVFREFLRTEYSEENMLFWLACEELKKEANKHvIEEKARLIYEDYISILSPKEVSLDSRVREVIN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1765945278 316 QNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQ 352
Cdd:cd08718    81 RNMLEPSPHTFDDAQLQIYTLMHRDSYPRFLNSAIYK 117

Regulator of G protein signaling (RGS) domain found in the RGS8 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS8 protein. RGS8 is a member of R4/RGS subfamily of RGS family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha subunits. The RGS domain controls G-protein signaling by accelerating the GTPase activity of the G-alpha subunit which leads to G protein deactivation and promotes desensitization. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS8 is involved in G-protein-gated potassium channels regulation and predominantly expressed in the brain. RGS8 also is selectively expressed in the hematopoietic system (NK cells).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 230 SQQRVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKK-RPIKEVPSRVQEIWQEFLAPGAPSAINLDS 308
Cdd:cd08711     1 STEEATRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKtRSTAKLVSKAHRIFEEFVDVQAPREVNIDF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1765945278 309 KSYDKTTQNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 353
Cdd:cd08711    81 QTREATRKNLQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLD 125

Regulator of G protein signaling (RGS) domain found in the RGS17 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS17 protein, a member of the RZ subfamily of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, the RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins play critical regulatory roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of the G-protein signaling controlled by the RGS domain, which accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, results in reassociation of the alpha-subunit with the beta-gamma-dimer and inhibition of downstream activity. The RZ subfamily of RGS proteins includes RGS19 (former GAIP), RGS20, and its splice variant Ret-RGS. RGS17 is a relatively non-selective GAP for G-alpha-z and other G-alpha-i/o proteins. RGS17 blocks dopamine receptor-mediated inhibition of cAMP accumulation; it also blocks thyrotropin releasing hormone-stimulated Ca++ mobilization. RGS17, like other members of RZ subfamily, can act either as a GAP or as G-protein effector antogonist.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 237 WGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIKEV-PSRVQEIWQEFLAPGAPSAINLDSKSYDKTT 315
Cdd:cd08744     1 WSQNFDKMMKTPAGRNLFREFLRTEYSEENLLFWLACEDLKKEQNKKViEEKARLIYEDYISILSPKEVSLDSRVREVIN 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1765945278 316 QNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQ 352
Cdd:cd08744    81 RNLLDPNPHMYEDAQLQIYTLMHRDSFPRFLNSQIYK 117

Regulator of G protein signaling (RGS) domain found in the RGS14 protein; RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS14 protein. RGS14 is a member of the RA/RGS subfamily of RGS proteins family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS14 belong to the R12 RGS subfamily, which includes RGS10 and RGS12, all of which are highly selective for G-alpha-i1 over G-alpha-q. RGS14 binds and regulates the subcellular localization and activities of H-Ras and Raf kinases in cells and thereby integrates G protein and Ras/Raf signaling pathways.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 231 QQRVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIKEVPSRVQE---IWQEFLAPGAPSAINLD 307
Cdd:cd08743     1 EKSVASWAVSFERLLQDPLGVEYFTEFLKKEFSAENVNFWKACERFQQIPASDTQQLAQEarkIYNEFLSSSSQSPVNID 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1765945278 308 SKSYdKTTQNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQELLQA 357
Cdd:cd08743    81 QQAW-IGEDMLATPSPDMFRAQQLQIFNLMKFDSYARFVKSPLYQDCLLA 129

G protein gamma subunit-like motifs;

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1765945278  163 DELQQQIKYWQIQLDRHRLKMSKVADSLLSYTEQYLEYDPFLLPPDPS-NPWLSDDTTFWEL 223
Cdd:smart00224   2 DQLRKEVEQLRKELSRERIKVSKAAEELLAYCEQHAEEDPLLTGPPPSkNPFIEDKTSCWIL 63

Regulator of G protein signaling (RGS) domain found in the RGS12 protein; RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS12 protein. RGS12 is a member of the RA/RGS subfamily of RGS proteins family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS12 belong to the R12 RGS subfamily, which includes RGS10 and RGS14, all of which are highly selective for G-alpha-i1 over G-alpha-q. RGS12 exist in multiple splice variants: RGS12s (short) contains the core RGS/RBD/GoLoco domains, while RGS12L (long) has additional N-terminal PDZ and PTB domains. RGS12 splice variants show distinct expression patterns, suggesting that they have discrete functions during mouse embryogenesis. RGS12 also may play a critical role in coordinating Ras-dependent signals that are required for promoting and maintaining neuronal differentiation.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 245 LKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPI---KEVPSRVQEIWQEFLAPGAPSAINLDSKSyDKTTQNVKEP 321
Cdd:cd08742     5 LQDPVGVRYFSEFLRKEFSEENILFWQACEYFNHVPAhdkKELSYRAREIFSKFLCSKATTPVNIDSQA-QLADDILNAP 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1765945278 322 GRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 353
Cdd:cd08742    84 HPDMFKEQQLQIFNLMKFDSYTRFLKSPLYQE 115

G protein gamma subunit-like motifs, the alpha-helical G-gamma chain dimerizes with the G-beta propeller subunit as part of the heterotrimeric G-protein complex; involved in signal transduction via G-protein-coupled receptors

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1765945278 163 DELQQQIKYWQIQLDRHRLKMSKVADSLLSYTEQYLEYDPFLLPPD-PSNPWLSDD 217
Cdd:cd00068     2 DQLKKEVEQLRKELSRERLKVSKAAAELLKYCEQNAENDPLLTGPPsPSNPWIEKK 57

Regulator of G protein signaling (RGS) domain found in the FLBA (Fluffy Low BrlA) protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the FLBA (Fluffy Low BrlA) protein. FLBA is a member of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins play a critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of the G-protein signaling controlled by the RGS domain accelerates the GTPase activity of the alpha subunit by hydrolysis of GTP to GDP which results in reassociation of the alpha-subunit with the beta-gamma-dimer and thereby inhibition of downstream activity. As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes. The RGS domain of the FLBA protein antagonizes G protein signaling to block proliferation and allow development. It is required for control of mycelial proliferation and activation of asexual sporulation in yeast.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 241 MDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKK------RPIKEVPSRVQE-------------IWQEFLAPGAP 301
Cdd:cd08708     2 LDKILKDPGLRYLFREHLEKEFCEENLSFYLEVKEFLKkmtilsKLLDFKSSQAADedldreslaqayhIYNTYLAPGSP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1765945278 302 SAINLDSKSYDKTTQNVKEPGR--------------YTFEDAQEHIYK-LMKSDSYPRFIRSSAY 351
Cdd:cd08708    82 CELNIDHNLRNRITTIMTEKIVgeddsmaeslqgveALFEEAQNAVFKpLMAGDSVPKFLKQPEY 146

Regulator of G protein signaling (RGS) domain found in the Sorting Nexin 13 (SNX13) protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX13 (Sorting Nexin 13) protein, a member of the RGS protein family. They are a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. The RGS-domain of SNX13 plays a major role through attenuation of Galphas-mediated signaling and regulates endocytic trafficking and degradation of the epidermal growth factor receptor. Snx13-null mice were embryonic lethal around midgestation which supports an essential role for SNX13 in mouse development and regulation of endocytosis dynamics.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 244 ALKDPVGREQFLKFLESEFSSENLRFWLAVEDLK-------------KRPIKEVPSRVQE--------IWQEFLAPGAPS 302
Cdd:cd08719     1 ILVNNVALSYFIDFMQSVGGQAYLFFWLTVEGYRvsaeqqlselhlrQRGGEHQRSDVYEmlraaalnIYDQYLSEKASP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1765945278 303 AINLDSKSYDKTTQ--NVKEPGRYTFEDAQEHIYKLMKSDS--YPRFIRSSAY 351
Cdd:cd08719    81 RVPLDDSLVKKLLNrlRNDTPSDLWFDDIQQKVFDIMQEDErfYPAFKKSPAY 133

Regulator of G protein signaling (RGS) domain found in the Axin protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the Axin protein. Axin is a member of the RA/RGS subfamily of the RGS protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). As a major G-protein regulator, RGS domain containing proteins are involved in many crucial cellular processes such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, and skeletal and muscle development. The RGS domain of Axin is specifically interacts with the heterotrimeric G-alpha12 protein, but not with closely related G-alpha13, and provides a unique tool to regulate G-alpha12-mediated signaling processes. The RGS domain of Axin also interacts with the tumor suppressor protein APC (Adenomatous Polyposis Coli) in order to control the cytoplasmic level of the proto-oncogene, beta-catenin.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 245 LKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKR-PIKEVPSRV-QEIWQEFLAPGAPSAINL--DSKSYDKTTQNVKE 320
Cdd:cd08707     5 LDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMsDSEEKRSKLaKAIYRRYIKDNGIVSRQLkpATKSFIKECIKKQQ 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1765945278 321 PGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 353
Cdd:cd08707    85 LDPAMFDQAQTEIQTTMEENTYPSFLKSDIYLE 117

Regulator of G protein signaling domain (RGS) found in G protein-coupled receptor kinase 5 (GRK5); The RGS domain is an essential part of the GRK5 (G protein-coupled receptor kinase 5) protein, a membrane-associated serine/threonine protein kinases which phosphorylates G protein-coupled receptors (GPCRs) upon agonist stimulation. This phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events. GRK5 is a member of the GRK kinase family which include three major subfamilies: the GRK4 subfamily (GRK4, GRK5 and GRK6), the rhodopsin kinase or visual GRK subfamily (GRK1 and GRK7), and the beta-adrenergic receptor kinases subfamily (GRK2/GRK3). The RGS domain of the GRKs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 246 KDPVGREQFLKFLESEFSSEN-LRFWLAVEDLKKRPIKEVPSRVQEIWQEFLAPGAPSAINLDSKSYDKTTQN--VKEPG 322
Cdd:cd08752     7 KQPIGRLLFRQFCETRPGLECyIQFLDSVAEYEVTPDEKLGEKGKEIMTKYLTPKSPVFIPQVGQDLVSQTEEklLQKPC 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1765945278 323 RYTFEDAQEHIYKLMKSDSYPRFIRSSAYQELLQAK 358
Cdd:cd08752    87 KELFSACTQSVHDYLRGEPFHEYLDSMYFDRFLQWK 122

Uncharacterized Regulator of G protein Signaling (RGS) domain subfamily, child 4; These uncharacterized RGS-like domains consists largely of hypothetical proteins. The RGS domain is an essential part of the Regulator of G-protein Signaling (RGS) protein family, a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play an important role in neuronal signal modulation. Some RGS proteins are the principal elements needed for proper vision.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1765945278 265 ENLRFWLAVEDLKKRPIKEVPSRV---QEIWQEFLAPGAPSAINLDSKSYDKTTQNVKEPGRYT---FEDAQEHIYKLMK 338
Cdd:cd08732    38 EDDDFDEQVEELRYILDTDQILLKdqwRHIMNTYIHHDSPLQINLSHTMRKEIVEEDDNPNIHTpdlLLNAYNEVLRLLK 117

                          90       100
                  ....*....|....*....|..
gi 1765945278 339 SDSYPRFIRSSAYQELLQAKKK 360
Cdd:cd08732   118 ENFYPEFKNLPKYRKLKEEESK 139