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 1622880703  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDAKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGI 161
Cdd:cd08707     1 LHSLLDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMSDSEEKRSKLAKAIYRRYIKDNGIVSRQLKPATKSFIKECI 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622880703 162 KKQQIDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08707    81 KKQQLDPAMFDQAQTEIQTTMEENTYPSFLKSDIYLE 117

Axin-1 tankyrase binding domain; This is the N-terminal domain tankyrase binding domain of Axin-1.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622880703   9 RLPDPSSSFREDAPRPPVPGEEGETPPCQLG-------VGKGQVTKPVPVSSNTRRNEDGLG-EPEGRASPDSPL 75
Cdd:pfam16646   1 ALPDGGGSFREDAPRPPVPGEEGEVPGCGPQhgsfgpsSKKEALKKEASVASTPRRNEDGLGeEPEGSASPDPPL 75

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 1622880703  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDAKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGI 161
Cdd:cd08707     1 LHSLLDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMSDSEEKRSKLAKAIYRRYIKDNGIVSRQLKPATKSFIKECI 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622880703 162 KKQQIDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08707    81 KKQQLDPAMFDQAQTEIQTTMEENTYPSFLKSDIYLE 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 1622880703   81 SLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMnLKDAKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDG 160
Cdd:smart00315   1 SLESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKKA-EDDEERIAKAREIYDKFLSPNAPKEVNLDSDLREKIEEN 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622880703  161 IKKQQIDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLEY 199
Cdd:smart00315  80 LESEEPPPDLFDEAQREVYELLEKDSFPRFLESDYYLRF 118

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880703 782 ELVVTYFFCGEEIPYRRML--KAQSLTLGHFKEQLSKKGNYRYYFKKASDEFacGAVFEEIWEDETVLPMYEGRILGKV 858
Cdd:pfam00778   1 ETKVIYYLCDEPVPYRIKIhkPGGQITLGDFKELLPKKGNYRYFFKTLDPEF--GTVKEEITDDDDILPLWEGKIVAKV 77

Tankyrase binding N-terminal segment of axin; This N-terminal region of axin mediates interactions with the ankyrin-repeat clusters 2 and 3 of tankyrase, which controls the turnover of axin via poly-ADP-ribosylation. Axin functions as a negative regulator of the WNT signaling pathway.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880703  12 DPSSSFREDAPRPPVPGEEGETPPCQLGVG------KGQVTKPVPVSSNTRRNEDGLG-EPEGRASPDS 73
Cdd:cd11582     1 DPGSSFREDAPRPPVPGEEGELTPSDPRSSshsysnKSDSLKPEPSAATPRRIEAPLGfEPEGSASPTP 69

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 1622880703  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDAKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGI 161
Cdd:cd08707     1 LHSLLDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMSDSEEKRSKLAKAIYRRYIKDNGIVSRQLKPATKSFIKECI 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622880703 162 KKQQIDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08707    81 KKQQLDPAMFDQAQTEIQTTMEENTYPSFLKSDIYLE 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 1622880703   81 SLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMnLKDAKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDG 160
Cdd:smart00315   1 SLESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKKA-EDDEERIAKAREIYDKFLSPNAPKEVNLDSDLREKIEEN 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622880703  161 IKKQQIDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLEY 199
Cdd:smart00315  80 LESEEPPPDLFDEAQREVYELLEKDSFPRFLESDYYLRF 118

DIX domain; The DIX domain is present in Dishevelled and axin. This domain is involved in homo- and hetero-oligomerization. It is involved in the homo- oligomerization of mouse axin. The axin DIX domain also interacts with the dishevelled DIX domain. The DIX domain has also been called the DAX domain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880703 782 ELVVTYFFCGEEIPYRRML--KAQSLTLGHFKEQLSKKGNYRYYFKKASDEFacGAVFEEIWEDETVLPMYEGRILGKV 858
Cdd:pfam00778   1 ETKVIYYLCDEPVPYRIKIhkPGGQITLGDFKELLPKKGNYRYFFKTLDPEF--GTVKEEITDDDDILPLWEGKIVAKV 77

Regulator of G protein signaling (RGS) domain superfamily; 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 roles as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. While inactive, G-alpha-subunits bind GDP, which is released and replaced by GTP upon agonist activation. GTP binding leads to dissociation of the alpha-subunit and the beta-gamma-dimer, allowing them to interact with effectors molecules and propagate signaling cascades associated with cellular growth, survival, migration, and invasion. Deactivation of the G-protein signaling controlled by the RGS domain accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP, which results in the 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 such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. RGS proteins are also involved in apoptosis and cell proliferation, as well as modulation of cardiac development. Several RGS proteins can fine-tune immune responses, while others play important roles in neuronal signals modulation. Some RGS proteins are principal elements needed for proper vision.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880703  86 LGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDAKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGIKKQQ 165
Cdd:cd07440     1 LRDPYGLEYFRQFLKSEHCEENLEFWLAVEKFKKTTSSDEELKSKAKEIYDKYISKDAPKEINIPESIREEIEENLEEPY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622880703 166 IDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd07440    81 PDPDCFDEAQEHILNLLEKDSYPRFLKSDLYLK 113

Regulator of G protein signaling (RGS) domain found in the RGS3 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS3 protein. RGS3 is a 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). 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 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. RGS3 induces apoptosis when overexpressed and is involved in cell migration through interaction with the Ephrin receptor. RGS3 exits as several splice isoforms and interacts with neuroligin, estrogen receptor-alpha, and 14-3-3 outside of the GPCR pathways.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880703  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDAKTLRvAKAIYKRYIENNSIVSKQLKPATKTYIRDGI 161
Cdd:cd08713     1 LEKLLLHKYGLAVFRAFLQTEFSEENLEFWLACEEYKKIKSQSKMASR-AKKIFAEYIAIQSCKEVNLDSYTREHTKENL 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622880703 162 kkQQIDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08713    80 --QNPTRGCFDLAQKRIYGLMEKDSYPRFLRSDLYQD 114

Regulator of G protein signaling (RGS) domain found in the RGS2 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS2 protein. RGS2 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. RGS2 plays important roles in the regulation of blood pressure and the pathogenesis of human hypertension, as well as in bone formation in osteoblasts. Outside of the GPCR pathway RGS2 interacts with calmodulin, beta- COP, tubulin, PKG1-alpha, and TRPV6.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880703  85 LLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDAKTLRvAKAIYKRYIENNSIVSKQLKPATKTYIRDGIkkQ 164
Cdd:cd08709     4 LLASKYGVAAFRAFLKSEFSEENIEFWLACEDFKKTKSPQKLTSK-AKKIYTDFIEKEAPKEINIDFQTKTLIAQNI--Q 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622880703 165 QIDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08709    81 EATSGCFTAAQKRVYSLMENNSYPRFLESEFYQE 114

Regulator of G protein signaling (RGS) domain found in the RGS1 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS1 protein. RGS1 is a 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. RGS 1 is expressed predominantly in hematopoietic compartments, including T and B lymphocytes, and may play a major role in chemokine-mediated homing of lymphocytes to secondary lymphoid organs. In addition, RGS1 interacts with calmodulin and 14-3-3 protein outside of the GPCR pathway.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880703  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNlkdAKTLRV-AKAIYKRYIENNSIvsKQLKPATKTyiRDG 160
Cdd:cd08715     1 LEKLLASQTGQNVFRSFLKSEFSEENIEFWLACEDYKKTE---SDLLPCkAEEIYKEFVQSDAA--KQINIDFRT--RES 73

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622880703 161 IKKQQID--SIMFDQAQTEIQSVMEENAYQMFLTSDIYL 197
Cdd:cd08715    74 TAKKIKAptPTCFDEAQKVIYILMERDSYPRFLKSDIYL 112

Axin beta-catenin binding motif; This motif is found on the scaffolding protein Axin which is a component of the beta-catenin destruction complex. It competes with the tumour suppressor adenomatous polyposis coli protein (APC) for binding to beta-catenin.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622880703 451 EDPQTILDDHLSRVLKTPGCQSPgvGRYSPRSRSPD 486
Cdd:pfam08833   1 DNPQSILDEHVSRVWKTPGCQSP--GRHSPRSRSPD 34

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 1622880703  85 LLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDAKTLRvAKAIYKRYIENNSIVSKQLKPATKTYIRDGIKKQ 164
Cdd:cd08723     1 LLANQAGLDAFRTFLKSEFSEENVEFWLACEDFKKTKSSTEIALK-AQMIYSEFIQADAPKEINIDFHTRDLISQNISEP 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622880703 165 QIDSimFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08723    80 TLKC--FDEAQSLIYCLMAKDSFPRFLKSEVYKK 111

Regulator of G protein signaling (RGS) domain found in the RGS10 protein; RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS10 protein. RGS10 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. RGS10 belong to the R12 RGS subfamily, which includes RGS12 and RGS14, all of which are highly selective for G-alpha-i1 over G-alpha-q. RGS10 exists in 2 splice isoforms. RGS10A is specifically expressed in osteoclasts and is a key component in the RANKL signaling mechanism for osteoclast differentiation, whereas RGS10B expressed in brain and in immune tissues and has been implicated in diverse processes including: promoting of dopaminergic neuron survival via regulation of the microglial inflammatory response, modulation of presynaptic and postsynaptic G-protein signalling, as well as a possible role in regulation of gene expression.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880703  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDaKTLRVAKAIYKRYIENNSivSKQLKPATKTYIRDGI 161
Cdd:cd08741     1 LENLLEDPEGVKRFREFLKKEFSEENVLFWLACEDFKKMQDKT-QMQEKAKEIYMTFLSSKA--SSQVNVEGQSRLNEKI 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622880703 162 KKQQiDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08741    78 LEEP-HPLMFQKLQDQIFNLMKYDSYSRFLKSDLFLK 113

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 1622880703  55 TRRNED------------GLGEPEGRASPDSPLTR---WTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQ 119
Cdd:cd08746    12 TVRNQEdernrrtsyefrAEGIPNCEESPKPTLEEvcaWGQSFDKLMLTPAGRNAFREFLRTEFSEENMLFWMACEELKK 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622880703 120 MNLKDAKTLRvAKAIYKRYIennSIVSKQlKPATKTYIRDGIKKQQID--SIMFDQAQTEIQSVMEENAYQMFLTSDIY 196
Cdd:cd08746    92 EANKSVIEEK-ARIIYEDYI---SILSPK-EVSLDSRVREVINRNMLEpsQHTFDDAQLQIYTLMHRDSYPRFMNSAIY 165

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 1622880703  72 DSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKD-AKTLRVAKAIYKRYIENNSI----VS 146
Cdd:cd08743     1 EKSVASWAVSFERLLQDPLGVEYFTEFLKKEFSAENVNFWKACERFQQIPASDtQQLAQEARKIYNEFLSSSSQspvnID 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622880703 147 KQlkpatkTYI-RDGIKKQQIDsiMFDQAQTEIQSVMEENAYQMFLTSDIYLEYVRS 202
Cdd:cd08743    81 QQ------AWIgEDMLATPSPD--MFRAQQLQIFNLMKFDSYARFVKSPLYQDCLLA 129

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 1622880703  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNlKDAKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGI 161
Cdd:cd08717     1 LDKLLQNSYGLASFKSFLKSEFSEENIEFWEACEDYKKTK-SPLKMATKAKKIYEEFIQTEAPKEVNIDHFTKDVTMKNL 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622880703 162 KKQQIDSimFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08717    80 VEPSSSS--FDLAQKRIFALMEKDSLPRFVRSEFYQE 114

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 1622880703  78 WTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDAKTLRvAKAIYKRYIennSIVSKQlKPATKTYI 157
Cdd:cd08744     1 WSQNFDKMMKTPAGRNLFREFLRTEYSEENLLFWLACEDLKKEQNKKVIEEK-ARLIYEDYI---SILSPK-EVSLDSRV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622880703 158 RDGIKKQQID--SIMFDQAQTEIQSVMEENAYQMFLTSDIY 196
Cdd:cd08744    76 REVINRNLLDpnPHMYEDAQLQIYTLMHRDSFPRFLNSQIY 116

Regulator of G protein signaling (RGS) domain found in the RGS13 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS13 protein. RGS13 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. RGS13 is predominantly expressed in T and B lymphocytes and in mast cells, and plays a role in adaptive immune responses. RGS13 also found in Rgs13, which is also expressed in dendritic cells and in neuroendocrine cells of the thymus, gastrointestinal, and respiratory tracts. Outside of the GPCR pathway, RGS5 interacts with the PIP3 protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622880703  91 GAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDAKtLRVAKAIYKRYIENNSIVSKQL-KPATKTYIRDgikKQQIDSI 169
Cdd:cd08716    10 GPIIYATYLKTEHSDENIEFWLACETYKKIASQRKR-ISMARKLFASYIQPQAPREINIdSPTRKAIIRN---IQEPTQS 85

                          90       100
                  ....*....|....*....|....*..
gi 1622880703 170 MFDQAQTEIQSVMEENAYQMFLTSDIY 196
Cdd:cd08716    86 CFDEAQRIVYMHMERDSYPRFLESKFY 112

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 1622880703  85 LLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDAKTLRV-AKAIYKRYIENNSIVSKQLKPATKtYIRDGIKK 163
Cdd:cd08742     4 LLQDPVGVRYFSEFLRKEFSEENILFWQACEYFNHVPAHDKKELSYrAREIFSKFLCSKATTPVNIDSQAQ-LADDILNA 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622880703 164 QQIDsiMFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08742    83 PHPD--MFKEQQLQIFNLMKFDSYTRFLKSPLYQE 115

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 1622880703  77 RWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDAKTlRVaKAIYKRYIENNSIVSKQLKpaTKTY 156
Cdd:cd08738     4 RWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIREVPS-RV-QEIWQEFLAPGAPSAINLD--SKSY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622880703 157 IRDGIKKQQIDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08738    80 DKTTQNVKDPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQE 121

Uncharacterized Regulator of G protein Signaling (RGS) domain subfamily, child 1; 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. As a major G-protein regulator, the RGS domain containing proteins that are involved in many crucial cellular processes. 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 1622880703  88 DQDGAYLFRTFLEREKCVDTLDFWFACNGFRQmNLKDAKTLRVAKAIYKRYIENNS-----IVSKQLKPATKTYIRDGIK 162
Cdd:cd08734     1 DPNTSPLFGFSAESDFSGENLSFLTLVKEYKR-LSNPAEKFTLASKIYKEFISSESpfqinISSAMLRRLDNDFELLTGA 79

                          90       100
                  ....*....|....*....|....*....
gi 1622880703 163 KQQIDSIMFDQAQTEIQSVMEENAYQMFL 191
Cdd:cd08734    80 FANVDSGLNTPFNEEISKIEASDLYPAFV 108