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 195927059  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGI 161
Cdd:cd08707    1 LHSLLDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMSDSEEKRSKLAKAIYRRYIKDNGIVSRQLKPATKSFIKECI 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 195927059 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 195927059   10 LPDPSSSFREDAPRPPVPGEEGETPPCQPG-------VGKGQVTKPMPVSSNTRRNEDGLG-EPEGRASPDSPL 75
Cdd:pfam16646   2 LPDGGGSFREDAPRPPVPGEEGEVPGCGPQhgsfgpsSKKEALKKEASVASTPRRNEDGLGeEPEGSASPDPPL 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 195927059  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGI 161
Cdd:cd08707    1 LHSLLDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMSDSEEKRSKLAKAIYRRYIKDNGIVSRQLKPATKSFIKECI 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 195927059 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 195927059    81 SLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMnLKDTKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDG 160
Cdd:smart00315   1 SLESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKKA-EDDEERIAKAREIYDKFLSPNAPKEVNLDSDLREKIEEN 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 195927059   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 195927059  763 ELVVTYFFCGEEIPYRRML--KAQSLTLGHFKEQLSKKGNYRYYFKKASDEFacGAVFEEIWEDETVLPMYEGRILGKV 839
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 195927059  12 DPSSSFREDAPRPPVPGEEGETPPCQPGVG------KGQVTKPMPVSSNTRRNEDGLG-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 195927059  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGI 161
Cdd:cd08707    1 LHSLLDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMSDSEEKRSKLAKAIYRRYIKDNGIVSRQLKPATKSFIKECI 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 195927059 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 195927059    81 SLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMnLKDTKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDG 160
Cdd:smart00315   1 SLESLLSDPIGRLLFREFLESEFSEENLEFWLAVEEFKKA-EDDEERIAKAREIYDKFLSPNAPKEVNLDSDLREKIEEN 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 195927059   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 195927059  763 ELVVTYFFCGEEIPYRRML--KAQSLTLGHFKEQLSKKGNYRYYFKKASDEFacGAVFEEIWEDETVLPMYEGRILGKV 839
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 195927059  86 LGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGIKKQQ 165
Cdd:cd07440    1 LRDPYGLEYFRQFLKSEHCEENLEFWLAVEKFKKTTSSDEELKSKAKEIYDKYISKDAPKEINIPESIREEIEENLEEPY 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 195927059 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 195927059  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRvAKAIYKRYIENNSIVSKQLKPATKTYIRDGI 161
Cdd:cd08713    1 LEKLLLHKYGLAVFRAFLQTEFSEENLEFWLACEEYKKIKSQSKMASR-AKKIFAEYIAIQSCKEVNLDSYTREHTKENL 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 195927059 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 195927059  85 LLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRvAKAIYKRYIENNSIVSKQLKPATKTYIRDGIkkQ 164
Cdd:cd08709    4 LLASKYGVAAFRAFLKSEFSEENIEFWLACEDFKKTKSPQKLTSK-AKKIYTDFIEKEAPKEINIDFQTKTLIAQNI--Q 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 195927059 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 195927059  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNlkdTKTLRV-AKAIYKRYIENNSIvsKQLKPATKTyiRDG 160
Cdd:cd08715    1 LEKLLASQTGQNVFRSFLKSEFSEENIEFWLACEDYKKTE---SDLLPCkAEEIYKEFVQSDAA--KQINIDFRT--RES 73

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 195927059 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 195927059  433 EDPQTILDDHLSRVLKTPGCQSPgvGRYSPRSRSPD 468
Cdd:pfam08833   1 DNPQSILDEHVSRVWKTPGCQSP--GRHSPRSRSPD 34

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 195927059  76 TRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNlKDTKTLRVAKAIYKRYIENNSIVSKQLKPATKT 155
Cdd:cd08711    6 TRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTR-STAKLVSKAHRIFEEFVDVQAPREVNIDFQTRE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 195927059 156 YIRDGIKKQQIDSimFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08711   85 ATRKNLQEPSLTC--FDQAQGKVHSLMEKDSYPRFLRSKMYLD 125

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 195927059  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDtKTLRVAKAIYKRYIENNSivSKQLKPATKTYIRDGI 161
Cdd:cd08741    1 LENLLEDPEGVKRFREFLKKEFSEENVLFWLACEDFKKMQDKT-QMQEKAKEIYMTFLSSKA--SSQVNVEGQSRLNEKI 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 195927059 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 195927059  55 TRRNED------------GLGEPEGRASPDSPLTR---WTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQ 119
Cdd:cd08746   12 TVRNQEdernrrtsyefrAEGIPNCEESPKPTLEEvcaWGQSFDKLMLTPAGRNAFREFLRTEFSEENMLFWMACEELKK 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 195927059 120 MNLKDTKTLRvAKAIYKRYIennSIVSKQlKPATKTYIRDGIKKQQID--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 195927059  72 DSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTL-RVAKAIYKRYIENNSI----VS 146
Cdd:cd08743    1 EKSVASWAVSFERLLQDPLGVEYFTEFLKKEFSAENVNFWKACERFQQIPASDTQQLaQEARKIYNEFLSSSSQspvnID 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 195927059 147 KQlkpatkTYI-RDGIKKQQIDsiMFDQAQTEIQSVMEENAYQMFLTSDIYLEYVRS 202
Cdd:cd08743   81 QQ------AWIgEDMLATPSPD--MFRAQQLQIFNLMKFDSYARFVKSPLYQDCLLA 129

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 195927059  78 WTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRvAKAIYKRYIennSIVSKQlKPATKTYI 157
Cdd:cd08744    1 WSQNFDKMMKTPAGRNLFREFLRTEYSEENLLFWLACEDLKKEQNKKVIEEK-ARLIYEDYI---SILSPK-EVSLDSRV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 195927059 158 RDGIKKQQID--SIMFDQAQTEIQSVMEENAYQMFLTSDIY 196
Cdd:cd08744   76 REVINRNLLDpnPHMYEDAQLQIYTLMHRDSFPRFLNSQIY 116

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 195927059  82 LHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNlKDTKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGI 161
Cdd:cd08717    1 LDKLLQNSYGLASFKSFLKSEFSEENIEFWEACEDYKKTK-SPLKMATKAKKIYEEFIQTEAPKEVNIDHFTKDVTMKNL 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 195927059 162 KKQQIDSimFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08717   80 VEPSSSS--FDLAQKRIFALMEKDSLPRFVRSEFYQE 114

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 195927059  91 GAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKtLRVAKAIYKRYIENNSIVSKQL-KPATKTYIRDgikKQQIDSI 169
Cdd:cd08716   10 GPIIYATYLKTEHSDENIEFWLACETYKKIASQRKR-ISMARKLFASYIQPQAPREINIdSPTRKAIIRN---IQEPTQS 85

                         90       100
                 ....*....|....*....|....*..
gi 195927059 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 195927059  85 LLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRV-AKAIYKRYIENNSIVSKQLKPATKtYIRDGIKK 163
Cdd:cd08742    4 LLQDPVGVRYFSEFLRKEFSEENILFWQACEYFNHVPAHDKKELSYrAREIFSKFLCSKATTPVNIDSQAQ-LADDILNA 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 195927059 164 QQIDsiMFDQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08742   83 PHPD--MFKEQQLQIFNLMKFDSYTRFLKSPLYQE 115

Regulator of G protein signaling (RGS) domain found in the Sorting Nexin14 (SNX14) protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the SNX14 (Sorting Nexin14) 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. SNX14 is believed to regulates membrane trafficking in motor neurons.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195927059  86 LGDQDGAYLFRTFLEREKCVDTLDFWFACNGF--RQMNLKDTKTLRV-----AKAIYKRYIENNSIVSKQLKPATKTYIR 158
Cdd:cd08722    2 LDDQRLLFPFMQFLKEEGAVHLLQFCLTVEDFnrRILNPDLTDEEKQslhkeAQEIYKTYFLPEAPDRIHFPPDIVEEIK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 195927059 159 D-------GIKKQQIDSIMFdQAQTEIQSVMEENAYQMFLTSDIYLE 198
Cdd:cd08722   82 QileggpeKIVKLRTSRPLF-EAYEHVYSLLESVFCPLFCHSDEYFI 127

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 195927059  88 DQDGAYLFRTFLEREKCVDTLDFWFACNGFRQmNLKDTKTLRVAKAIYKRYIENNS-----IVSKQLKPATKTYIRDGIK 162
Cdd:cd08734    1 DPNTSPLFGFSAESDFSGENLSFLTLVKEYKR-LSNPAEKFTLASKIYKEFISSESpfqinISSAMLRRLDNDFELLTGA 79

                         90       100
                 ....*....|....*....|....*....
gi 195927059 163 KQQIDSIMFDQAQTEIQSVMEENAYQMFL 191
Cdd:cd08734   80 FANVDSGLNTPFNEEISKIEASDLYPAFV 108