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 768942821 116 LHSLLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKTSQ--EKRAKLAKAIYRKYIVDgSGIVSRQIKAATKSFIRDC 193
Cdd:cd08707    1 LHSLLDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMSDseEKRSKLAKAIYRRYIKD-NGIVSRQLKPATKSFIKEC 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 768942821 194 VGRPHPDPAMFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08707   80 IKKQQLDPAMFDQAQTEIQTTMEENTYPSFLKSDIYLE 117

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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942821  27 HFTEDAPRPPVPGEEGSDvdPPVQSSGTRPAALSQSLGYLSSSSSkmgdasshtlssssATPRRPDLDLGYEPEGSASPT 106
Cdd:cd11582    5 SFREDAPRPPVPGEEGEL--TPSDPRSSSHSYSNKSDSLKPEPSA--------------ATPRRIEAPLGFEPEGSASPT 68

                 .
gi 768942821 107 P 107
Cdd:cd11582   69 P 69

Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942821   525 PGCQSPGATNSTLGGGGRHSPpkssrsPDGGTGPPHypphrGGGHSLPAAGVKGTHHHKQIYHHRGREGQDEAGSRSQAN 604
Cdd:smart00157  18 PGQGSPGGNRYPPQGGGWGQP------HGGGWGQPH-----GGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTN 86

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 768942821   605 FmwngdpgrsRNYADCAGAGAVEG--VGYSKGSTLSR 639
Cdd:smart00157  87 M---------KHVAGAAAAGAVVGglGGYMLGSAMSR 114

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 768942821 116 LHSLLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKTSQ--EKRAKLAKAIYRKYIVDgSGIVSRQIKAATKSFIRDC 193
Cdd:cd08707    1 LHSLLDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMSDseEKRSKLAKAIYRRYIKD-NGIVSRQLKPATKSFIKEC 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 768942821 194 VGRPHPDPAMFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08707   80 IKKQQLDPAMFDQAQTEIQTTMEENTYPSFLKSDIYLE 117

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 768942821  803 TVAYYFCGEPIPYRT--SVKGRVVTLGQFKELLTKKGHYRFYFKKVSDEFDCgvVFEEVRDDDATLPIFEEKIIGKV 877
Cdd:pfam00778   3 KVIYYLCDEPVPYRIkiHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGT--VKEEITDDDDILPLWEGKIVAKV 77

Domain present in Dishevelled and axin; Domain of unknown function.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942821   799 CENMTVAYYFCGEPIPYRTSVKGR--VVTLGQFKELLTKKGhYRFYFKKVSDEFDcGVVFEEVRDDDATLPIFEEKIIGK 876
Cdd:smart00021   1 CSETKVIYHLDDEETPYLVKVPVPaeRVTLGDFKEVLTKKN-YKYYFKSMDDDFG-GVVKEEIRDDSARLPCFNGRVVSW 78

                   ....*
gi 768942821   877 VEKVD 881
Cdd:smart00021  79 LVSVE 83

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942821   28 FTEDAPRPPVPGEEGSdvdppVQSSGTRPAALSQSlgylssssskMGDASSHTLSSSSATPRRPDLDLGYEPEGSASPTP 107
Cdd:pfam16646   9 FREDAPRPPVPGEEGE-----VPGCGPQHGSFGPS----------SKKEALKKEASVASTPRRNEDGLGEEPEGSASPDP 73

                  ..
gi 768942821  108 PY 109
Cdd:pfam16646  74 PL 75

Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942821   525 PGCQSPGATNSTLGGGGRHSPpkssrsPDGGTGPPHypphrGGGHSLPAAGVKGTHHHKQIYHHRGREGQDEAGSRSQAN 604
Cdd:smart00157  18 PGQGSPGGNRYPPQGGGWGQP------HGGGWGQPH-----GGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTN 86

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 768942821   605 FmwngdpgrsRNYADCAGAGAVEG--VGYSKGSTLSR 639
Cdd:smart00157  87 M---------KHVAGAAAAGAVVGglGGYMLGSAMSR 114

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 768942821 116 LHSLLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKTSQ--EKRAKLAKAIYRKYIVDgSGIVSRQIKAATKSFIRDC 193
Cdd:cd08707    1 LHSLLDDQDGIELFRTYLEQEGCADLLDFWFACNGFRKMSDseEKRSKLAKAIYRRYIKD-NGIVSRQLKPATKSFIKEC 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 768942821 194 VGRPHPDPAMFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08707   80 IKKQQLDPAMFDQAQTEIQTTMEENTYPSFLKSDIYLE 117

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 768942821  803 TVAYYFCGEPIPYRT--SVKGRVVTLGQFKELLTKKGHYRFYFKKVSDEFDCgvVFEEVRDDDATLPIFEEKIIGKV 877
Cdd:pfam00778   3 KVIYYLCDEPVPYRIkiHKPGGQITLGDFKELLPKKGNYRYFFKTLDPEFGT--VKEEITDDDDILPLWEGKIVAKV 77

Domain present in Dishevelled and axin; Domain of unknown function.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942821   799 CENMTVAYYFCGEPIPYRTSVKGR--VVTLGQFKELLTKKGhYRFYFKKVSDEFDcGVVFEEVRDDDATLPIFEEKIIGK 876
Cdd:smart00021   1 CSETKVIYHLDDEETPYLVKVPVPaeRVTLGDFKEVLTKKN-YKYYFKSMDDDFG-GVVKEEIRDDSARLPCFNGRVVSW 78

                   ....*
gi 768942821   877 VEKVD 881
Cdd:smart00021  79 LVSVE 83

Regulator of G protein signaling (RGS) domain found in the R12 subfamily of proteins; The RGS (Regulator of G-protein Signaling) domain is an essential part of the R12 (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). RGS proteins play a critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. Deactivation of G-protein signaling, controlled by RGS domain, accelerates GTPase activity of the alpha subunit by hydrolysis of GTP to GDP that 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 such as regulation of intracellular trafficking, glial differentiation, embryonic axis formation, skeletal and muscle development, and cell migration during early embryogenesis. The R12 RGS subfamily includes RGS10, RGS12 and RGS14 all of which are highly selective for G-alpha-i1 over G-alpha-q.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942821 116 LHSLLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKTS-QEKRAKLAKAIYRKYI---------VDGSGIVSRQIKAA 185
Cdd:cd08706    1 FERLLQDPVGVKYFTEFLKKEFSEENILFWQACEKFKKIPdKKQLVQEAREIYDTFLsskasspvnIDSQAQLAEEMLEE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 768942821 186 tksfirdcvgrPHPDpaMFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08706   81 -----------PHPD--MFQKQQLQIFNLMKFDSYSRFLKSPLYQQ 113

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 768942821 111 KWAESLHSLLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKTSQEKRAKLAKAIYRKYIVDGSgivSRQIKAATKSF- 189
Cdd:cd08705    4 RWGFSFSELLKDPVGREQFLKFLEKEFSGENLRFWEACQDLKYGPQSQVPEKVQEIYQEFLAPGA---PSWINIDSKTMe 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 768942821 190 -IRDCVGRPHpdPAMFEQAQIEIQSVMEENTYPLFLKSDLY 229
Cdd:cd08705   81 iTLKNLKDPH--RYTFDAAQEHIYMLMKKDSYPRFLRSDIY 119

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 768942821 116 LHSLLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKT-SQEKRAKLAKAIYRKYIVDGSgivSRQIK--AATKSFIRD 192
Cdd:cd08713    1 LEKLLLHKYGLAVFRAFLQTEFSEENLEFWLACEEYKKIkSQSKMASRAKKIFAEYIAIQS---CKEVNldSYTREHTKE 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 768942821 193 CVgrPHPDPAMFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08713   78 NL--QNPTRGCFDLAQKRIYGLMEKDSYPRFLRSDLYQD 114

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 768942821 111 KWAESLHSLLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKT-SQEKRAKLAKAIYRKYIvDGSGIVSRQIKAATKSF 189
Cdd:cd08711    7 RWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTrSTAKLVSKAHRIFEEFV-DVQAPREVNIDFQTREA 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 768942821 190 IRDcvGRPHPDPAMFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08711   86 TRK--NLQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLD 125

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 768942821 119 LLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKT-SQEKRAKLAKAIYRKYIvDGSGIVSRQIKAATKSFIRDCVgrP 197
Cdd:cd08709    4 LLASKYGVAAFRAFLKSEFSEENIEFWLACEDFKKTkSPQKLTSKAKKIYTDFI-EKEAPKEINIDFQTKTLIAQNI--Q 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 768942821 198 HPDPAMFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08709   81 EATSGCFTAAQKRVYSLMENNSYPRFLESEFYQE 114

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 768942821 108 PYLKWAESLHSLLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKTSQEKRAKL---AKAIYRKYIVDGSgivSRQIKA 184
Cdd:cd08743    3 SVASWAVSFERLLQDPLGVEYFTEFLKKEFSAENVNFWKACERFQQIPASDTQQLaqeARKIYNEFLSSSS---QSPVNI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 768942821 185 ATKSFI-RDCVGRPHPDpaMFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08743   80 DQQAWIgEDMLATPSPD--MFRAQQLQIFNLMKFDSYARFVKSPLYQD 125

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 768942821 119 LLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKT-SQEKRAKLAKAIYRKYI-VDGSGIVSrqIKAATKSFIRDCVGR 196
Cdd:cd08723    1 LLANQAGLDAFRTFLKSEFSEENVEFWLACEDFKKTkSSTEIALKAQMIYSEFIqADAPKEIN--IDFHTRDLISQNISE 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 768942821 197 phPDPAMFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08723   79 --PTLKCFDEAQSLIYCLMAKDSFPRFLKSEVYKK 111

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 768942821 112 WAESLHSLLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKTSQEKR-AKLAKAIYRKYIvdgsGIVSRQiKAATKSFI 190
Cdd:cd08744    1 WSQNFDKMMKTPAGRNLFREFLRTEYSEENLLFWLACEDLKKEQNKKViEEKARLIYEDYI----SILSPK-EVSLDSRV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 768942821 191 RDCVGRP--HPDPAMFEQAQIEIQSVMEENTYPLFLKSDLY 229
Cdd:cd08744   76 REVINRNllDPNPHMYEDAQLQIYTLMHRDSFPRFLNSQIY 116

Regulator of G protein signaling (RGS) domain found in the RGS9 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS9 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. Other members of the R7 subfamily (Neuronal RGS) include: RGS6, RGS7, 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. RGS9 forms constitutive complexes with G-beta-5 subunit and controls such fundamental functions as vision and behavior. RGS9 exists in two splice isoforms: RGS9-1 which regulates phototransduction in rods and cones and RGS9-2 which regulates dopamine and opioid signaling in the basal ganglia. In addition, RGS9 was found to bind many other proteins outside of G protein signaling pathways including: mu-opioid receptor, beta-arrestin, alpha-actinin-2, NMDAR, polycystin, spinophilin, and guanylyl cyclase, among others.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942821 111 KWAESLHSLLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKTSQEKRAKLAKAIYRKYIVDGSgivSRQIKAATKSFI 190
Cdd:cd08739    4 RWAFNFSELIRDPKGRQSFQLFLKKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGA---RRWINIDGKTMD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 768942821 191 RDCVGRPHPDPAMFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08739   81 ITVKGLKHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKE 121

Regulator of G protein signaling (RGS) domain found in the RGS4 protein; The RGS (Regulator of G-protein Signaling) domain is an essential part of the RGS4 protein. RGS4 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. RGS4 is expressed widely in brain including prefrontal cortex, striatum, locus coeruleus (LC), and hippocampus and has been implicated in regulation of opioid, cholinergic, and serotonergic signaling. Dysfunctions in RGS4 proteins are involved in etiology of Parkinson's disease, addiction, and schizophrenia. RGS4 also is up-regulated in the failing human heart. RGS4 interacts with many binding partners outside of GPCR pathways, including calmodulin, COP, Kir3, PIP, calcium/CaM, PA, ErbB3, and 14-3-3.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942821 116 LHSLLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKT-SQEKRAKLAKAIYRKYIvdgsgivSRQikaATKSFIRDCV 194
Cdd:cd08714    1 LENLINHECGLAAFKAFLKSEYSEENIDFWVSCEDYKKTkSPSKLSPKARKIYEEFI-------SVQ---ATKEVNLDSC 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 768942821 195 GRPH-------PDPAMFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08714   71 TREEtsrnmlePTISCFDEAQKKIFTLMEKDSYRRFLKSRFYLD 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 768942821 128 LFKNFLHQEGCADLLDFWFACSGFRK-TSQEKRAKLAKAIYRKYIVDGSgivSRQIK---AATKSFIRDCvgrPHPDPAM 203
Cdd:cd08716   13 IYATYLKTEHSDENIEFWLACETYKKiASQRKRISMARKLFASYIQPQA---PREINidsPTRKAIIRNI---QEPTQSC 86

                         90       100
                 ....*....|....*....|....*.
gi 768942821 204 FEQAQIEIQSVMEENTYPLFLKSDLY 229
Cdd:cd08716   87 FDEAQRIVYMHMERDSYPRFLESKFY 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        40
                  ....*....|....*....|....*....|....*....|....*..
gi 768942821  508 DDPESILDEHVQRVMKTPGCQSPgatnstlgggGRHSPPksSRSPDG 554
Cdd:pfam08833   1 DNPQSILDEHVSRVWKTPGCQSP----------GRHSPR--SRSPDS 35

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 768942821 119 LLDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRKTSQEKRAKL---AKAIYRKYIvdgSGIVSRQIKAATKSFIRDCVG 195
Cdd:cd08742    4 LLQDPVGVRYFSEFLRKEFSEENILFWQACEYFNHVPAHDKKELsyrAREIFSKFL---CSKATTPVNIDSQAQLADDIL 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 768942821 196 R-PHPDpaMFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08742   81 NaPHPD--MFKEQQLQIFNLMKFDSYTRFLKSPLYQE 115

Regulator of G protein signaling (RGS) domain 2 found in the A-kinase anchoring protein, D-AKAP2; The RGS (Regulator of G-protein Signaling) domain is an essential part of the D-AKAP2 (A-kinase anchoring 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. D-AKAP2 contains two RGS domains which play an important role in spatiotemporal localization of cAMP-dependent PKA (cyclic AMP-dependent protein kinase) that regulates many different signaling pathways by phosphorylation of target proteins. This cd contains the second RGS domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942821 129 FKNFLHQEGCADLLDFWFACSGFRKTSQEKRAKL--------AKAIYRKYIvdgsgivSRQikaATKSFIRDCVGRPH-- 198
Cdd:cd08721   11 FMEYMEQEGARNLLQFWLAADNFQSQLAAKEGQYdgqqaqndAMIIYDKYF-------SLQ---ATEPLGFDDKTRLEve 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 768942821 199 --------PDPAMFEQAQIEIQSVMEENTYPLFLKSDLY 229
Cdd:cd08721   81 snicreggPLPSCFEAPLLQALTTLEQHYLPGFLSSQLY 119

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 768942821 120 LDDQEGIHLFKNFLHQEGCADLLDFWFACSGFRK-------TSQEKRA--KLAKAIYRKYIVDGS-------GIVSRQIK 183
Cdd:cd08722    2 LDDQRLLFPFMQFLKEEGAVHLLQFCLTVEDFNRrilnpdlTDEEKQSlhKEAQEIYKTYFLPEApdrihfpPDIVEEIK 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768942821 184 AAT----KSFIRDCVGRPhpdpamFEQAQIEIQSVMEENTYPLFLKSDLYLE 231
Cdd:cd08722   82 QILeggpEKIVKLRTSRP------LFEAYEHVYSLLESVFCPLFCHSDEYFI 127

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 768942821 129 FKNFLHQEGCADLLDFWFACSGFRKTSQEKRAKL---------------------AKAIYRKYIVDGSGI---VSRQIKA 184
Cdd:cd08719   11 FIDFMQSVGGQAYLFFWLTVEGYRVSAEQQLSELhlrqrggehqrsdvyemlraaALNIYDQYLSEKASPrvpLDDSLVK 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 768942821 185 ATKSFIRDcvgrPHPDPAMFEQAQIEIQSVMEENT--YPLFLKSDLY 229
Cdd:cd08719   91 KLLNRLRN----DTPSDLWFDDIQQKVFDIMQEDErfYPAFKKSPAY 133

Major prion protein; The prion protein is a major component of scrapie-associated fibrils in Creutzfeldt-Jakob disease, kuru, Gerstmann-Straussler syndrome and bovine spongiform encephalopathy.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768942821   525 PGCQSPGATNSTLGGGGRHSPpkssrsPDGGTGPPHypphrGGGHSLPAAGVKGTHHHKQIYHHRGREGQDEAGSRSQAN 604
Cdd:smart00157  18 PGQGSPGGNRYPPQGGGWGQP------HGGGWGQPH-----GGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTN 86

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 768942821   605 FmwngdpgrsRNYADCAGAGAVEG--VGYSKGSTLSR 639
Cdd:smart00157  87 M---------KHVAGAAAAGAVVGglGGYMLGSAMSR 114