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Conserved domains on  [gi|110611937|ref|NP_001036056|]
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arrestin domain-containing protein 3 [Mus musculus]

Protein Classification

arrestin family protein( domain architecture ID 10448464)

arrestin family protein with both N-terminal and C-terminal Ig-like beta-sandwich domains found in arrestin (S antigen); similar to Homo sapiens beta-arrestin-1 and arrestin domain-containing protein

CATH:  2.60.40.840
Gene Ontology:  GO:0005515
PubMed:  7720881|7833798|35563378
SCOP:  4007521

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Arrestin_N pfam00339
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 22-165 1.06e-37

Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with C-terminal domain.


:

Pssm-ID: 425619  Cd Length: 148  Bit Score: 133.57  E-value: 1.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611937   22 PVYSSGDTVSGRVNLEVTGEIRVKSLKIHARGHAKVRWTESRNA--GSNTAYTQNYTEEVEYFNHKDILIGHERDDDNse 99
Cdd:pfam00339  10 GVYFPGETVTGRVLLENEEPKKARAVKIELRGKARTGWEESEVRkeGLTFRKDLYYKGTEVYLPTETSLWGSKTGGQN-- 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110611937  100 egfhTIHSGRHEYAFSFELPQTpLATSFEGRHGSVRYWVKAELHRPWLLPVKLKKEFTVFEHIDIN 165
Cdd:pfam00339  88 ----KLPAGTHTFPFSFTLPPN-CPSSFEGKHGGIRYEVKVTLDRPWKFNKSFRRVFTVIPKLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 187-314 2.51e-31

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain. Arrestins comprise a family of closely-related proteins that includes beta-arrestin-1 and -2, which regulate the function of beta-adrenergic receptors by binding to their phosphorylated forms, impairing their capacity to activate G(S) proteins; Cone photoreceptors C-arrestin (arrestin-X). which could bind to phosphorylated red/green opsins; and Drosophila phosrestins I and II, which undergo light-induced phosphorylation, and probably play a role in photoreceptor transduction.


:

Pssm-ID: 214976 [Multi-domain]  Cd Length: 142  Bit Score: 116.67  E-value: 2.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611937   187 TSGPISLSAKIERKGYTPGESIQIFAEIENCSSRMVV-PKAAIYQTQAFYA-------------KGKMKEVKQLVANLRG 252
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKkIKVSLVQTVTYVSsdgpvkrslaeksKEKKADRKTLVKELDG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110611937   253 ESLSSGKTETWNGKlLKIPPVSPSILDCSIIRVEYSLMVYVDIPG-AMDLLLSLPLVIGTIPL 314
Cdd:smart01017  81 GPVLPGNKDKFEGQ-LKVPPLPPTSRTCRLIKVEYKLKVKLRLSGkHSELRLELPITIGTVPL 142
 
Name Accession Description Interval E-value
Arrestin_N pfam00339
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 22-165 1.06e-37

Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with C-terminal domain.


Pssm-ID: 425619  Cd Length: 148  Bit Score: 133.57  E-value: 1.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611937   22 PVYSSGDTVSGRVNLEVTGEIRVKSLKIHARGHAKVRWTESRNA--GSNTAYTQNYTEEVEYFNHKDILIGHERDDDNse 99
Cdd:pfam00339  10 GVYFPGETVTGRVLLENEEPKKARAVKIELRGKARTGWEESEVRkeGLTFRKDLYYKGTEVYLPTETSLWGSKTGGQN-- 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110611937  100 egfhTIHSGRHEYAFSFELPQTpLATSFEGRHGSVRYWVKAELHRPWLLPVKLKKEFTVFEHIDIN 165
Cdd:pfam00339  88 ----KLPAGTHTFPFSFTLPPN-CPSSFEGKHGGIRYEVKVTLDRPWKFNKSFRRVFTVIPKLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 187-314 2.51e-31

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain. Arrestins comprise a family of closely-related proteins that includes beta-arrestin-1 and -2, which regulate the function of beta-adrenergic receptors by binding to their phosphorylated forms, impairing their capacity to activate G(S) proteins; Cone photoreceptors C-arrestin (arrestin-X). which could bind to phosphorylated red/green opsins; and Drosophila phosrestins I and II, which undergo light-induced phosphorylation, and probably play a role in photoreceptor transduction.


Pssm-ID: 214976 [Multi-domain]  Cd Length: 142  Bit Score: 116.67  E-value: 2.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611937   187 TSGPISLSAKIERKGYTPGESIQIFAEIENCSSRMVV-PKAAIYQTQAFYA-------------KGKMKEVKQLVANLRG 252
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKkIKVSLVQTVTYVSsdgpvkrslaeksKEKKADRKTLVKELDG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110611937   253 ESLSSGKTETWNGKlLKIPPVSPSILDCSIIRVEYSLMVYVDIPG-AMDLLLSLPLVIGTIPL 314
Cdd:smart01017  81 GPVLPGNKDKFEGQ-LKVPPLPPTSRTCRLIKVEYKLKVKLRLSGkHSELRLELPITIGTVPL 142
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 187-314 1.11e-29

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain.


Pssm-ID: 460676  Cd Length: 135  Bit Score: 112.03  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611937  187 TSGPISLSAKIERKGYTPGESIQIFAEIENCSSRMVVP-KAAIYQTQAFYAKGKM---KEVKQLVANLRGESLSSGKTET 262
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKiKISLVQQLTYKAKTPLgesKREERVVAKEKNPGVAPGSKDK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110611937  263 WNGKL-LKIP-PVSPSILDCSIIRVEYSLMVYVDIPG-AMDLLLSLPLVIGTIPL 314
Cdd:pfam02752  81 WEKELqLQIPtDLPPSSTKCKIIKVEYKLKVTVDLSGsASELRLELPITIGTSPL 135
ART10-like cd22952
Arrestin-related trafficking adapter 10 and similar proteins; Arrestin-related trafficking ...
 16-148 2.02e-09

Arrestin-related trafficking adapter 10 and similar proteins; Arrestin-related trafficking adaptors (ARTs) function by targeting specific plasma membrane proteins to the endocytic system. They contain multiple PY motifs that are required for recruitment of Rsp5/Nedd4-like ubiquitin ligase which modifies the cargoes. It has been proposed that ARTs remodel the cell surface in response to environmental cues and may serve as part of a quality-control system at the plasma membrane, targeting damaged and misfolded membrane proteins for ubiquitination and subsequent degradation in the lysosome/vacuole. The specific target protein for ART10 is not yet known.


Pssm-ID: 438568 [Multi-domain]  Cd Length: 409  Bit Score: 58.92  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611937  16 LNDSNVPVYSSGDTVSGRVNLEVTGEIRVKSLKIHARGHAKVR-WTESRNAGSNTAYTQNYTEEVEYFNHKDILIGHERD 94
Cdd:cd22952    5 LLDDNGEFYTNLDVISGRVILKLTKSESISAIVVKLEGESRTRlKVPKGNYNGQNDRGRTATEVHKLLYKVQQVFPPPNV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611937  95 DDNSEEGFHTIHSGRHEYAFSFELPQT------------------------------------PLATSFeGRHGSVRYWV 138
Cdd:cd22952   85 RSVSSSKSFTLTPGEYEYPFEFKIPFNnscsdphskstsgglggslmdglppsfnrhvkktlpPSLTGF-PGEAEIRYYV 163

                        170
                 ....*....|
gi 110611937 139 KAELHRPWLL 148
Cdd:cd22952  164 KVTVQRPSFF 173
 
Name Accession Description Interval E-value
Arrestin_N pfam00339
Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 22-165 1.06e-37

Arrestin (or S-antigen), N-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with C-terminal domain.


Pssm-ID: 425619  Cd Length: 148  Bit Score: 133.57  E-value: 1.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611937   22 PVYSSGDTVSGRVNLEVTGEIRVKSLKIHARGHAKVRWTESRNA--GSNTAYTQNYTEEVEYFNHKDILIGHERDDDNse 99
Cdd:pfam00339  10 GVYFPGETVTGRVLLENEEPKKARAVKIELRGKARTGWEESEVRkeGLTFRKDLYYKGTEVYLPTETSLWGSKTGGQN-- 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110611937  100 egfhTIHSGRHEYAFSFELPQTpLATSFEGRHGSVRYWVKAELHRPWLLPVKLKKEFTVFEHIDIN 165
Cdd:pfam00339  88 ----KLPAGTHTFPFSFTLPPN-CPSSFEGKHGGIRYEVKVTLDRPWKFNKSFRRVFTVIPKLDLN 148
Arrestin_C smart01017
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 187-314 2.51e-31

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain. Arrestins comprise a family of closely-related proteins that includes beta-arrestin-1 and -2, which regulate the function of beta-adrenergic receptors by binding to their phosphorylated forms, impairing their capacity to activate G(S) proteins; Cone photoreceptors C-arrestin (arrestin-X). which could bind to phosphorylated red/green opsins; and Drosophila phosrestins I and II, which undergo light-induced phosphorylation, and probably play a role in photoreceptor transduction.


Pssm-ID: 214976 [Multi-domain]  Cd Length: 142  Bit Score: 116.67  E-value: 2.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611937   187 TSGPISLSAKIERKGYTPGESIQIFAEIENCSSRMVV-PKAAIYQTQAFYA-------------KGKMKEVKQLVANLRG 252
Cdd:smart01017   1 WSGPLSLEVSLPKKGYVPGETIPVTIKITNLSKKTVKkIKVSLVQTVTYVSsdgpvkrslaeksKEKKADRKTLVKELDG 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110611937   253 ESLSSGKTETWNGKlLKIPPVSPSILDCSIIRVEYSLMVYVDIPG-AMDLLLSLPLVIGTIPL 314
Cdd:smart01017  81 GPVLPGNKDKFEGQ-LKVPPLPPTSRTCRLIKVEYKLKVKLRLSGkHSELRLELPITIGTVPL 142
Arrestin_C pfam02752
Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports ...
 187-314 1.11e-29

Arrestin (or S-antigen), C-terminal domain; Ig-like beta-sandwich fold. Scop reports duplication with N-terminal domain.


Pssm-ID: 460676  Cd Length: 135  Bit Score: 112.03  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611937  187 TSGPISLSAKIERKGYTPGESIQIFAEIENCSSRMVVP-KAAIYQTQAFYAKGKM---KEVKQLVANLRGESLSSGKTET 262
Cdd:pfam02752   1 WSGKVSYSVSLPKKGYVPGETIPVTIEIDNQSKKKIKKiKISLVQQLTYKAKTPLgesKREERVVAKEKNPGVAPGSKDK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110611937  263 WNGKL-LKIP-PVSPSILDCSIIRVEYSLMVYVDIPG-AMDLLLSLPLVIGTIPL 314
Cdd:pfam02752  81 WEKELqLQIPtDLPPSSTKCKIIKVEYKLKVTVDLSGsASELRLELPITIGTSPL 135
ART10-like cd22952
Arrestin-related trafficking adapter 10 and similar proteins; Arrestin-related trafficking ...
 16-148 2.02e-09

Arrestin-related trafficking adapter 10 and similar proteins; Arrestin-related trafficking adaptors (ARTs) function by targeting specific plasma membrane proteins to the endocytic system. They contain multiple PY motifs that are required for recruitment of Rsp5/Nedd4-like ubiquitin ligase which modifies the cargoes. It has been proposed that ARTs remodel the cell surface in response to environmental cues and may serve as part of a quality-control system at the plasma membrane, targeting damaged and misfolded membrane proteins for ubiquitination and subsequent degradation in the lysosome/vacuole. The specific target protein for ART10 is not yet known.


Pssm-ID: 438568 [Multi-domain]  Cd Length: 409  Bit Score: 58.92  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611937  16 LNDSNVPVYSSGDTVSGRVNLEVTGEIRVKSLKIHARGHAKVR-WTESRNAGSNTAYTQNYTEEVEYFNHKDILIGHERD 94
Cdd:cd22952    5 LLDDNGEFYTNLDVISGRVILKLTKSESISAIVVKLEGESRTRlKVPKGNYNGQNDRGRTATEVHKLLYKVQQVFPPPNV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110611937  95 DDNSEEGFHTIHSGRHEYAFSFELPQT------------------------------------PLATSFeGRHGSVRYWV 138
Cdd:cd22952   85 RSVSSSKSFTLTPGEYEYPFEFKIPFNnscsdphskstsgglggslmdglppsfnrhvkktlpPSLTGF-PGEAEIRYYV 163

                        170
                 ....*....|
gi 110611937 139 KAELHRPWLL 148
Cdd:cd22952  164 KVTVQRPSFF 173
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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