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Conserved domains on  [gi|157818341|ref|NP_001103034|]
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protein phosphatase 1 regulatory subunit 3D [Rattus norvegicus]

Protein Classification

CBM21 domain-containing protein( domain architecture ID 15819480)

CBM21 domain-containing protein carries a family 21 carbohydrate-binding module (CBM21), such as found in many eukaryotic proteins involved in glycogen metabolism, which might mediate interactions with glycogen; similar to regulatory subunits 3A, 3B, 3C, 3E, 3F, and 3G of protein phosphatase 1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBM_21 pfam03370
Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic ...
 151-257 6.80e-42

Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.


:

Pssm-ID: 427265  Cd Length: 112  Bit Score: 139.68  E-value: 6.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818341  151 RLARQLVCLERVTCSD--LGISGTVRVRNVAFEKQVTVRYTFSGWRSAHEAVARWRGPAGG---EGTEDIFAFGFPVPPF 225
Cdd:pfam03370   1 RLQGQPVCLERLFLSDdkKSLVGTVRVKNLAFEKRVAVRYTFDNWKTISDVPAEYVPDARSsldGDNYDRFKFKIPLPPL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 157818341  226 LLELGSQVHFALRYGVAGAEYWDNNDGQDYSL 257
Cdd:pfam03370  81 LNLEGKTLEFCIRYEVNGQEYWDNNNGKNYQV 112
PBD_PPP1R3 super family cl41685
PP1C binding domain found in protein phosphatase 1 regulatory subunit 3 (PPP1R3) family; The ...
 11-105 1.08e-04

PP1C binding domain found in protein phosphatase 1 regulatory subunit 3 (PPP1R3) family; The PPP1R3 family includes three protein phosphatase 1 regulatory subunits, PPP1R3A, PPP1R3B and PPP1R3C, that act as glycogen-targeting subunits for protein phosphatase 1 (PP1). PPP1R3A, also called protein phosphatase 1 glycogen-associated regulatory subunit (PP1G), protein phosphatase type-1 glycogen targeting subunit, or RG1, is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility, and protein synthesis. PPP1R3A plays an important role in glycogen synthesis but is not essential for insulin activation of glycogen synthase. PPP1R3B, also called hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL, protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, or protein phosphatase 1 subunit GL, facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. PPP1R3B suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by glycogen phosphorylase liver form (PYGL), resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. PPP1R3C, also called protein phosphatase 1 regulatory subunit 5 (PPP1R5), PP1 subunit R5, or protein targeting to glycogen (PTG), activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. It can dramatically increase basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types. This model corresponds to protein phosphatase 1 catalytic subunit (PP1C) binding domain, which contains a RVxF PP1C-binding motif that mediates interactions with PP1C.


The actual alignment was detected with superfamily member cd22255:

Pssm-ID: 455118  Cd Length: 82  Bit Score: 40.01  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818341  11 PSTPGPRKLAPRSLSCLSDMDGRScRPPGCDPRLRPIIQRRSRSLPTSPERRAKAAGaqgaacgagcNRqvRVRFADALG 90
Cdd:cd22255    1 PGLSPSLLEPPELSDGDEEDEEEE-EVSGIKPKSSPLPRRRSSSESEESEPEPPPSV----------RR--KVSFADAFG 67

                         90
                 ....*....|....*
gi 157818341  91 LELAQVKVFNAGDDP 105
Cdd:cd22255   68 LDLVSVKEFDTWDSP 82
 
Name Accession Description Interval E-value
CBM_21 pfam03370
Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic ...
 151-257 6.80e-42

Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.


Pssm-ID: 427265  Cd Length: 112  Bit Score: 139.68  E-value: 6.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818341  151 RLARQLVCLERVTCSD--LGISGTVRVRNVAFEKQVTVRYTFSGWRSAHEAVARWRGPAGG---EGTEDIFAFGFPVPPF 225
Cdd:pfam03370   1 RLQGQPVCLERLFLSDdkKSLVGTVRVKNLAFEKRVAVRYTFDNWKTISDVPAEYVPDARSsldGDNYDRFKFKIPLPPL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 157818341  226 LLELGSQVHFALRYGVAGAEYWDNNDGQDYSL 257
Cdd:pfam03370  81 LNLEGKTLEFCIRYEVNGQEYWDNNNGKNYQV 112
PBD_PPP1R3A cd22255
PP1C binding domain found in protein phosphatase 1 regulatory subunit 3A (PPP1R3A) and similar ...
 11-105 1.08e-04

PP1C binding domain found in protein phosphatase 1 regulatory subunit 3A (PPP1R3A) and similar proteins; PPP1R3A, also called protein phosphatase 1 glycogen-associated regulatory subunit (PP1G), protein phosphatase type-1 glycogen targeting subunit, or RG1, acts as a glycogen-targeting subunit for PP1 that is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility, and protein synthesis. PPP1R3A plays an important role in glycogen synthesis but is not essential for insulin activation of glycogen synthase. It interacts with the PPP1CC catalytic subunit of PP1 and associates with glycogen. This model corresponds to the protein phosphatase 1 catalytic subunit (PP1C) binding domain of PPP1R3A, which contains a RVxF PP1C-binding motif that mediates interactions with PP1C.


Pssm-ID: 439277  Cd Length: 82  Bit Score: 40.01  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818341  11 PSTPGPRKLAPRSLSCLSDMDGRScRPPGCDPRLRPIIQRRSRSLPTSPERRAKAAGaqgaacgagcNRqvRVRFADALG 90
Cdd:cd22255    1 PGLSPSLLEPPELSDGDEEDEEEE-EVSGIKPKSSPLPRRRSSSESEESEPEPPPSV----------RR--KVSFADAFG 67

                         90
                 ....*....|....*
gi 157818341  91 LELAQVKVFNAGDDP 105
Cdd:cd22255   68 LDLVSVKEFDTWDSP 82
 
Name Accession Description Interval E-value
CBM_21 pfam03370
Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic ...
 151-257 6.80e-42

Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.


Pssm-ID: 427265  Cd Length: 112  Bit Score: 139.68  E-value: 6.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818341  151 RLARQLVCLERVTCSD--LGISGTVRVRNVAFEKQVTVRYTFSGWRSAHEAVARWRGPAGG---EGTEDIFAFGFPVPPF 225
Cdd:pfam03370   1 RLQGQPVCLERLFLSDdkKSLVGTVRVKNLAFEKRVAVRYTFDNWKTISDVPAEYVPDARSsldGDNYDRFKFKIPLPPL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 157818341  226 LLELGSQVHFALRYGVAGAEYWDNNDGQDYSL 257
Cdd:pfam03370  81 LNLEGKTLEFCIRYEVNGQEYWDNNNGKNYQV 112
CBM53 pfam16760
Starch/carbohydrate-binding module (family 53);
177-258 1.42e-14

Starch/carbohydrate-binding module (family 53);


Pssm-ID: 465261 [Multi-domain]  Cd Length: 76  Bit Score: 67.32  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818341  177 NVAFEK----QVTVRYTFSGWRSAHEAVARWRGPAGGEGTediFAFGFPVPPFllelGSQVHFALRygvAGAEYWDNNDG 252
Cdd:pfam16760   1 NIYYNGslakEVYIHGGFNGWKNVQDVPMEKLPPTGGGDW---FSATVPVPED----AYVLDFVFK---DGAGNWDNNNG 70


                  ....*.
gi 157818341  253 QDYSLT 258
Cdd:pfam16760  71 QNYHIP 76
PBD_PPP1R3A cd22255
PP1C binding domain found in protein phosphatase 1 regulatory subunit 3A (PPP1R3A) and similar ...
 11-105 1.08e-04

PP1C binding domain found in protein phosphatase 1 regulatory subunit 3A (PPP1R3A) and similar proteins; PPP1R3A, also called protein phosphatase 1 glycogen-associated regulatory subunit (PP1G), protein phosphatase type-1 glycogen targeting subunit, or RG1, acts as a glycogen-targeting subunit for PP1 that is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility, and protein synthesis. PPP1R3A plays an important role in glycogen synthesis but is not essential for insulin activation of glycogen synthase. It interacts with the PPP1CC catalytic subunit of PP1 and associates with glycogen. This model corresponds to the protein phosphatase 1 catalytic subunit (PP1C) binding domain of PPP1R3A, which contains a RVxF PP1C-binding motif that mediates interactions with PP1C.


Pssm-ID: 439277  Cd Length: 82  Bit Score: 40.01  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818341  11 PSTPGPRKLAPRSLSCLSDMDGRScRPPGCDPRLRPIIQRRSRSLPTSPERRAKAAGaqgaacgagcNRqvRVRFADALG 90
Cdd:cd22255    1 PGLSPSLLEPPELSDGDEEDEEEE-EVSGIKPKSSPLPRRRSSSESEESEPEPPPSV----------RR--KVSFADAFG 67

                         90
                 ....*....|....*
gi 157818341  91 LELAQVKVFNAGDDP 105
Cdd:cd22255   68 LDLVSVKEFDTWDSP 82
PBD_PPP1R3B cd22814
PP1C binding domain found in protein phosphatase 1 regulatory subunit 3B (PPP1R3B); PPP1R3B, ...
 44-111 3.24e-03

PP1C binding domain found in protein phosphatase 1 regulatory subunit 3B (PPP1R3B); PPP1R3B, also called hepatic glycogen-targeting protein phosphatase 1 (PP1) regulatory subunit GL, protein phosphatase 1 regulatory subunit 4, PP1 subunit R4, or protein phosphatase 1 subunit GL, acts as a glycogen-targeting subunit for PP1. It facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. PPP1R3B suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by glycogen phosphorylase liver form (PYGL), resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. It can dramatically increase basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes. PPP1R3B interacts with glycogen, the PPP1CC catalytic subunit of PP1, and PYGL. It associates with glycogen particles. This model corresponds to the protein phosphatase 1 catalytic subunit (PP1C) binding domain of PPP1R3B, which contains a RVxF PP1C-binding motif that mediates interactions with PP1C.


Pssm-ID: 439279  Cd Length: 74  Bit Score: 35.59  E-value: 3.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157818341  44 LRPIIQRRSRSLPTSPERRAKAAGAQGaacgagcnrQVRVRFADALGLELAQVKVFNAGDDP-SVPLHV 111
Cdd:cd22814    3 LRPCIQLNSKNKLSGGMSEPSVQENKV---------KKHVSFADHKGLALTMVKVFSEFDDPlDIPFNI 62
 
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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