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Conserved domains on  [gi|28558115|sp|Q9ERT9|]
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RecName: Full=Protein phosphatase 1 regulatory subunit 1A; AltName: Full=Protein phosphatase inhibitor 1; Short=I-1; Short=IPP-1

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DARPP-32 super family cl05121
Protein phosphatase inhibitor 1/DARPP-32; This family consists of several mammalian protein ...
 5-142 2.30e-33

Protein phosphatase inhibitor 1/DARPP-32; This family consists of several mammalian protein phosphatase inhibitor 1 (IPP-1) and dopamine- and cAMP-regulated neuronal phosphoprotein (DARPP-32) proteins. Protein phosphatase inhibitor-1 is involved in signal transduction and is an endogenous inhibitor of protein phosphatase-1. It has been demonstrated that DARPP-32, if phosphorylated, can inhibit protein-phosphatase-1. DARPP-32 has a key role in many neurotransmitter pathways throughout the brain and has been shown to be involved in controlling receptors, ion channels and other physiological factors including the brain's response to drugs of abuse, such as cocaine, opiates and nicotine. DARPP-32 is reciprocally regulated by the two neurotransmitters that are most often implicated in schizophrenia - dopamine and glutamate. Dopamine activates DARPP-32 through the D1 receptor pathway and disables DARPP-32 through the D2 receptor. Glutamate, acting through the N-methyl-d-aspartate receptor, renders DARPP-32 inactive. A mutant form of DARPP-32 has been linked with gastric cancers.


The actual alignment was detected with superfamily member pfam05395:

Pssm-ID: 428454  Cd Length: 136  Bit Score: 114.94  E-value: 2.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558115     5 NSPRKIQFTVPLLEPHLDPEAAEQIRRRRPTPATLVLTSDQSSPEiDEDRIPNSLLKSTLSMSPRQRKKMTRTTPTMKEL 84
Cdd:pfam05395   3 KERKKIQFAVPAPPSQLDPRQVEMIRRRRPTPATLFRVSDQSSPE-DEQSSHQWVVGENGILKPKRRNPCVYTPPSLKAV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 28558115    85 QTMVEHHLgqQKQGEEPEGATESTGNQESCPPGIPDTGSASrPDTPGTAQKSAESNPK 142
Cdd:pfam05395  82 QRMAEAHM--QKLGVYPNLEDPPEGQEEEDELGEPEGNEDS-PPTSGEEGEEEESEEE 136
 
Name Accession Description Interval E-value
DARPP-32 pfam05395
Protein phosphatase inhibitor 1/DARPP-32; This family consists of several mammalian protein ...
 5-142 2.30e-33

Protein phosphatase inhibitor 1/DARPP-32; This family consists of several mammalian protein phosphatase inhibitor 1 (IPP-1) and dopamine- and cAMP-regulated neuronal phosphoprotein (DARPP-32) proteins. Protein phosphatase inhibitor-1 is involved in signal transduction and is an endogenous inhibitor of protein phosphatase-1. It has been demonstrated that DARPP-32, if phosphorylated, can inhibit protein-phosphatase-1. DARPP-32 has a key role in many neurotransmitter pathways throughout the brain and has been shown to be involved in controlling receptors, ion channels and other physiological factors including the brain's response to drugs of abuse, such as cocaine, opiates and nicotine. DARPP-32 is reciprocally regulated by the two neurotransmitters that are most often implicated in schizophrenia - dopamine and glutamate. Dopamine activates DARPP-32 through the D1 receptor pathway and disables DARPP-32 through the D2 receptor. Glutamate, acting through the N-methyl-d-aspartate receptor, renders DARPP-32 inactive. A mutant form of DARPP-32 has been linked with gastric cancers.


Pssm-ID: 428454  Cd Length: 136  Bit Score: 114.94  E-value: 2.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558115     5 NSPRKIQFTVPLLEPHLDPEAAEQIRRRRPTPATLVLTSDQSSPEiDEDRIPNSLLKSTLSMSPRQRKKMTRTTPTMKEL 84
Cdd:pfam05395   3 KERKKIQFAVPAPPSQLDPRQVEMIRRRRPTPATLFRVSDQSSPE-DEQSSHQWVVGENGILKPKRRNPCVYTPPSLKAV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 28558115    85 QTMVEHHLgqQKQGEEPEGATESTGNQESCPPGIPDTGSASrPDTPGTAQKSAESNPK 142
Cdd:pfam05395  82 QRMAEAHM--QKLGVYPNLEDPPEGQEEEDELGEPEGNEDS-PPTSGEEGEEEESEEE 136
 
Name Accession Description Interval E-value
DARPP-32 pfam05395
Protein phosphatase inhibitor 1/DARPP-32; This family consists of several mammalian protein ...
 5-142 2.30e-33

Protein phosphatase inhibitor 1/DARPP-32; This family consists of several mammalian protein phosphatase inhibitor 1 (IPP-1) and dopamine- and cAMP-regulated neuronal phosphoprotein (DARPP-32) proteins. Protein phosphatase inhibitor-1 is involved in signal transduction and is an endogenous inhibitor of protein phosphatase-1. It has been demonstrated that DARPP-32, if phosphorylated, can inhibit protein-phosphatase-1. DARPP-32 has a key role in many neurotransmitter pathways throughout the brain and has been shown to be involved in controlling receptors, ion channels and other physiological factors including the brain's response to drugs of abuse, such as cocaine, opiates and nicotine. DARPP-32 is reciprocally regulated by the two neurotransmitters that are most often implicated in schizophrenia - dopamine and glutamate. Dopamine activates DARPP-32 through the D1 receptor pathway and disables DARPP-32 through the D2 receptor. Glutamate, acting through the N-methyl-d-aspartate receptor, renders DARPP-32 inactive. A mutant form of DARPP-32 has been linked with gastric cancers.


Pssm-ID: 428454  Cd Length: 136  Bit Score: 114.94  E-value: 2.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28558115     5 NSPRKIQFTVPLLEPHLDPEAAEQIRRRRPTPATLVLTSDQSSPEiDEDRIPNSLLKSTLSMSPRQRKKMTRTTPTMKEL 84
Cdd:pfam05395   3 KERKKIQFAVPAPPSQLDPRQVEMIRRRRPTPATLFRVSDQSSPE-DEQSSHQWVVGENGILKPKRRNPCVYTPPSLKAV 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 28558115    85 QTMVEHHLgqQKQGEEPEGATESTGNQESCPPGIPDTGSASrPDTPGTAQKSAESNPK 142
Cdd:pfam05395  82 QRMAEAHM--QKLGVYPNLEDPPEGQEEEDELGEPEGNEDS-PPTSGEEGEEEESEEE 136
TRAP_alpha pfam03896
Translocon-associated protein (TRAP), alpha subunit; The alpha-subunit of the TRAP complex ...
 30-73 1.66e-03

Translocon-associated protein (TRAP), alpha subunit; The alpha-subunit of the TRAP complex (TRAP alpha) is a single-spanning membrane protein of the endoplasmic reticulum (ER) which is found in proximity of nascent polypeptide chains translocating across the membrane.


Pssm-ID: 461085  Cd Length: 279  Bit Score: 37.76  E-value: 1.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 28558115    30 RRRRPTPATLVLTSDQSSPEIDEDRIP----NSLLKSTLSMSPRQRKK 73
Cdd:pfam03896 225 KRRVPGKKRPVETGTANTNDVDYDWLPketlNQLNKSSPKQSPRQRKV 272
 
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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