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Protein

cAMP-dependent protein kinase type I-alpha regulatory subunit

Gene

Prkar1a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei202cAMP 11
Binding sitei211cAMP 11
Binding sitei326cAMP 21
Binding sitei335cAMP 21

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi137 – 254cAMP 1Add BLAST118
Nucleotide bindingi255 – 381cAMP 2Add BLAST127

GO - Molecular functioni

  • cAMP binding Source: RGD
  • cAMP-dependent protein kinase inhibitor activity Source: Ensembl
  • cAMP-dependent protein kinase regulator activity Source: RGD
  • protein kinase A catalytic subunit binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-163615. PKA activation.
R-RNO-164378. PKA activation in glucagon signalling.
R-RNO-180024. DARPP-32 events.
R-RNO-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-RNO-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-RNO-5610787. Hedgehog 'off' state.
R-RNO-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type I-alpha regulatory subunit
Cleaved into the following chain:
Gene namesi
Name:Prkar1a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi3391. Prkar1a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004232181 – 381cAMP-dependent protein kinase type I-alpha regulatory subunitAdd BLAST381
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00002053802 – 381cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processedAdd BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylalanine; in cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processedBy similarity1
Modified residuei3PhosphoserineCombined sources1
Disulfide bondi18Interchain (with C-39)By similarity
Disulfide bondi39Interchain (with C-18)By similarity
Modified residuei75PhosphothreonineBy similarity1
Modified residuei77PhosphoserineBy similarity1
Modified residuei83PhosphoserineCombined sources1
Modified residuei101PhosphoserineBy similarity1
Modified residuei258PhosphoserineCombined sources1

Post-translational modificationi

The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP09456.
PRIDEiP09456.

PTM databases

iPTMnetiP09456.
PhosphoSitePlusiP09456.

Expressioni

Gene expression databases

BgeeiENSRNOG00000049876.
GenevisibleiP09456. RN.

Interactioni

Subunit structurei

The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. PRKAR1A also interacts with RFC2; the complex may be involved in cell survival. Interacts with AKAP4. Interacts with RARA; the interaction occurs in the presence of cAMP or FSH and regulates RARA transcriptional activity. Interacts with the phosphorylated form of PJA2. Interacts with CBFA2T3. Interacts with PRKX; regulates this cAMP-dependent protein kinase (By similarity). Interacts with smAKAP; this interaction may target PRKAR1A to the plasma membrane. Interacts with AICDA (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PDE4DIPQ5VU43-112EBI-916215,EBI-10769071From a different organism.

GO - Molecular functioni

  • protein kinase A catalytic subunit binding Source: RGD

Protein-protein interaction databases

IntActiP09456. 2 interactors.
MINTiMINT-1775716.
STRINGi10116.ENSRNOP00000067771.

Structurei

3D structure databases

ProteinModelPortaliP09456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 136Dimerization and phosphorylationAdd BLAST135

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi96 – 100Pseudophosphorylation motif5

Sequence similaritiesi

Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOVERGENiHBG002025.
InParanoidiP09456.
KOiK04739.
OMAiQTMPESE.
OrthoDBiEOG091G0F1K.
PhylomeDBiP09456.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09456-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGSMAASE EERSLRECEL YVQKHNIQAL LKDSIVQLCT ARPERPMAFL
60 70 80 90 100
REYFERLEKE EARQIQSLQK SGIRTDSRED EISPPPPNPV VKGRRRRGAI
110 120 130 140 150
SAEVYTEEDA ASYVRKVIPK DYKTMAALAK AIEKNVLFSH LDDNERSDIF
160 170 180 190 200
DAMFPVSFIA GETVIQQGDE GDNFYVIDQG EMDVYVNNEW ATSVGEGGSF
210 220 230 240 250
GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL RKRKMYEEFL
260 270 280 290 300
SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGTA
310 320 330 340 350
AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL
360 370 380
DRPRFERVLG PCSDILKRNI QQYNSFVSLS V
Length:381
Mass (Da):43,095
Last modified:January 23, 2007 - v2
Checksum:iAF00CA8DECE462FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17086 mRNA. Translation: AAB54276.1.
PIRiA26910. OKRT1R.
RefSeqiNP_037313.1. NM_013181.1.
XP_008766533.1. XM_008768311.1.
XP_017452536.1. XM_017597047.1.
UniGeneiRn.10990.

Genome annotation databases

EnsembliENSRNOT00000071153; ENSRNOP00000067771; ENSRNOG00000049876.
GeneIDi25725.
KEGGirno:25725.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17086 mRNA. Translation: AAB54276.1.
PIRiA26910. OKRT1R.
RefSeqiNP_037313.1. NM_013181.1.
XP_008766533.1. XM_008768311.1.
XP_017452536.1. XM_017597047.1.
UniGeneiRn.10990.

3D structure databases

ProteinModelPortaliP09456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP09456. 2 interactors.
MINTiMINT-1775716.
STRINGi10116.ENSRNOP00000067771.

PTM databases

iPTMnetiP09456.
PhosphoSitePlusiP09456.

Proteomic databases

PaxDbiP09456.
PRIDEiP09456.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000071153; ENSRNOP00000067771; ENSRNOG00000049876.
GeneIDi25725.
KEGGirno:25725.

Organism-specific databases

CTDi5573.
RGDi3391. Prkar1a.

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOVERGENiHBG002025.
InParanoidiP09456.
KOiK04739.
OMAiQTMPESE.
OrthoDBiEOG091G0F1K.
PhylomeDBiP09456.

Enzyme and pathway databases

ReactomeiR-RNO-163615. PKA activation.
R-RNO-164378. PKA activation in glucagon signalling.
R-RNO-180024. DARPP-32 events.
R-RNO-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-RNO-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-RNO-5610787. Hedgehog 'off' state.
R-RNO-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

PROiP09456.

Gene expression databases

BgeeiENSRNOG00000049876.
GenevisibleiP09456. RN.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAP0_RAT
AccessioniPrimary (citable) accession number: P09456
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Two types of regulatory chains are found: type I, which predominates in skeletal muscle, and type II, which predominates in cardiac muscle.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.