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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei202 – 2021cAMP 1
Binding sitei211 – 2111cAMP 1
Binding sitei326 – 3261cAMP 2
Binding sitei335 – 3351cAMP 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi137 – 254118cAMP 1Add
BLAST
Nucleotide bindingi255 – 381127cAMP 2Add
BLAST

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-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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381cAMP-dependent protein kinase type I-alpha regulatory subunitPRO_0000423218Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 381380cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processedPRO_0000205380Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylalanine; in cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processedBy similarity
Modified residuei3 – 31PhosphoserineCombined sources
Disulfide bondi18 – 18Interchain (with C-39)By similarity
Disulfide bondi39 – 39Interchain (with C-18)By similarity
Modified residuei75 – 751PhosphothreonineBy similarity
Modified residuei77 – 771PhosphoserineBy similarity
Modified residuei83 – 831PhosphoserineCombined sources
Modified residuei101 – 1011PhosphoserineBy similarity
Modified residuei258 – 2581PhosphoserineCombined sources

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.
PhosphoSiteiP09456.

Expressioni

Gene expression databases

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 interactions.
MINTiMINT-1775716.
STRINGi10116.ENSRNOP00000067771.

Structurei

3D structure databases

ProteinModelPortaliP09456.
SMRiP09456. Positions 14-63, 92-381.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 136135Dimerization and phosphorylationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi96 – 1005Pseudophosphorylation motif

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.
OrthoDBiEOG72JWG6.
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.
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.
UniGeneiRn.10990.

3D structure databases

ProteinModelPortaliP09456.
SMRiP09456. Positions 14-63, 92-381.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP09456.
PhosphoSiteiP09456.

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.
OrthoDBiEOG72JWG6.
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-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

NextBioi607833.
PROiP09456.

Gene expression databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and cDNA structure of the regulatory subunit of type I cAMP-dependent protein kinase from rat brain."
    Kuno T., Ono Y., Hirai M., Hashimoto S., Shuntoh H., Tanaka C.
    Biochem. Biophys. Res. Commun. 146:878-883(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-83 AND SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: January 20, 2016
This is version 127 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.