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Protein

cAMP-dependent protein kinase type I-alpha regulatory subunit

Gene

Prkar1a

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

Functioni

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

Miscellaneous

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

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 domain specific binding Source: Ensembl
  • protein kinase A catalytic subunit binding Source: RGD
  • ubiquitin protein ligase binding Source: Ensembl

GO - Biological processi

Keywordsi

LigandcAMP, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi3391 Prkar1a

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

GuidetoPHARMACOLOGYi1472

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-protein interaction databases

IntActiP09456, 2 interactors
STRINGi10116.ENSRNOP00000067771

Structurei

3D structure databases

ProteinModelPortaliP09456
SMRiP09456
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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1113 Eukaryota
COG0664 LUCA
GeneTreeiENSGT00530000062947
HOVERGENiHBG002025
InParanoidiP09456
KOiK04739
OMAiVQLCTVR
OrthoDBiEOG091G0F1K
PhylomeDBiP09456

Family and domain databases

CDDicd00038 CAP_ED, 2 hits
Gene3Di2.60.120.10, 2 hits
InterProiView protein in InterPro
IPR012198 cAMP_dep_PK_reg_su
IPR003117 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
PfamiView protein in Pfam
PF00027 cNMP_binding, 2 hits
PF02197 RIIa, 1 hit
PIRSFiPIRSF000548 PK_regulatory, 1 hit
SMARTiView protein in SMART
SM00100 cNMP, 2 hits
SM00394 RIIa, 1 hit
SUPFAMiSSF51206 SSF51206, 2 hits
PROSITEiView protein in PROSITE
PS00888 CNMP_BINDING_1, 2 hits
PS00889 CNMP_BINDING_2, 2 hits
PS50042 CNMP_BINDING_3, 2 hits

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

Similar proteinsi

Entry informationi

Entry nameiKAP0_RAT
AccessioniPrimary (citable) accession number: P09456
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 144 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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