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Protein

cAMP-dependent protein kinase type I-alpha regulatory subunit

Gene

PRKAR1A

Organism
Bos taurus (Bovine)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei201cAMP 11
Binding sitei210cAMP 11
Binding sitei325cAMP 21
Binding sitei334cAMP 21

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi136 – 253cAMP 1Add BLAST118
Nucleotide bindingi254 – 380cAMP 2Add BLAST127

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-163615. PKA activation.
R-BTA-164378. PKA activation in glucagon signalling.
R-BTA-180024. DARPP-32 events.
R-BTA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-BTA-5610787. Hedgehog 'off' state.
R-BTA-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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 19

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004232161 – 380cAMP-dependent protein kinase type I-alpha regulatory subunitAdd BLAST380
Initiator methionineiRemoved; alternate1 Publication
ChainiPRO_00002053762 – 380cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processedAdd BLAST379

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 processed1 Publication1
Modified residuei3PhosphoserineBy similarity1
Disulfide bondi17Interchain (with C-37)1 Publication
Disulfide bondi38Interchain (with C-16)1 Publication
Modified residuei76PhosphoserineBy similarity1
Modified residuei82PhosphoserineBy similarity1
Modified residuei100PhosphoserineBy similarity1
Modified residuei257PhosphoserineBy similarity1

Post-translational modificationi

The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity. The physiological significance of the in vitro phosphorylation of a proximal serine is unclear.

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP00514.
PRIDEiP00514.

PTM databases

iPTMnetiP00514.

Expressioni

Tissue specificityi

Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.

Gene expression databases

BgeeiENSBTAG00000008621.

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 (By similarity). Interacts with the phosphorylated form of PJA2 (By similarity). Interacts with CBFA2T3 (By similarity). Interacts with PRKX; regulates this cAMP-dependent protein kinase (By similarity). Interacts with smAKAP; this interaction may target PRKAR1A to the plasma membrane (By similarity). Interacts with AICDA (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-36644N.
IntActiP00514. 2 interactors.
MINTiMINT-1778627.
STRINGi9913.ENSBTAP00000011371.

Chemistry databases

BindingDBiP00514.

Structurei

Secondary structure

1380
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 23Combined sources10
Helixi26 – 40Combined sources15
Helixi45 – 61Combined sources17
Helixi106 – 109Combined sources4
Helixi121 – 133Combined sources13
Helixi135 – 137Combined sources3
Beta strandi138 – 140Combined sources3
Helixi142 – 151Combined sources10
Beta strandi153 – 157Combined sources5
Beta strandi162 – 164Combined sources3
Beta strandi172 – 179Combined sources8
Beta strandi181 – 185Combined sources5
Beta strandi188 – 193Combined sources6
Helixi202 – 206Combined sources5
Beta strandi211 – 218Combined sources8
Beta strandi220 – 226Combined sources7
Helixi227 – 233Combined sources7
Helixi235 – 240Combined sources6
Helixi246 – 250Combined sources5
Helixi253 – 255Combined sources3
Helixi260 – 269Combined sources10
Beta strandi271 – 275Combined sources5
Beta strandi277 – 279Combined sources3
Beta strandi280 – 282Combined sources3
Beta strandi284 – 286Combined sources3
Beta strandi290 – 304Combined sources15
Beta strandi305 – 309Combined sources5
Beta strandi311 – 317Combined sources7
Beta strandi322 – 324Combined sources3
Helixi326 – 328Combined sources3
Beta strandi335 – 350Combined sources16
Helixi351 – 358Combined sources8
Helixi361 – 365Combined sources5
Helixi369 – 375Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1APKmodel-A2-380[»]
1BPKmodel-A2-380[»]
1NE4X-ray2.40A95-377[»]
1NE6X-ray2.30A95-377[»]
1PVKmodel-A114-245[»]
1RGSX-ray2.80A93-380[»]
1RL3X-ray2.70A/B93-380[»]
2EZWNMR-A/B13-62[»]
2QCSX-ray2.20B91-380[»]
3FHIX-ray2.00B92-245[»]
3IIAX-ray2.70A92-245[»]
3IM3X-ray2.00A13-62[»]
3IM4X-ray2.28A/B13-62[»]
3PLQX-ray2.30A92-245[»]
3PNAX-ray1.50A/B92-245[»]
3PVBX-ray3.30B85-244[»]
4JV4X-ray2.95A93-377[»]
4MX3X-ray3.88A/B2-380[»]
4X6RX-ray2.40B91-380[»]
5HVZX-ray2.00A/B13-62[»]
DisProtiDP00245.
ProteinModelPortaliP00514.
SMRiP00514.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00514.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 135Dimerization and phosphorylationAdd BLAST134

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi95 – 99Pseudophosphorylation motif5

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
HOVERGENiHBG002025.
InParanoidiP00514.
KOiK04739.
OMAiRECERYV.
OrthoDBiEOG091G0F1K.
TreeFamiTF314920.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. 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.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
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.

P00514-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGTTASEE ERSLRECELY VQKHNIQALL KDSIVQLCTA RPERPMAFLR
60 70 80 90 100
EYFEKLEKEE AKQIQNLQKA GSRADSREDE ISPPPPNPVV KGRRRRGAIS
110 120 130 140 150
AEVYTEEDAA SYVRKVIPKD YKTMAALAKA IEKNVLFSHL DDNERSDIFD
160 170 180 190 200
AMFPVSFIAG ETVIQQGDEG DNFYVIDQGE MDVYVNNEWA TSVGEGGSFG
210 220 230 240 250
ELALIYGTPR AATVKAKTNV KLWGIDRDSY RRILMGSTLR KRKMYEEFLS
260 270 280 290 300
KVSILESLDK WERLTVADAL EPVQFEDGQK IVVQGEPGDE FFIILEGSAA
310 320 330 340 350
VLQRRSENEE FVEVGRLGPS DYFGEIALLM NRPRAATVVA RGPLKCVKLD
360 370 380
RPRFERVLGP CSDILKRNIQ QYNSFVSLSV
Length:380
Mass (Da):42,893
Last modified:April 17, 2007 - v2
Checksum:iB086A291809422F4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti230Y → N in AAA30708 (PubMed:6190178).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT030573 mRNA. Translation: ABQ13013.1.
BC118242 mRNA. Translation: AAI18243.1.
K00833 mRNA. Translation: AAA30708.1.
PIRiA00617. OKBO1R.
I45957.
RefSeqiNP_001069826.1. NM_001076358.1.
UniGeneiBt.10903.

Genome annotation databases

EnsembliENSBTAT00000011371; ENSBTAP00000011371; ENSBTAG00000008621.
GeneIDi615074.
KEGGibta:615074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT030573 mRNA. Translation: ABQ13013.1.
BC118242 mRNA. Translation: AAI18243.1.
K00833 mRNA. Translation: AAA30708.1.
PIRiA00617. OKBO1R.
I45957.
RefSeqiNP_001069826.1. NM_001076358.1.
UniGeneiBt.10903.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1APKmodel-A2-380[»]
1BPKmodel-A2-380[»]
1NE4X-ray2.40A95-377[»]
1NE6X-ray2.30A95-377[»]
1PVKmodel-A114-245[»]
1RGSX-ray2.80A93-380[»]
1RL3X-ray2.70A/B93-380[»]
2EZWNMR-A/B13-62[»]
2QCSX-ray2.20B91-380[»]
3FHIX-ray2.00B92-245[»]
3IIAX-ray2.70A92-245[»]
3IM3X-ray2.00A13-62[»]
3IM4X-ray2.28A/B13-62[»]
3PLQX-ray2.30A92-245[»]
3PNAX-ray1.50A/B92-245[»]
3PVBX-ray3.30B85-244[»]
4JV4X-ray2.95A93-377[»]
4MX3X-ray3.88A/B2-380[»]
4X6RX-ray2.40B91-380[»]
5HVZX-ray2.00A/B13-62[»]
DisProtiDP00245.
ProteinModelPortaliP00514.
SMRiP00514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36644N.
IntActiP00514. 2 interactors.
MINTiMINT-1778627.
STRINGi9913.ENSBTAP00000011371.

Chemistry databases

BindingDBiP00514.

PTM databases

iPTMnetiP00514.

Proteomic databases

PaxDbiP00514.
PRIDEiP00514.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000011371; ENSBTAP00000011371; ENSBTAG00000008621.
GeneIDi615074.
KEGGibta:615074.

Organism-specific databases

CTDi5573.

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
HOVERGENiHBG002025.
InParanoidiP00514.
KOiK04739.
OMAiRECERYV.
OrthoDBiEOG091G0F1K.
TreeFamiTF314920.

Enzyme and pathway databases

ReactomeiR-BTA-163615. PKA activation.
R-BTA-164378. PKA activation in glucagon signalling.
R-BTA-180024. DARPP-32 events.
R-BTA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-BTA-5610787. Hedgehog 'off' state.
R-BTA-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTraceiP00514.
PROiP00514.

Gene expression databases

BgeeiENSBTAG00000008621.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. 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.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
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_BOVIN
AccessioniPrimary (citable) accession number: P00514
Secondary accession number(s): A5D9F4, Q17QP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 17, 2007
Last modified: November 2, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.