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P00514

- KAP0_BOVIN

UniProt

P00514 - KAP0_BOVIN

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Protein

cAMP-dependent protein kinase type I-alpha regulatory subunit

Gene

PRKAR1A

Organism
Bos taurus (Bovine)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei201 – 2011cAMP 1
Binding sitei210 – 2101cAMP 1
Binding sitei325 – 3251cAMP 2
Binding sitei334 – 3341cAMP 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi136 – 253118cAMP 1Add
BLAST
Nucleotide bindingi254 – 380127cAMP 2Add
BLAST

GO - Molecular functioni

  1. cAMP binding Source: UniProtKB-KW
  2. cAMP-dependent protein kinase inhibitor activity Source: Ensembl
  3. cAMP-dependent protein kinase regulator activity Source: Ensembl

GO - Biological processi

  1. cardiac muscle cell proliferation Source: Ensembl
  2. mesoderm formation Source: Ensembl
  3. negative regulation of cAMP-dependent protein kinase activity Source: Ensembl
  4. sarcomere organization Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_202137. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_205490. DARPP-32 events.
REACT_213932. PKA activation.
REACT_215067. Factors involved in megakaryocyte development and platelet production.
REACT_217846. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_219718. PKA activation in glucagon signalling.
REACT_270061. Hedgehog 'off' state.

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
ProteomesiUP000009136: Chromosome 19

Subcellular locationi

Cell membrane By similarity

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: Ensembl
  2. cAMP-dependent protein kinase complex Source: InterPro
  3. neuromuscular junction Source: Ensembl
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380cAMP-dependent protein kinase type I-alpha regulatory subunitPRO_0000423216Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 380379cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processedPRO_0000205376Add
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 processed
Disulfide bondi17 – 17Interchain (with C-37)1 Publication
Disulfide bondi38 – 38Interchain (with C-16)1 Publication
Modified residuei82 – 821PhosphoserineBy similarity
Modified residuei100 – 1001PhosphoserineBy similarity

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

PRIDEiP00514.

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.

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 interactions.
MINTiMINT-1778627.
STRINGi9913.ENSBTAP00000011371.

Structurei

Secondary structure

1
380
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2310Combined sources
Helixi26 – 4015Combined sources
Helixi45 – 6117Combined sources
Helixi106 – 1094Combined sources
Helixi121 – 13313Combined sources
Helixi135 – 1373Combined sources
Beta strandi138 – 1403Combined sources
Helixi142 – 15110Combined sources
Beta strandi153 – 1575Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi172 – 1798Combined sources
Beta strandi181 – 1855Combined sources
Beta strandi188 – 1936Combined sources
Helixi202 – 2065Combined sources
Beta strandi211 – 2188Combined sources
Beta strandi220 – 2267Combined sources
Helixi227 – 2337Combined sources
Helixi235 – 2406Combined sources
Helixi246 – 2505Combined sources
Helixi253 – 2553Combined sources
Helixi260 – 26910Combined sources
Beta strandi271 – 2755Combined sources
Beta strandi277 – 2793Combined sources
Beta strandi280 – 2823Combined sources
Beta strandi284 – 2863Combined sources
Beta strandi290 – 30415Combined sources
Beta strandi305 – 3095Combined sources
Beta strandi311 – 3177Combined sources
Beta strandi322 – 3243Combined sources
Helixi326 – 3283Combined sources
Beta strandi335 – 35016Combined sources
Helixi351 – 3588Combined sources
Helixi361 – 3655Combined sources
Helixi369 – 3757Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00245.
ProteinModelPortaliP00514.
SMRiP00514. Positions 13-62, 110-377.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00514.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 135134Dimerization and phosphorylationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi95 – 995Pseudophosphorylation motif

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0664.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
HOVERGENiHBG002025.
InParanoidiP00514.
KOiK04739.
OMAiXVIPKDY.
OrthoDBiEOG72JWG6.
TreeFamiTF314920.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR002373. cAMP/cGMP_kin.
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.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
PRINTSiPR00103. CAMPKINASE.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti230 – 2301Y → N in AAA30708. (PubMed:6190178)Curated

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 .
PIRi A00617. OKBO1R.
I45957.
RefSeqi NP_001069826.1. NM_001076358.1.
UniGenei Bt.10903.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1APK model - A 2-380 [» ]
1BPK model - A 2-380 [» ]
1NE4 X-ray 2.40 A 95-377 [» ]
1NE6 X-ray 2.30 A 95-377 [» ]
1PVK model - A 114-245 [» ]
1RGS X-ray 2.80 A 93-380 [» ]
1RL3 X-ray 2.70 A/B 93-380 [» ]
2EZW NMR - A/B 13-62 [» ]
2QCS X-ray 2.20 B 91-380 [» ]
3FHI X-ray 2.00 B 92-245 [» ]
3IIA X-ray 2.70 A 92-245 [» ]
3IM3 X-ray 2.00 A 13-62 [» ]
3IM4 X-ray 2.28 A/B 13-62 [» ]
3PLQ X-ray 2.30 A 92-245 [» ]
3PNA X-ray 1.50 A/B 92-245 [» ]
3PVB X-ray 3.30 B 85-244 [» ]
4JV4 X-ray 2.95 A 93-377 [» ]
4MX3 X-ray 3.88 A/B 2-380 [» ]
DisProti DP00245.
ProteinModelPortali P00514.
SMRi P00514. Positions 13-62, 110-377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-36644N.
IntActi P00514. 2 interactions.
MINTi MINT-1778627.
STRINGi 9913.ENSBTAP00000011371.

Chemistry

BindingDBi P00514.

Proteomic databases

PRIDEi P00514.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000011371 ; ENSBTAP00000011371 ; ENSBTAG00000008621 .
GeneIDi 615074.
KEGGi bta:615074.

Organism-specific databases

CTDi 5573.

Phylogenomic databases

eggNOGi COG0664.
GeneTreei ENSGT00530000062947.
HOGENOMi HOG000196669.
HOVERGENi HBG002025.
InParanoidi P00514.
KOi K04739.
OMAi XVIPKDY.
OrthoDBi EOG72JWG6.
TreeFami TF314920.

Enzyme and pathway databases

Reactomei REACT_202137. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_205490. DARPP-32 events.
REACT_213932. PKA activation.
REACT_215067. Factors involved in megakaryocyte development and platelet production.
REACT_217846. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_219718. PKA activation in glucagon signalling.
REACT_270061. Hedgehog 'off' state.

Miscellaneous databases

EvolutionaryTracei P00514.
NextBioi 20899431.

Family and domain databases

Gene3Di 2.60.120.10. 2 hits.
InterProi IPR002373. cAMP/cGMP_kin.
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.
[Graphical view ]
Pfami PF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view ]
PIRSFi PIRSF000548. PK_regulatory. 1 hit.
PRINTSi PR00103. CAMPKINASE.
SMARTi SM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view ]
SUPFAMi SSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEi PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Basal ganglia.
  3. "Amino acid sequence of the regulatory subunit of bovine type I adenosine cyclic 3',5'-phosphate dependent protein kinase."
    Titani K., Sasagawa T., Ericsson L.H., Kumar S., Smith S.B., Krebs E.G., Walsh K.A.
    Biochemistry 23:4193-4199(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-380.
  4. "Isolation of a cDNA clone for the type I regulatory subunit of bovine cAMP-dependent protein kinase."
    Lee D.C., Carmichael D.F., Krebs E.G., McKnight G.S.
    Proc. Natl. Acad. Sci. U.S.A. 80:3608-3612(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 214-232.
  5. "Predicted structures of cAMP binding domains of type I and II regulatory subunits of cAMP-dependent protein kinase."
    Weber I.T., Steitz T.A., Bubis J., Taylor S.S.
    Biochemistry 26:343-351(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  6. "Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains."
    Su Y., Dostmann W.R., Herberg F.W., Durick K., Xuong N.H., ten Eyck L., Taylor S.S., Varughese K.I.
    Science 269:807-813(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 114-380.
  7. "Antiparallel alignment of the two protomers of the regulatory subunit dimer of cAMP-dependent protein kinase I."
    Bubis J., Vedvick T.S., Taylor S.S.
    J. Biol. Chem. 262:14961-14966(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.

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 26, 2014
This is version 142 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

External Data

Dasty 3