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P00514

- KAP0_BOVIN

UniProt

P00514 - KAP0_BOVIN

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
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
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    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

    Keywords - Ligandi

    cAMP, cAMP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_202137. Regulation of water balance by renal 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.

    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-SubCell

    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 – 2310
    Helixi26 – 4015
    Helixi45 – 6117
    Helixi106 – 1094
    Helixi121 – 13313
    Helixi135 – 1373
    Beta strandi138 – 1403
    Helixi142 – 15110
    Beta strandi153 – 1575
    Beta strandi162 – 1643
    Beta strandi172 – 1798
    Beta strandi181 – 1855
    Beta strandi188 – 1936
    Helixi202 – 2065
    Beta strandi211 – 2188
    Beta strandi220 – 2267
    Helixi227 – 2337
    Helixi235 – 2406
    Helixi246 – 2505
    Helixi253 – 2553
    Helixi260 – 26910
    Beta strandi271 – 2755
    Beta strandi277 – 2793
    Beta strandi280 – 2823
    Beta strandi284 – 2863
    Beta strandi290 – 30415
    Beta strandi305 – 3095
    Beta strandi311 – 3177
    Beta strandi322 – 3243
    Helixi326 – 3283
    Beta strandi335 – 35016
    Helixi351 – 3588
    Helixi361 – 3655
    Helixi369 – 3757

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MASGTTASEE ERSLRECELY VQKHNIQALL KDSIVQLCTA RPERPMAFLR    50
    EYFEKLEKEE AKQIQNLQKA GSRADSREDE ISPPPPNPVV KGRRRRGAIS 100
    AEVYTEEDAA SYVRKVIPKD YKTMAALAKA IEKNVLFSHL DDNERSDIFD 150
    AMFPVSFIAG ETVIQQGDEG DNFYVIDQGE MDVYVNNEWA TSVGEGGSFG 200
    ELALIYGTPR AATVKAKTNV KLWGIDRDSY RRILMGSTLR KRKMYEEFLS 250
    KVSILESLDK WERLTVADAL EPVQFEDGQK IVVQGEPGDE FFIILEGSAA 300
    VLQRRSENEE FVEVGRLGPS DYFGEIALLM NRPRAATVVA RGPLKCVKLD 350
    RPRFERVLGP CSDILKRNIQ QYNSFVSLSV 380
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. Regulation of water balance by renal 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.

    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

    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: October 1, 2014
    This is version 140 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