LOCUS       NP_062137                401 aa            linear   ROD 29-JUL-2024
DEFINITION  cAMP-dependent protein kinase type II-alpha regulatory subunit
            [Rattus norvegicus].
ACCESSION   NP_062137
VERSION     NP_062137.1
DBSOURCE    REFSEQ: accession NM_019264.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Isensee,J., Kaufholz,M., Knape,M.J., Hasenauer,J., Hammerich,H.,
            Gonczarowska-Jorge,H., Zahedi,R.P., Schwede,F., Herberg,F.W. and
            Hucho,T.
  TITLE     PKA-RII subunit phosphorylation precedes activation by cAMP and
            regulates activity termination
  JOURNAL   J Cell Biol 217 (6), 2167-2184 (2018)
   PUBMED   29615473
  REMARK    GeneRIF: RII phosphorylation precedes cAMP binding and controls the
            inactivation by modulating the reassociation involving the
            coordinated action of phosphodiesterases and phosphatases.
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Burgers,P.P., van der Heyden,M.A., Kok,B., Heck,A.J. and
            Scholten,A.
  TITLE     A systematic evaluation of protein kinase A-A-kinase anchoring
            protein interaction motifs
  JOURNAL   Biochemistry 54 (1), 11-21 (2015)
   PUBMED   25097019
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Nishimura,T., Fujii,W., Sugiura,K. and Naito,K.
  TITLE     Cytoplasmic anchoring of cAMP-dependent protein kinase (PKA) by
            A-kinase anchor proteins (AKAPs) is required for meiotic arrest of
            porcine full-grown and growing oocytes
  JOURNAL   Biol Reprod 90 (3), 58 (2014)
   PUBMED   24501172
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Biesemann,C., Gronborg,M., Luquet,E., Wichert,S.P., Bernard,V.,
            Bungers,S.R., Cooper,B., Varoqueaux,F., Li,L., Byrne,J.A.,
            Urlaub,H., Jahn,O., Brose,N. and Herzog,E.
  TITLE     Proteomic screening of glutamatergic mouse brain synaptosomes
            isolated by fluorescence activated sorting
  JOURNAL   EMBO J 33 (2), 157-170 (2014)
   PUBMED   24413018
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Nishimura,T., Sugiura,K. and Naito,K.
  TITLE     A-kinase anchor protein 1 (AKAP1) regulates cAMP-dependent protein
            kinase (PKA) localization and is involved in meiotic maturation of
            porcine oocytes
  JOURNAL   Biol Reprod 88 (4), 85 (2013)
   PUBMED   23426434
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Kultgen,P.L., Byrd,S.K., Ostrowski,L.E. and Milgram,S.L.
  TITLE     Characterization of an A-kinase anchoring protein in human ciliary
            axonemes
  JOURNAL   Mol Biol Cell 13 (12), 4156-4166 (2002)
   PUBMED   12475942
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Dwivedi,Y., Rizavi,H.S. and Pandey,G.N.
  TITLE     Differential effects of haloperidol and clozapine on [(3)H]cAMP
            binding, protein kinase A (PKA) activity, and mRNA and protein
            expression of selective regulatory and catalytic subunit isoforms
            of PKA in rat brain
  JOURNAL   J Pharmacol Exp Ther 301 (1), 197-209 (2002)
   PUBMED   11907174
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Marx,S.O., Reiken,S., Hisamatsu,Y., Jayaraman,T., Burkhoff,D.,
            Rosemblit,N. and Marks,A.R.
  TITLE     PKA phosphorylation dissociates FKBP12.6 from the calcium release
            channel (ryanodine receptor): defective regulation in failing
            hearts
  JOURNAL   Cell 101 (4), 365-376 (2000)
   PUBMED   10830164
REFERENCE   9  (residues 1 to 401)
  AUTHORS   Feliciello,A., Cardone,L., Garbi,C., Ginsberg,M.D., Varrone,S.,
            Rubin,C.S., Avvedimento,E.V. and Gottesman,M.E.
  TITLE     Yotiao protein, a ligand for the NMDA receptor, binds and targets
            cAMP-dependent protein kinase II(1)
  JOURNAL   FEBS Lett 464 (3), 174-178 (1999)
   PUBMED   10618500
REFERENCE   10 (residues 1 to 401)
  AUTHORS   Scott,J.D., Glaccum,M.B., Zoller,M.J., Uhler,M.D., Helfman,D.M.,
            McKnight,G.S. and Krebs,E.G.
  TITLE     The molecular cloning of a type II regulatory subunit of the
            cAMP-dependent protein kinase from rat skeletal muscle and mouse
            brain
  JOURNAL   Proc Natl Acad Sci U S A 84 (15), 5192-5196 (1987)
   PUBMED   3037538
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF533978.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF533978.1, J02934.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Rattus norvegicus"
                     /strain="Sprague-Dawley"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q32"
     Protein         1..401
                     /product="cAMP-dependent protein kinase type II-alpha
                     regulatory subunit"
                     /EC_number="2.7.11.1"
                     /note="protein kinase, cAMP-dependent, regulatory subunit
                     type II alpha; protein kinase, cAMP-dependent, regulatory,
                     type 2, alpha; protein kinase cAMP-dependent type 2
                     regulatory subunit alpha; protein kinase, cAMP dependent
                     regulatory, type II alpha"
                     /calculated_mol_wt=45409
     Region          2..135
                     /region_name="Dimerization and phosphorylation"
                     /note="propagated from UniProtKB/Swiss-Prot (P12368.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P13861; propagated from
                     UniProtKB/Swiss-Prot (P12368.4)"
     Region          4..44
                     /region_name="DD_RIIalpha_PKA"
                     /note="dimerization/docking (D/D) domain of the Type II
                     alpha Regulatory subunit of cAMP-dependent protein kinase;
                     cd12103"
                     /db_xref="CDD:438524"
     Site            order(4..8,10,13..14,17..18,21..22,25,28..31,33..34,
                     37..38,40..41)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:438524"
     Site            order(6,10..11,14..15,18..19,22..23)
                     /site_type="other"
                     /note="AKAP interaction site [polypeptide binding]"
                     /db_xref="CDD:438524"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13861; propagated from
                     UniProtKB/Swiss-Prot (P12368.4)"
     Region          55..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12368.4)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13861; propagated from
                     UniProtKB/Swiss-Prot (P12368.4)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13861; propagated from
                     UniProtKB/Swiss-Prot (P12368.4)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16641100,
                     ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P12368.4)"
     Region          136..248
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(204..205,214..216)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PDPK1.
                     /evidence=ECO:0000250|UniProtKB:P00515; propagated from
                     UniProtKB/Swiss-Prot (P12368.4)"
     Site            order(236..238,242..244)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Region          258..379
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(334..335,344..346)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13861; propagated from
                     UniProtKB/Swiss-Prot (P12368.4)"
     Site            order(366..368,372..374)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P12368.4)"
     CDS             1..401
                     /gene="Prkar2a"
                     /coded_by="NM_019264.2:110..1315"
                     /db_xref="GeneID:29699"
                     /db_xref="RGD:3393"
ORIGIN      
        1 mshiqippgl tellqgytve vlrqqppdlv dfaveyftrl rearrqesds fiappttfha
       61 qessgvpvie edgesesdsd dedlevpips kftrrvsvca etfnpdeeed ndprvvhpkt
      121 deqryrlqea ckdillfknl dqeqlsqvld amfekivktd ehvidqgddg dnfyviergt
      181 ydilvtkdnq trsvgqydnr gsfgelalmy ntpraativa tsdgslwgld rvtfrriivk
      241 nnakkrkmfe sfiesvplfk slemsermki vdvigekiyk dgeriitqge kadsfyiies
      301 gevsilirsk tktnknggnq eveiahchkg qyfgelalvt nkpraasaya vgdvkclvmd
      361 vqaferllgp cmdimkrnis hyeeqlvkmf gsnldlldpg q
//
