GenomeNet

Database: UniProt
Entry: F7IC18_CALJA
LinkDB: F7IC18_CALJA
Original site: F7IC18_CALJA 
ID   F7IC18_CALJA            Unreviewed;       404 AA.
AC   F7IC18;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=cAMP-dependent protein kinase type II-alpha regulatory subunit {ECO:0000256|ARBA:ARBA00041039};
GN   Name=PRKAR2A {ECO:0000313|EMBL:JAB08691.1,
GN   ECO:0000313|Ensembl:ENSCJAP00000005968.1};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB08691.1};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000005968.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB08691.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Bladder {ECO:0000313|EMBL:JAB08691.1}, Cerebellum
RC   {ECO:0000313|EMBL:JAB41934.1}, Cerebral cortex
RC   {ECO:0000313|EMBL:JAB28834.1}, Hippocampus
RC   {ECO:0000313|EMBL:JAB14919.1}, and Skeletal muscle
RC   {ECO:0000313|EMBL:JAB36646.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
RN   [3] {ECO:0000313|Ensembl:ENSCJAP00000005968.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
CC       involved in cAMP signaling in cells. Type II regulatory chains mediate
CC       membrane association by binding to anchoring proteins, including the
CC       MAP2 kinase. {ECO:0000256|ARBA:ARBA00037198}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family. {ECO:0000256|ARBA:ARBA00005753}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GAMT01003170; JAB08691.1; -; mRNA.
DR   EMBL; GAMS01008217; JAB14919.1; -; mRNA.
DR   EMBL; GAMR01005098; JAB28834.1; -; mRNA.
DR   EMBL; GAMQ01005205; JAB36646.1; -; mRNA.
DR   EMBL; GAMP01010821; JAB41934.1; -; mRNA.
DR   RefSeq; XP_003734888.1; XM_003734840.3.
DR   STRING; 9483.ENSCJAP00000005968; -.
DR   Ensembl; ENSCJAT00000006290.3; ENSCJAP00000005968.1; ENSCJAG00000003255.3.
DR   GeneID; 100415419; -.
DR   KEGG; cjc:100415419; -.
DR   CTD; 5576; -.
DR   eggNOG; KOG1113; Eukaryota.
DR   GeneTree; ENSGT00940000154836; -.
DR   OMA; NPYERSK; -.
DR   OrthoDB; 55978at2759; -.
DR   TreeFam; TF314920; -.
DR   Proteomes; UP000008225; Chromosome 15.
DR   Bgee; ENSCJAG00000003255; Expressed in heart and 6 other cell types or tissues.
DR   GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:Ensembl.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:Ensembl.
DR   GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0034236; F:protein kinase A catalytic subunit binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd12103; DD_RIIalpha_PKA; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR   PANTHER; PTHR11635:SF153; CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA REGULATORY SUBUNIT; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   2: Evidence at transcript level;
KW   cAMP {ECO:0000256|ARBA:ARBA00023149, ECO:0000256|PIRSR:PIRSR000548-1};
KW   cAMP-binding {ECO:0000256|ARBA:ARBA00022566, ECO:0000256|PIRSR:PIRSR000548-
KW   1}; Kinase {ECO:0000313|EMBL:JAB08691.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000548-1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|EMBL:JAB08691.1}.
FT   DOMAIN          139..258
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          261..388
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          47..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         208
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT   BINDING         217
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT   BINDING         338
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT   BINDING         347
FT                   /ligand="3',5'-cyclic AMP"
FT                   /ligand_id="ChEBI:CHEBI:58165"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
SQ   SEQUENCE   404 AA;  45569 MW;  FD516727488DB52E CRC64;
     MSHIQIPPGL TELLQGYTVE VLRQQPPDLV KFAVDYFTRL REARAPASVL PDATPRQSLG
     HTTPEPGPDH VADANGDSES EEDEDLEVPV PSRFNRRVSV CAETYNPDEE EEDTDPRVIH
     PKTDEQRCRL QEACKDILLF KNLDQEQLSQ VLDAMFERIV KADEHVIDQG DDGDNFYVIE
     RGTYDILVTK NNQTRSVGQY DNRGSFGELA LMYNTPRAAT IVATSEGSLW GLDRVTFRRI
     IVKNNAKKRK MFESFIESVP LLKSLELSER MKIVDVIGEK IYKDGERIIT QGEKADSFYI
     IESGEVSILI RSKTKSNKDG GNQEVEITRC HKGQYFGELA LVTNKPRAAS AYAVGDVKCL
     VMDVQAFERL LGPCMDIMKR NISHYEEQLV KMFGSSMDLG NLGQ
//
DBGET integrated database retrieval system