ID A0AAF7A663_BOVIN Unreviewed; 348 AA. AC A0AAF7A663; DT 24-JUL-2024, integrated into UniProtKB/TrEMBL. DT 24-JUL-2024, sequence version 1. DT 02-OCT-2024, entry version 2. DE RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha {ECO:0000256|ARBA:ARBA00020608}; DE EC=2.7.11.11 {ECO:0000256|ARBA:ARBA00012444}; GN Name=PRKACA {ECO:0000313|VGNC:VGNC:50250}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000063436.2, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000063436.2, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000063436.2, RC ECO:0000313|Proteomes:UP000009136}; RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A., RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C., RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.; RT "ARS-UCD1.2."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSBTAP00000063436.2} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000063436.2}; RG Ensembl; RL Submitted (JUN-2024) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; CC Evidence={ECO:0000256|ARBA:ARBA00001036}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.11; Evidence={ECO:0000256|ARBA:ARBA00000541}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor CC {ECO:0000256|ARBA:ARBA00004635}. Mitochondrion CC {ECO:0000256|ARBA:ARBA00004173}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. cAMP subfamily. {ECO:0000256|ARBA:ARBA00007115}. 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 Ensembl; ENSBTAT00000085342.2; ENSBTAP00000063436.2; ENSBTAG00000006642.6. DR VGNC; VGNC:50250; PRKACA. DR GeneTree; ENSGT00940000162186; -. DR Proteomes; UP000009136; Chromosome 7. DR CDD; cd14209; STKc_PKA; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR044109; STKc_PKA. DR PANTHER; PTHR24353:SF82; CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA; 1. DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; cAMP {ECO:0000256|ARBA:ARBA00023149}; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00022707}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Myristate {ECO:0000256|ARBA:ARBA00022707}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 41..295 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 296..348 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51285" FT BINDING 70 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 348 AA; 40279 MW; D2102EAF32D4DD77 CRC64; GGNACFQASV QGVKEFLAKA KEDFLKKWEN PAQNTAHLDQ FERIKTLGTG SFGRVMLVKH METGNHYAMK ILDKQKVVKL KQIEHTLNEK RILQAVNFPF LVKLEFSFKD NSNLYMVMEY VPGGEMFSHL RRIGRFSEPH ARFYAAQIVL TFEYLHSLDL IYRDLKPENL LIDQQGYIQV TDFGFAKRVK GRTWTLCGTP EYLAPEIILS KGYNKAVDWW ALGVLIYEMA AGYPPFFADQ PIQIYEKIVS GKVRFPSHFS SDLKDLLRNL LQVDLTKRFG NLKNGVNDIK NHKWFATTDW IAIYQRKVEA PFIPKFKGPG DTSNFDDYEE EEIRVSINEK CGKEFSEF //