ID A0A2I2YB49_GORGO Unreviewed; 351 AA. AC A0A2I2YB49; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 27-NOV-2024, entry version 40. 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|Ensembl:ENSGGOP00000032040.1}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000032040.1, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000032040.1, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000032040.1, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=22398555; DOI=10.1038/nature10842; RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I., RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T., RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y., RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K., RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y., RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G., RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D., RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K., RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J., RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T., RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T., RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C., RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.; RT "Insights into hominid evolution from the gorilla genome sequence."; RL Nature 483:169-175(2012). RN [3] {ECO:0000313|Ensembl:ENSGGOP00000032040.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2024) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.11; CC Evidence={ECO:0000256|ARBA:ARBA00000541}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane CC {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 EMBL; CABD030111917; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030111918; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030111919; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030111920; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030111921; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_004060204.1; XM_004060156.2. DR AlphaFoldDB; A0A2I2YB49; -. DR SMR; A0A2I2YB49; -. DR STRING; 9593.ENSGGOP00000032040; -. DR Ensembl; ENSGGOT00000060240.1; ENSGGOP00000032040.1; ENSGGOG00000013294.3. DR GeneTree; ENSGT00940000162186; -. DR InParanoid; A0A2I2YB49; -. DR OMA; NDPFFDW; -. DR Proteomes; UP000001519; Chromosome 19. DR Bgee; ENSGGOG00000013294; Expressed in heart and 6 other cell types or tissues. DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl. DR GO; GO:0005930; C:axoneme; IEA:Ensembl. DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central. DR GO; GO:0005813; C:centrosome; IEA:Ensembl. DR GO; GO:0097546; C:ciliary base; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl. DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl. DR GO; GO:0098794; C:postsynapse; IEA:GOC. DR GO; GO:0036126; C:sperm flagellum; IEA:Ensembl. DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl. DR GO; GO:0030145; F:manganese ion binding; IEA:Ensembl. DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl. DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IBA:GO_Central. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0106310; F:protein serine kinase activity; IEA:Ensembl. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:Ensembl. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:0070417; P:cellular response to cold; IEA:Ensembl. DR GO; GO:0071377; P:cellular response to glucagon stimulus; IEA:Ensembl. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl. DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl. DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl. DR GO; GO:0006397; P:mRNA processing; IEA:Ensembl. DR GO; GO:1904539; P:negative regulation of glycolytic process through fructose-6-phosphate; IEA:Ensembl. DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IEA:Ensembl. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:Ensembl. DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl. DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IEA:Ensembl. DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl. DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl. DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl. DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl. DR GO; GO:0006611; P:protein export from nucleus; IEA:Ensembl. DR GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central. DR GO; GO:1990044; P:protein localization to lipid droplet; IEA:Ensembl. DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; IEA:Ensembl. DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl. DR GO; GO:0045667; P:regulation of osteoblast differentiation; IEA:Ensembl. DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEA:Ensembl. DR GO; GO:0070613; P:regulation of protein processing; IEA:Ensembl. DR GO; GO:0048240; P:sperm capacitation; IEA:Ensembl. DR CDD; cd14209; STKc_PKA; 1. DR FunFam; 3.30.200.20:FF:000005; cAMP-dependent protein kinase catalytic subunit; 1. DR FunFam; 1.10.510.10:FF:000005; cAMP-dependent protein kinase catalytic subunit alpha; 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:ARBA00023288}; 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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 44..298 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 299..351 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51285" FT BINDING 73 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 351 AA; 40590 MW; BF6D3ECD2614E5AB CRC64; MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WESPAQNTAH LDQFERIKTL GTGSFGRVML VKHKETGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFSE F //