ID Q3ZB92_DANRE Unreviewed; 351 AA. AC Q3ZB92; DT 27-SEP-2005, integrated into UniProtKB/TrEMBL. DT 27-SEP-2005, sequence version 1. DT 03-AUG-2022, entry version 150. DE RecName: Full=cAMP-dependent protein kinase {ECO:0000256|ARBA:ARBA00012444}; DE EC=2.7.11.11 {ECO:0000256|ARBA:ARBA00012444}; GN Name=prkacb {ECO:0000313|EMBL:AAI03488.1}; GN OrderedLocusNames=prkacbb {ECO:0000313|Ensembl:ENSDARP00000076580, GN ECO:0000313|ZFIN:ZDB-GENE-050904-4}; GN ORFNames=SO:0001217 {ECO:0000313|ZFIN:ZDB-GENE-050904-4}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI03488.1}; RN [1] {ECO:0000313|EMBL:AAI03488.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Singapore local strain {ECO:0000313|EMBL:AAI03488.1}; RC TISSUE=Embryo {ECO:0000313|EMBL:AAI03488.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSDARP00000076580} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000076580}; RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. RN [3] {ECO:0000313|Ensembl:ENSDARP00000076580} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000076580}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). 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 -!- 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; CR848026; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; FP015789; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC103487; AAI03488.1; -; mRNA. DR RefSeq; NP_001030148.1; NM_001034976.1. DR RefSeq; XP_017206779.1; XM_017351290.1. DR STRING; 7955.ENSDARP00000076580; -. DR Ensembl; ENSDART00000082143.6; ENSDARP00000076580.3; ENSDARG00000059125.6. DR GeneID; 563147; -. DR KEGG; dre:563147; -. DR CTD; 563147; -. DR ZFIN; ZDB-GENE-050904-4; prkacbb. DR ZFIN; ZDB-GENE-050904-4; SO:0001217. DR eggNOG; KOG0616; Eukaryota. DR GeneTree; ENSGT00940000163111; -. DR OMA; GNARYNK; -. DR OrthoDB; 963519at2759; -. DR TreeFam; TF313399; -. DR Reactome; R-DRE-163615; PKA activation. DR Reactome; R-DRE-164378; PKA activation in glucagon signalling. DR Reactome; R-DRE-180024; DARPP-32 events. DR Reactome; R-DRE-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR Reactome; R-DRE-392517; Rap1 signalling. DR Reactome; R-DRE-422356; Regulation of insulin secretion. DR Reactome; R-DRE-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR Reactome; R-DRE-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-DRE-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase. DR Reactome; R-DRE-5610785; GLI3 is processed to GLI3R by the proteasome. DR Reactome; R-DRE-5610787; Hedgehog 'off' state. DR Reactome; R-DRE-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-DRE-8853659; RET signaling. DR Reactome; R-DRE-8963896; HDL assembly. DR Reactome; R-DRE-9634597; GPER1 signaling. DR Reactome; R-DRE-983231; Factors involved in megakaryocyte development and platelet production. DR Proteomes; UP000814640; Chromosome 2. DR Bgee; ENSDARG00000059125; Expressed in early embryo and 34 other tissues. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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; IEA:UniProtKB-EC. DR GO; GO:0010737; P:protein kinase A signaling; IBA:GO_Central. DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro. DR CDD; cd14209; STKc_PKA; 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 Pfam; PF00069; Pkinase; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 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 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; cAMP {ECO:0000256|ARBA:ARBA00023149}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAI03488.1}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00022707}; KW Myristate {ECO:0000256|ARBA:ARBA00022707}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q3ZB92}; 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; 40650 MW; 969567145CA2C677 CRC64; MGNAATAKKG NELESVKEFL AKAKEDFLRK WESPQQSTTC LDDFDRQKTL GTGSFGRVLL VKHKASDQYY AMKVLDKQKV VKLKQVEHTL NEKRILQAVS FPFLVRLEYA FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQHGY IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLRNGVN DIKNHKWFAT TDWIAIYERK VEAPFIPKCR GPGDTSNFDD YEEEDIRVSV TEKCAKEFSE F //