ID F1R506_DANRE Unreviewed; 713 AA. AC F1R506; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 3. DT 03-AUG-2022, entry version 86. DE RecName: Full=Protein kinase C {ECO:0000256|ARBA:ARBA00012429, ECO:0000256|PIRNR:PIRNR000551}; DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429, ECO:0000256|PIRNR:PIRNR000551}; GN OrderedLocusNames=prkcq {ECO:0000313|Ensembl:ENSDARP00000046252, GN ECO:0000313|ZFIN:ZDB-GENE-041210-195}; GN ORFNames=SO:0001217 {ECO:0000313|ZFIN:ZDB-GENE-041210-195}; 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|Ensembl:ENSDARP00000046252}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000046252} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000046252}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000046252} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000046252}; 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=2.7.11.13; CC Evidence={ECO:0000256|ARBA:ARBA00000946}; 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=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569, CC ECO:0000256|PIRNR:PIRNR000551}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490, CC ECO:0000256|PIRNR:PIRNR000551}. 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; AL954652; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001082839.2; NM_001089370.2. DR AlphaFoldDB; F1R506; -. DR SMR; F1R506; -. DR STRING; 7955.ENSDARP00000046252; -. DR PaxDb; F1R506; -. DR Ensembl; ENSDART00000046253.5; ENSDARP00000046252.5; ENSDARG00000034173.9. DR GeneID; 555521; -. DR KEGG; dre:555521; -. DR CTD; 5588; -. DR ZFIN; ZDB-GENE-041210-195; prkcq. DR ZFIN; ZDB-GENE-041210-195; SO:0001217. DR eggNOG; KOG0694; Eukaryota. DR GeneTree; ENSGT00940000157638; -. DR InParanoid; F1R506; -. DR OrthoDB; 222529at2759; -. DR TreeFam; TF102004; -. DR Reactome; R-DRE-111465; Apoptotic cleavage of cellular proteins. DR Reactome; R-DRE-114508; Effects of PIP2 hydrolysis. DR Reactome; R-DRE-202424; Downstream TCR signaling. DR Reactome; R-DRE-2871837; FCERI mediated NF-kB activation. DR Reactome; R-DRE-373752; Netrin-1 signaling. DR Reactome; R-DRE-9648002; RAS processing. DR Proteomes; UP000814640; Chromosome 4. DR Bgee; ENSDARG00000034173; Expressed in muscle tissue and 16 other tissues. DR ExpressionAtlas; F1R506; baseline. DR GO; GO:0001772; C:immunological synapse; IDA:ZFIN. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0048513; P:animal organ development; IEA:UniProt. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central. DR CDD; cd00029; C1; 2. DR CDD; cd05619; STKc_nPKC_theta; 1. DR Gene3D; 2.60.40.150; -; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR020454; DAG/PE-bd. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR034668; nPKC_theta. DR InterPro; IPR002219; PE/DAG-bd. DR InterPro; IPR017892; Pkinase_C. DR InterPro; IPR014376; Prot_kin_PKC_delta. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00130; C1_1; 2. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR PIRSF; PIRSF000551; PKC_delta; 1. DR PRINTS; PR00008; DAGPEDOMAIN. DR SMART; SM00109; C1; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF49562; SSF49562; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR SUPFAM; SSF57889; SSF57889; 2. 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. DR PROSITE; PS00479; ZF_DAG_PE_1; 1. DR PROSITE; PS50081; ZF_DAG_PE_2; 2. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000551}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000551}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022771}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR000551}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|PIRNR:PIRNR000551}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000551}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 159..209 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT DOMAIN 231..281 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT DOMAIN 386..640 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 641..712 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51285" FT REGION 298..372 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 351..372 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 510 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000551-50" FT BINDING 392..400 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51" FT BINDING 415 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51, FT ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 713 AA; 81868 MW; BF40C104194AB191 CRC64; MSPFLRIAFS SFEMDPGLAY HEEVLNPYCA VYMKEAVETE KGQVYKQKRP TMYPPWSSTF DAHVHKGRVM HVVVKDKTAE LKTEATVQLD TLASRCKKEN GKLEIWVELK PQGRLLMEAR YFLERSGEHG ETEREKEGVF ALHHRRGAIK QAKVHVVKCH EFTATFFPQP TFCSVCKEFV WGLNKQGYQC RQCNAAIHKK CIDKVIAKCT GSAVNSKETM IHKERFKIDM PHRFKVYNYM SPTFCEHCGT LLWGLARQGL KCEECGMNVH HKCQKKVANL CGVNQKLMAE ALAMIESTQQ QARSSRDTET VGREGPVSAD QPGVIREPSG RLAISPLTPA PPLPRKEHQG ISWDSPADGR RPSLEEPEPL YATPRKEHHK FTIDSFILHK MLGKGSFGKV FLAELKGSGQ FFAVKALKKD VVLMDDDVEC TMVERRVLSL AWDHPFLTHL YCTFQTKENL FFVMEYLNGG DLMFHIQTCH RFDLPRSTFY AAEIICGLQF LHSKGIVYRD LKLDNILLDT DGHIKIADFG MCKENIIGEA RTCTFCGTPD YIAPEILLGQ KYGTSVDWWS FGVLLYEMLI GQSPFHGHDE EELFQSIRTD DPCYPRWLTR DARDILVKLF VREPERRLGV KGNIRQHPFF RETDWSALEE RQVEPPFKPT VKSANDCSNF DKEFINEKPR LSVTDRMMIN SMDQSMFENF SFINPIMTRL KSP //