ID F1R506_DANRE Unreviewed; 719 AA. AC F1R506; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 2. DT 28-FEB-2018, entry version 58. DE RecName: Full=Protein kinase C {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00929532}; DE EC=2.7.11.13 {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00929532}; GN Name=prkcq {ECO:0000313|Ensembl:ENSDARP00000046252, GN 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 Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000046252, ECO:0000313|Proteomes:UP000000437}; 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, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000046252, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA 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., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA 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., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [3] {ECO:0000313|Ensembl:ENSDARP00000144017} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000144017}; RG Ensembl; RL Submitted (OCT-2017) to UniProtKB. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00935732}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. PKC subfamily. CC {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00929254}. CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSDARP00000046252}. 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; XP_005164878.1; XM_005164821.3. DR RefSeq; XP_009298659.1; XM_009300384.2. DR RefSeq; XP_009298660.1; XM_009300385.2. DR UniGene; Dr.88140; -. DR UniGene; Dr.93138; -. DR SMR; F1R506; -. DR STRING; 7955.ENSDARP00000046252; -. DR PaxDb; F1R506; -. DR Ensembl; ENSDART00000046253; ENSDARP00000046252; ENSDARG00000034173. DR Ensembl; ENSDART00000176982; ENSDARP00000144017; ENSDARG00000034173. DR GeneID; 555521; -. DR CTD; 5588; -. DR ZFIN; ZDB-GENE-041210-195; prkcq. DR eggNOG; KOG0694; Eukaryota. DR eggNOG; ENOG410XNPH; LUCA. DR GeneTree; ENSGT00820000126964; -. DR InParanoid; F1R506; -. DR OMA; EPQGISW; -. DR OrthoDB; EOG091G0QRS; -. 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 Proteomes; UP000000437; Chromosome 4. DR Bgee; ENSDARG00000034173; -. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. 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; 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 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|PIRNR:PIRNR000551, KW ECO:0000256|PIRSR:PIRSR000551-51, ECO:0000256|SAAS:SAAS00593399}; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Kinase {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00593820}; KW Metal-binding {ECO:0000256|SAAS:SAAS00515414}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000551, KW ECO:0000256|PIRSR:PIRSR000551-51, ECO:0000256|SAAS:SAAS00593601}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000551, KW ECO:0000256|SAAS:SAAS00593706}; KW Transferase {ECO:0000256|PIRNR:PIRNR000551, KW ECO:0000256|SAAS:SAAS00592725}; Zinc {ECO:0000256|SAAS:SAAS00515409}; KW Zinc-finger {ECO:0000256|SAAS:SAAS00732991}. FT DOMAIN 165 215 Phorbol-ester/DAG-type. FT {ECO:0000259|PROSITE:PS50081}. FT DOMAIN 237 287 Phorbol-ester/DAG-type. FT {ECO:0000259|PROSITE:PS50081}. FT DOMAIN 392 646 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT DOMAIN 647 718 AGC-kinase C-terminal. FT {ECO:0000259|PROSITE:PS51285}. FT NP_BIND 398 406 ATP. {ECO:0000256|PIRSR:PIRSR000551-51}. FT ACT_SITE 516 516 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000551-50}. FT BINDING 421 421 ATP. {ECO:0000256|PIRSR:PIRSR000551-51}. SQ SEQUENCE 719 AA; 82355 MW; 0694F4F9D0F24DC3 CRC64; MSPFLRIAFS SFEMDPGLAY HEEVLNPYCA VYMKEAVETE KGQVYKQKRP TMYPPWSSTF DAHVHKGRVM HVVVKDKTAE LKTEATVQLD TLASRCKKEN GKLEIWVELK PQGRLLMEAR YFLERSDAAG HGEGDGETER EKEGVFALHH RRGAIKQAKV HVVKCHEFTA TFFPQPTFCS VCKEFVWGLN KQGYQCRQCN AAIHKKCIDK VIAKCTGSAV NSKETMIHKE RFKIDMPHRF KVYNYMSPTF CEHCGTLLWG LARQGLKCEE CGMNVHHKCQ KKVANLCGVN QKLMAEALAM IESTQQQARS SRDTETVGRE GPVSADQPGV IREPSGRLAI SPLTPAPPLP RKEHQGISWD SPADGRRPSL EEPEPLYATP RKEHHKFTID SFILHKMLGK GSFGKVFLAE LKGSGQFFAV KALKKDVVLM DDDVECTMVE RRVLSLAWDH PFLTHLYCTF QTKENLFFVM EYLNGGDLMF HIQTCHRFDL PRSTFYAAEI ICGLQFLHSK GIVYRDLKLD NILLDTDGHI KIADFGMCKE NIIGEARTCT FCGTPDYIAP EILLGQKYGT SVDWWSFGVL LYEMLIGQSP FHGHDEEELF QSIRTDDPCY PRWLTRDARD ILVKLFVREP ERRLGVKGNI RQHPFFRETD WSALEERQVE PPFKPTVKSA NDCSNFDKEF INEKPRLSVT DRMMINSMDQ SMFENFSFIN PIMTRLKSP //