ID F1R506_DANRE Unreviewed; 713 AA. AC F1R506; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 3. DT 16-OCT-2019, entry version 73. DE RecName: Full=Protein kinase C {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS01199224}; DE EC=2.7.11.13 {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS01199224}; 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). 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, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC EC=2.7.11.13; Evidence={ECO:0000256|SAAS:SAAS01199216}; 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|PIRNR:PIRNR000551, CC ECO:0000256|SAAS:SAAS01199205}; 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:SAAS01199204}. 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 STRING; 7955.ENSDARP00000046252; -. DR Ensembl; ENSDART00000046253; ENSDARP00000046252; ENSDARG00000034173. DR GeneID; 555521; -. DR KEGG; dre:555521; -. DR CTD; 5588; -. DR ZFIN; ZDB-GENE-041210-195; prkcq. DR eggNOG; KOG0694; Eukaryota. DR eggNOG; ENOG410XNPH; LUCA. DR GeneTree; ENSGT00940000157638; -. DR InParanoid; F1R506; -. DR KO; K18052; -. 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 Proteomes; UP000000437; Chromosome 4. DR Bgee; ENSDARG00000034173; Expressed in 15 organ(s), highest expression level in muscle tissue. DR ExpressionAtlas; F1R506; baseline. 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; 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:SAAS00253054}; 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 Repeat {ECO:0000256|SAAS:SAAS01019132}; 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:SAAS00253075}; KW Zinc-finger {ECO:0000256|SAAS:SAAS00732991}. FT DOMAIN 159 209 Phorbol-ester/DAG-type. FT {ECO:0000259|PROSITE:PS50081}. FT DOMAIN 231 281 Phorbol-ester/DAG-type. FT {ECO:0000259|PROSITE:PS50081}. FT DOMAIN 386 640 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT DOMAIN 641 712 AGC-kinase C-terminal. FT {ECO:0000259|PROSITE:PS51285}. FT NP_BIND 392 400 ATP. {ECO:0000256|PIRSR:PIRSR000551-51}. FT REGION 298 372 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 351 372 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT ACT_SITE 510 510 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000551-50}. FT BINDING 415 415 ATP. {ECO:0000256|PIRSR:PIRSR000551-51}. 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 //