ID A0A3P8Y9T4_ESOLU Unreviewed; 957 AA.
AC A0A3P8Y9T4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN Name=PRKD2 {ECO:0000313|Ensembl:ENSELUP00000013354.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000013354.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000013354.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000013354.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PKD subfamily. {ECO:0000256|ARBA:ARBA00008582}.
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DR RefSeq; XP_010871255.1; XM_010872953.3.
DR AlphaFoldDB; A0A3P8Y9T4; -.
DR Ensembl; ENSELUT00000021868.2; ENSELUP00000013354.2; ENSELUG00000013565.2.
DR GeneTree; ENSGT00950000183024; -.
DR InParanoid; A0A3P8Y9T4; -.
DR Proteomes; UP000265140; LG01.
DR Bgee; ENSELUG00000013565; Expressed in head kidney and 15 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd01239; PH_PKD; 1.
DR CDD; cd14082; STKc_PKD; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015727; Protein_Kinase_C_mu-related.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR PANTHER; PTHR22968:SF12; SERINE_THREONINE-PROTEIN KINASE D2; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000552; PKC_mu_nu_D2; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000552-
KW 2}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000552-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 167..217
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 317..367
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 627..883
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 272..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 750
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-1"
FT BINDING 633..641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-2"
FT BINDING 656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 957 AA; 105893 MW; 1E044E886ECD9909 CRC64;
MANASPCLPA GPMSQVFFPP GGPSPPSSVV IQPGPPMAVP ATPVYGGFPP VDLGVGPGPV
GAAMSPVPPT PAGVSFIIQI GLSRESVLLP QNYDLAYVKQ MACSIVDTKF PECGFYGIYD
KILLFKHDTG THNILQLVKS AQDIQEGDLV EVVLSAAATF EDFQIRPHAL NVHSYRAPAF
CDHCGEMLFG LVRQGLKCDG CGLNYHKRCA FSIPNNCSGA RKRRLSSSQS LRLSTTDSLS
SVGTVSVSTC NEEASLVRSH TTQMVPNSTC TASTSLGLSS SSSITRPMPR TPSEARRFYT
GRPVHLDKIL MSKVKVPHTF AVHSYTRPTV CQYCKRLLRG LFRQGLQCKD CKFNCHKRCA
YKVPNDCLGE TLGDSRSDML SPSVDTEVPM DYSSEYADSD KSSVMDDSDE SCSIPGSFSP
ESSQDGTSGD QSALFIPLMR VVQSMRQTTR RSSTSIKEGW MVHYSNKDTL RKRHYWRLDC
KCIILFQNNT TNKYYKEIPL SEVLEVRPAG DFSLVPPGTS PHCFEIITGT MCYFVGEDPN
IPILPHTTPQ SFPPTPPLPN NVAPNSGVGR EVAKAWESAI RQALMPVIFQ DAPPAEGHTP
HRQASVSISV SNSVIQENVD IGMVYQIFAD EVLGSGQFGV VYGGKHRKTG RDVAVKVIDK
LRFPTKQESQ LRNEVAILQS LRHLGIVNLE CMFETPEKVF VVMEKLHGDM LEMILSSEKG
RLPERLTKFL ITQILAALRH LHFKNIVHCD LKPENVLLAS AEPFPQVKLC DFGFARIIGE
KSFRRSVVGT PAYLAPEVLL NQGYNRSLDM WSVGVIMYVS LSGTFPFNED EDINDQIHNA
AFMYPPNPWK QISPDAIDLI NNLLQVKMRK RYSVDKSLSH SYLQDYHTWL DLRELETKLG
ERYITHESDD GRWQMFAHDH TLPYPAHLVA PSPATGSDDE AGEDTDMQGL TERVSIL
//
