ID H2S713_TAKRU Unreviewed; 932 AA.
AC H2S713;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN Name=PKN1 {ECO:0000313|Ensembl:ENSTRUP00000008185.2};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000008185.2, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000008185.2, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000008185.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
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DR RefSeq; XP_003972148.1; XM_003972099.2.
DR AlphaFoldDB; H2S713; -.
DR Ensembl; ENSTRUT00000008233.3; ENSTRUP00000008185.2; ENSTRUG00000003489.3.
DR GeneID; 101069685; -.
DR KEGG; tru:101069685; -.
DR CTD; 560840; -.
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000154990; -.
DR OrthoDB; 5400441at2759; -.
DR TreeFam; TF102005; -.
DR Proteomes; UP000005226; Chromosome 17.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd11630; HR1_PKN1_2; 1.
DR CDD; cd11622; HR1_PKN_1; 1.
DR CDD; cd05589; STKc_PKN; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR037317; PKN1_HR1_2.
DR InterPro; IPR037313; PKN_HR1_1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF242; PROTEIN KINASE C; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF02185; HR1; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00742; Hr1; 3.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF46585; HR1 repeat; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; PS51860; REM_1; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 24..100
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 111..192
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 193..274
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 605..864
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 865..932
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 569..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..97
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 244..271
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 932 AA; 105479 MW; 2D5A1A096570F65B CRC64;
MANDSIQSDP GGLSVLEQLG LDQNSDFSDS GVQQLLDEQR EKIRREIRKE LKIKEGAENL
RRATTDKRNA QQVDSQLRSS NRRLENLHDQ LQELDAHIVV KGGEENKEEC PLSPGTDRRT
SAHRDRIAAL ERQLNIELKV KQGVENMIPI YSNGSTKDKK MLQTAQQMLQ DSKTKIDIIR
MQIRKAMQAN EQSDDTQGNQ DVCGVELRIE ELRHHYRVEH AVAEGAKNVL RLLSASKVQD
KKALSEAQSR LSEASQRLDL LRDSLEQRLA ELPEDHPKAS VIKEELVLAS SPAFSSRHGA
PYLHNQYSTL NKPSPLTGTL QVQLVGCVGL LEVVPGRSKG ITVMLPCYCP GDTRSFMRGS
KGLYGRTGSV SGKTASKTDE LSFEVSAVLK LDNTVVGQTV WKTVGEQAWD QTFTVELERS
RELEIAVYWK DYRSLCALKY VKLEDFLDNQ KHRVQLELEP QGLLLAEVTF FNPVIERVPR
LQRQKKVFSK QQGKAFLRAR QMNVDIGTWV RLLRNAIPTV NNSGTYSPNA HSLTLHPGEV
SVEKLSLDAD SPIRGDYKRD METHTPERMP VIEPFSPPDL TPECPVRTPS VGSKQKKGPL
SLQDFRMIAV LGRGHFGKVL LSEYKKTGTM YAIKALKKGD IIARDEVESL MCEKRIFEIV
NMSHHPFLVN LLACFQTPEH VCFVMEYTAG GDLMMHIHTD VFTEPRAVFY SACVVLGLQF
LHDHKIVYRD LKLDNLLLDT DGYVKIADFG LCKEGMGFGD RTSTFCGTPE FLAPEVLTDT
SYTRAVDWWG LGVLIYEMLV GESPFPGDDE EEVFDSIVND EVRYPRFLSN EAIGIIRRLL
RRNPERRLGS GEKDAEEVKK QPFFRTMDWE ALLQRKVPPP FLPSITGKED VSNFDEEFTA
EAPTLTPPRE PRTLSRKDQE SFRDFDYVSD LC
//
