ID F1MFK1_BOVIN Unreviewed; 981 AA.
AC F1MFK1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 2.
DT 24-JAN-2024, entry version 92.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN Name=PKN2 {ECO:0000313|Ensembl:ENSBTAP00000029201.5,
GN ECO:0000313|VGNC:VGNC:32946};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000029201.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000029201.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000029201.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000029201.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000029201.5};
RG Ensembl;
RL Submitted (JUL-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: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Midbody
CC {ECO:0000256|ARBA:ARBA00004214}. Nucleus
CC {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; NP_001180171.1; NM_001193242.1.
DR AlphaFoldDB; F1MFK1; -.
DR SMR; F1MFK1; -.
DR STRING; 9913.ENSBTAP00000029201; -.
DR PaxDb; 9913-ENSBTAP00000029201; -.
DR Ensembl; ENSBTAT00000029201.6; ENSBTAP00000029201.5; ENSBTAG00000021900.6.
DR GeneID; 519754; -.
DR KEGG; bta:519754; -.
DR CTD; 5586; -.
DR VEuPathDB; HostDB:ENSBTAG00000021900; -.
DR VGNC; VGNC:32946; PKN2.
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000154339; -.
DR HOGENOM; CLU_000288_132_1_1; -.
DR InParanoid; F1MFK1; -.
DR OMA; EVTINGC; -.
DR OrthoDB; 5400441at2759; -.
DR TreeFam; TF102005; -.
DR Reactome; R-BTA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-BTA-8980692; RHOA GTPase cycle.
DR Reactome; R-BTA-9013106; RHOC GTPase cycle.
DR Reactome; R-BTA-9013149; RAC1 GTPase cycle.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000021900; Expressed in spiral colon and 111 other cell types or tissues.
DR ExpressionAtlas; F1MFK1; baseline.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08687; C2_PKN-like; 1.
DR CDD; cd11631; HR1_PKN2_2; 1.
DR CDD; cd11635; HR1_PKN2_3; 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; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037784; C2_PKN.
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; 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:SF229; 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; SM00239; C2; 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; PS50004; C2; 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}; Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..109
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 121..203
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 204..284
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 352..472
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 654..913
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 914..981
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 113..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 981 AA; 111552 MW; 4AA044789244422A CRC64;
MASNPERGEI LLTELQGDSR SLPFSENVSA VQKLDFSDTM VQQKLDDIKD RIKREIRKEL
KIKEGAENLR KVTTDKKSLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDVTDCPR
TPDTPSSDSR CSTSNNRLMA LQKQLDIELK VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL
QDSKTKIEVI RMQILQAVQT NELAFDNAKP VISPLELRME ELRHHFRIEF AVAEGAKNVM
KLLGSGKVTD RKALSEAQAR FNESSQKLDL LKYSLEQRLN ELPKNHPKSS IIIEELSLVA
SPTLSPRQSM ISTQNQYSTL SKPAALTGTL EVRLMGCQDI LENVPGRSKA ASVALPGWSP
SETRSSFMSR TSKSKSGSSR NLLKTDDLSN DVCAVLKLDN TVVGQTSWKP ISNQSWDQKF
TLELDRSREL EISVYWRDWR SLCAVKFLRL EDFLDNQRHG MCLYLEPQGT LFAEVTFFNP
VIERRPKLQR QKKIFSKQQG KTFLRAPQMN INIATWGRLV RRAIPTVNHS GTFSPQAPVP
ATVPVVDVHI PELAPPASDS TVTKLDFDLE PEPPPAPPRD SSLGEIDESA RDLDTPGQDS
ETVFDTENDR NRILPKSQSE YEPDIPQSGL EYSGIHELED RRSQQMFQFS LQDFRCCAVL
GRGHFGKVLL AEYKHTNEMF AIKALKKGDI VARDEVDSLM CEKRIFETVN SVRHPFLVNL
FACFQTKEHV CFVMEYAAGG DLMMHIHTDV FSEPRAVFYA ACVVLGLQYL HEHKIVYRDL
KLDNLLLDTE GFVKIADFGL CKEGMGYGDR TSTFCGTPEF LAPEVLTETS YTRAVDWWGL
GVLIYEMLVG ESPFPGDDEE EVFDSIVNDE VRYPRFLSTE AISIMRRLLR RNPERRLGAG
EKDAEDVKKH PFFRLIDWSA LMDKKVKPPF VPTIRGREDV SNFDDEFTSE APILTPPREP
RILSEEEQEM FRDFDYIADW C
//