ID W5Q018_SHEEP Unreviewed; 981 AA.
AC W5Q018;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 66.
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:ENSOARP00000016054.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000016054.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000016054.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000016054.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000016054.1}
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: 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 EMBL; AMGL01003167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01003168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01003169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01003170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01003171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01003172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012030800.1; XM_012175410.2.
DR AlphaFoldDB; W5Q018; -.
DR SMR; W5Q018; -.
DR STRING; 9940.ENSOARP00000016054; -.
DR PaxDb; 9940-ENSOARP00000016054; -.
DR Ensembl; ENSOART00000016288.1; ENSOARP00000016054.1; ENSOARG00000014959.1.
DR GeneID; 101118744; -.
DR KEGG; oas:101118744; -.
DR CTD; 5586; -.
DR eggNOG; KOG0694; Eukaryota.
DR HOGENOM; CLU_000288_132_1_1; -.
DR OMA; DPEDVTX; -.
DR OrthoDB; 5400441at2759; -.
DR Proteomes; UP000002356; Chromosome 1.
DR Bgee; ENSOARG00000014959; Expressed in embryo and 55 other cell types or tissues.
DR GO; GO:0043296; C:apical junction complex; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
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:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0070063; F:RNA polymerase binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0043297; P:apical junction assembly; IEA:Ensembl.
DR GO; GO:0010631; P:epithelial cell migration; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:2000145; P:regulation of cell motility; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08687; C2_PKN-like; 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; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF322; SERINE_THREONINE-PROTEIN KINASE N2; 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 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:UP000002356};
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 550..603
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 COMPBIAS 565..595
FT /note="Basic and acidic 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; 111646 MW; 16E2D43B5D3F96A2 CRC64;
MASNPEQGEI VLTELQSDSR 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
ATVPVVDVRN PELAPPASDS TVTKLDFDLE PEPPRAPPRD SSLGEIDESA RDLDTPGQDS
ETVFDTENDR NRILPKSQSE YEPDIPQSGL EYSGIHELED RRSQQMFQFN 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
//
