ID W5P4Q9_SHEEP Unreviewed; 833 AA.
AC W5P4Q9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000552};
DE EC=2.7.11.13 {ECO:0000256|PIRNR:PIRNR000552};
GN Name=PRKD1 {ECO:0000313|Ensembl:ENSOARP00000005412.1};
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:ENSOARP00000005412.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000005412.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000005412.1,
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:ENSOARP00000005412.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 ECO:0000256|PIRNR:PIRNR000552};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000552};
CC -!- ACTIVITY REGULATION: Activated by DAG and phorbol esters.
CC {ECO:0000256|PIRNR:PIRNR000552}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000552}.
CC 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 EMBL; AMGL01042243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01042244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01042245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01042246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01042247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01042248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01042249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01042250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5P4Q9; -.
DR SMR; W5P4Q9; -.
DR STRING; 9940.ENSOARP00000005412; -.
DR PaxDb; 9940-ENSOARP00000005412; -.
DR Ensembl; ENSOART00000005499.1; ENSOARP00000005412.1; ENSOARG00000005042.1.
DR eggNOG; KOG4236; Eukaryota.
DR HOGENOM; CLU_009772_1_0_1; -.
DR OMA; CHNSHRS; -.
DR Proteomes; UP000002356; Chromosome 18.
DR Bgee; ENSOARG00000005042; Expressed in aortic valve and 50 other cell types or tissues.
DR ExpressionAtlas; W5P4Q9; baseline.
DR GO; GO:0005737; C:cytoplasm; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20839; C1_PKD1_rpt1; 1.
DR CDD; cd20842; C1_PKD1_rpt2; 1.
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:SF9; SERINE_THREONINE-PROTEIN KINASE D1; 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; PS50003; PH_DOMAIN; 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|PIRNR:PIRNR000552};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR000552};
KW Kinase {ECO:0000256|PIRNR:PIRNR000552};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000552};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000552};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000552};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000552};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000552};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 67..117
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 191..241
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 343..462
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 504..760
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 141..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 627
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-1"
FT BINDING 510..518
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-2"
FT BINDING 533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 833 AA; 93858 MW; 401FB2798ADD3FEC CRC64;
MACSIVDQKF PECGFYGMYD KILLFRHDPT SENILQLVKT ASDIQEGDLI EVVLSASATF
EDFQIRPHTL FVHSYRAPAF CDHCGEMLWG LVRQGLKCEG CGLNYHKRCA FKIPNNCSGV
RRRRLSNVSL TGLSTVRTAS AELSTSAPDE PLLQKSPSES FIGREKRSNS QSYIGRPIQL
DKILLSKVKV PHTFVIHSYT RPTVCQYCKK LLKGLFRQGL QCKDCRFNCH KRCAPKVPNN
CLGEVTINGD LLSPGAESDI VMEEGSDDND SERNSGLMDE LEEAMVQDAE MVMAECQNDS
GEMQDPDPDH EDSNRTISPS TSNNIPLMRV VQSVKHTKRK SSTVMKEGWM VHYTSKDPLR
KRHYWRLDSK CITLFQNDTG SRYYKEIPLS EILSLEPAKP SALIPSGANP HCFEITTANI
VYYVGENVVN PSSPPPNSSV LTSGVGADVA RMWEVAIQHA LMPVIPKGSS VGSGTNVHRD
ISVSISVSNC QIQENVDIST VYQIFPDEVL GSGQFGIVYG GKHRKTGRDV AIKIIDKLRF
PTKQESQLRN EVAILQNLHH PGVVNLECMF ETPERVFVVM EKLHGDMLEM ILSSEKGRLP
EHVTKFLITQ ILVALRHLHF KNIVHCDLKP ENVLLASADP FPQVKLCDFG FARIIGEKSF
RRSVVGTPAY LAPEVLRNKG YNRSLDMWSV GVIIYVSLSG TFPFNEDEDI HDQIQNAAFM
YPPNPWKEIS HEAIDLINNL LQVKMRKRYS VDKTLSHPWL QDYQTWLDLR ELECKIGERY
ITHESDDSRW EQFAGEQGLQ YPTHLIDPNA GHSDSPEAEE TEMKALSERV SIL
//
