ID A0A2K5KM23_CERAT Unreviewed; 884 AA.
AC A0A2K5KM23;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:ENSCATP00000001737.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000001737.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000001737.1}
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 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 AlphaFoldDB; A0A2K5KM23; -.
DR Ensembl; ENSCATT00000008809.1; ENSCATP00000001737.1; ENSCATG00000007883.1.
DR GeneTree; ENSGT00950000183024; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000007883; Expressed in bone marrow and 12 other cell types or tissues.
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 GO; GO:0036211; P:protein modification process; IEA:UniProt.
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:UP000233060};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000552};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000552};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..884
FT /note="Serine/threonine-protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014431936"
FT DOMAIN 118..168
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 242..292
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 394..513
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 555..811
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 304..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 678
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-1"
FT BINDING 561..569
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-2"
FT BINDING 584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 884 AA; 100163 MW; 42B3265ECDB89740 CRC64;
MLLLTYRICL DLLSHLLFLN MPKQTDPVFC KQIAIIMCNR IGMKRLPFFM LLDCSKSHEG
FPECGFYGMY DKILLFRHDP TSENILQLVR TASDIQEGDL IEVVLSASAT FEDFQIRPHA
LFVHSYRAPA FCDHCGEMLW GLVRQGLKCE GCGLNYHKRC AFKIPNNCSG VRRRRLSNVS
LTGLSTIRTS SAELSTSAPD EPLLQKSPSE SFIGREKRSN SQSYIGRPIQ LDKILMSKVK
VPHTFVIHSY TRPTVCQYCK KLLKGLFRQG LQCKDCRFNC HKRCAPKVPN NCLGEVTING
DLLSPGTESD VVMEEGSDDN DSERNSRLMD DMEEAMVQDA EMAMAECQND SGEMQDPDPD
HEDANRTISP STSNNIPLMR VVQSVKHTKR KSSTVMKEGW MVHYTSKDTL RKRHYWRLDS
KCITLFQNDT GSRYYKEIPL SEILSLEPAK TSALIPNGAN PHCFEITTAN VVYYVGENVL
NPSSPPPNNS VLTSGVGADV ARMWEIAIQH ALMPVIPKGS SVGTGTNLHR DISVSISVSN
CQIQENVDIS TVYQIFPDEV LGSGQFGIVY GGKHRKTGRD VAIKIIDKLR FPTKQESQLR
NEVAILQNLH HPGVVNLECM FETPERVFVV MEKLHGDMLE MILSSEKGRL PEHITKFLIT
QILVALRHLH FKNIVHCDLK PENVLLASAD PFPQVKLCDF GFARIIGEKS FRRSVVGTPA
YLAPEVLRNK GYNRSLDMWS VGVIIYVSLS GTFPFNEDED IHDQIQNAAF MYPPNPWKEI
SHEAIDLINN LLQVKMRKRY SVDKTLSHPW LQDYQTWLDL RELECKIGER YITHESDDLR
WEQYAGEQGL QYPTHLINPS ASHSDSPETE ETEMKALGER VSIL
//
