ID T1PFJ3_MUSDO Unreviewed; 677 AA.
AC T1PFJ3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Protein kinase C {ECO:0000256|ARBA:ARBA00012429, ECO:0000256|PIRNR:PIRNR000550};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429, ECO:0000256|PIRNR:PIRNR000550};
GN Name=101894312 {ECO:0000313|EnsemblMetazoa:MDOA008448-PB};
GN Synonyms=LOC101894312 {ECO:0000313|RefSeq:XP_011290238.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EMBL:AFP62196.1};
RN [1] {ECO:0000313|EMBL:AFP62196.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ALHF {ECO:0000313|EMBL:AFP62196.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:AFP62196.1};
RA Liu N., Zhang L., Li M., Reid W.;
RT "Transcriptome of adult Musca domestica launches a platform for comparative
RT house fly gene expression and characterization of differential gene
RT expression among resistant and susceptible house flies.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:MDOA008448-PB}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA008448-PB};
RG EnsemblMetazoa;
RL Submitted (JAN-2021) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_011290238.1}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|RefSeq:XP_011290238.1};
RG RefSeq;
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|PIRNR:PIRNR000550};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR000550-4};
CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC domain. {ECO:0000256|PIRSR:PIRSR000550-4};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490,
CC ECO:0000256|PIRNR:PIRNR000550}.
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DR EMBL; KA647567; AFP62196.1; -; mRNA.
DR RefSeq; XP_011290238.1; XM_011291936.2.
DR STRING; 7370.T1PFJ3; -.
DR EnsemblMetazoa; MDOA008448-RB; MDOA008448-PB; MDOA008448.
DR GeneID; 101894312; -.
DR KEGG; mde:101894312; -.
DR VEuPathDB; VectorBase:MDOA008448; -.
DR eggNOG; KOG0696; Eukaryota.
DR OrthoDB; 841660at2759; -.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; Unplaced.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20792; C1_cPKC_nPKC_rpt1; 1.
DR CDD; cd04026; C2_PKC_alpha_gamma; 1.
DR CDD; cd05570; STKc_PKC; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014375; Protein_kinase_C_a/b/g.
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; PF00130; C1_1; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000550; PKC_alpha; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00239; C2; 1.
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; SSF57889; Cysteine-rich domain; 2.
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; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000550};
KW Calcium {ECO:0000256|PIRSR:PIRSR000550-4};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000550};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000550-4};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000550};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694905};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000550};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000550};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 49..99
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 114..164
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 167..288
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 348..606
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 607..677
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-1"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-4"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-4"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-4"
FT BINDING 208
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-2"
FT BINDING 258
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-2"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-4"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-4"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-4"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-4"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-4"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-4"
FT BINDING 354..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-3"
FT BINDING 377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000550-3,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 677 AA; 77263 MW; 3CCA2BAD47153B58 CRC64;
MAAAAAAPAA GAAPKDLVQI AGEGAFTNYM KNRLRRGGMK RKGLEIINGH KFAVRFFKQP
TYCGHCKEFI WGFGKQGYQC EDCRFNIHQK CCKFVVFKCP GTETDIDGEC AKVKHAWVST
TYSAPTFCDD CGLLLHGVQH QGVKCDNCNL NVHHNCKDKV PPLCGADITE IRGKLLLYVE
LKGNTLKVDI KEAANLIPMD TNGLSDPYIA IQLHPDRSGK TKKKTKTIQK NLNPVFNESF
TFDLGPQDRE KRLLIEVWDW DRTSRNDFMG SFSFSMEEIQ KEPIDGWYKF LSQVEGEHYN
IPCTDAVNDI ARLRDEVKTE KKTNKRRMDN KDMPHNMNKR DMIRAADFNF IKVLGKGSFG
KVLLAERRGT DELYAVKVLR KDIIIQADDM ELPMTEKFIL ALSGKSPFLV SLHSCFQTMD
RLFFVLEYCK GGDLLYQLQK YGRFKESVAI FYAVEVALAL FFLHERKIIY RDLKLDNILL
DLDGHVKLTD FGLSKDNIGE NDNTRTFCGT SCYLAPEILA YEPYSHTVDW WAYGVLLYEM
MAGQQPFEGE DDAAIYKNIK EKKAVFPKHF SQESMDVITS FLAKKPNNRL GAGKFARNEI
QTHPFYNIID WDSAAEKGME PPIIPKIKHR KDISNFDTTF TAEKTDLTPT DKLFMMNLDQ
GDFLGFSYMN PEFITLV
//
