ID H2R0T5_PANTR Unreviewed; 581 AA.
AC H2R0T5; A0A2J8KTN1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Protein kinase C {ECO:0000256|ARBA:ARBA00012429, ECO:0000256|PIRNR:PIRNR000551};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429, ECO:0000256|PIRNR:PIRNR000551};
GN Name=PRKCQ {ECO:0000313|Ensembl:ENSPTRP00000041216.5,
GN ECO:0000313|VGNC:VGNC:7859};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000041216.5, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000041216.5, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000041216.5}
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 ECO:0000256|PIRNR:PIRNR000551};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}.
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:PIRNR000551}.
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DR EMBL; AACZ04030381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04030382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04030383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009456183.1; XM_009457908.2.
DR AlphaFoldDB; H2R0T5; -.
DR Ensembl; ENSPTRT00000045745.5; ENSPTRP00000041216.5; ENSPTRG00000002270.6.
DR VGNC; VGNC:7859; PRKCQ.
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000157638; -.
DR HOGENOM; CLU_000288_54_4_1; -.
DR OMA; GRVMHII; -.
DR OrthoDB; 841660at2759; -.
DR TreeFam; TF102004; -.
DR Proteomes; UP000002277; Chromosome 10.
DR Bgee; ENSPTRG00000002270; Expressed in skeletal muscle tissue and 17 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd20834; C1_nPKC_theta-like_rpt1; 1.
DR CDD; cd20837; C1_nPKC_theta-like_rpt2; 1.
DR CDD; cd05619; STKc_nPKC_theta; 1.
DR Gene3D; 3.30.60.20; -; 2.
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; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR034668; nPKC_theta.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR014376; Prot_kin_PKC_delta.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF181; PROTEIN KINASE C THETA TYPE; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000551; PKC_delta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 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; 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; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000551};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000551};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000551};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR000551};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000551};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 34..84
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 106..156
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 255..509
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 510..581
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-50"
FT BINDING 261..269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51"
FT BINDING 284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 581 AA; 67561 MW; 09C4C59810BF6F58 CRC64;
MDTKDMNEFE TEGFFALHQR RGAIKQAKVH HVKCHEFTAT FFPQPTFCSV CHEFVWGLNK
QGYQCRQCNA AIHKKCIDKV IAKCTGSAIN SRETMFHKER FKIDMPHRFK VYNYKSPTFC
EHCGTLLWGL ARQGLKCDAC GMNVHHRCQT KVANLCGINQ KLMAEALAMI ESTQQARCLR
DTEQIFREGP VEIGLPCSIK NEARPPCLPT LGKREPQGIS WESPLDEVDK MCHLPEPELN
IERPSLQIKL KIEDFILHKM LGKGSFGKVF LAEFKKTNQF FAIKALKKDV VLMDDDVECT
MVEKRVLSLA WEHPFLTHMF CTFQTKENLF FVMEYLNGGD LMYHIQSCHK FDLSRATFYA
AEIILGLQFL HSKGIVYRDL KLDNILLDKD GHIKIADFGM CKENMLGDAK TNTFCGTPDY
IAPEILLGQK YNHSVDWWSF GVLLYEMLIG QSPFHGQDEE ELFHSIRMDN PFYPRWLEKE
AKDLLVKLFV REPEKRLGVR GDIRQHPLFR EINWEELERK EIDPPFRPKV KSPFDCSNFD
KEFLNEKPRL SFADRALINS MDQNMFRNFS FMNPGMERLI S
//
