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Database: UniProt
Entry: A0A2K6NZ12_RHIRO
LinkDB: A0A2K6NZ12_RHIRO
Original site: A0A2K6NZ12_RHIRO 
ID   A0A2K6NZ12_RHIRO        Unreviewed;       737 AA.
AC   A0A2K6NZ12;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Protein kinase C epsilon type {ECO:0000256|PIRNR:PIRNR000551};
DE            EC=2.7.11.13 {ECO:0000256|PIRNR:PIRNR000551};
DE   AltName: Full=nPKC-epsilon {ECO:0000256|PIRNR:PIRNR000551};
GN   Name=PRKCE {ECO:0000313|Ensembl:ENSRROP00000009524.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000009524.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000009524.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-
CC       dependent serine/threonine-protein kinase that plays essential roles in
CC       the regulation of multiple cellular processes linked to cytoskeletal
CC       proteins, such as cell adhesion, motility, migration and cell cycle,
CC       functions in neuron growth and ion channel regulation, and is involved
CC       in immune response, cancer cell invasion and regulation of apoptosis.
CC       Mediates cell adhesion to the extracellular matrix via integrin-
CC       dependent signaling, by mediating angiotensin-2-induced activation of
CC       integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS,
CC       which phosphorylates and activates PTK2/FAK, leading to the spread of
CC       cardiomyocytes. Involved in the control of the directional transport of
CC       ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an
CC       intermediate filament (IF) protein. In epithelial cells, associates
CC       with and phosphorylates keratin-8 (KRT8), which induces targeting of
CC       desmoplakin at desmosomes and regulates cell-cell contact.
CC       Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-
CC       cell detachment prior to migration. {ECO:0000256|PIRNR:PIRNR000551}.
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   -!- ACTIVITY REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are
CC       calcium-insensitive, but activated by diacylglycerol (DAG) and
CC       phosphatidylserine. {ECO:0000256|PIRNR:PIRNR000551}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000551}.
CC       Cytoplasm, cytoskeleton {ECO:0000256|PIRNR:PIRNR000551}. Cell membrane
CC       {ECO:0000256|PIRNR:PIRNR000551}. Cytoplasm, perinuclear region
CC       {ECO:0000256|PIRNR:PIRNR000551}. Nucleus
CC       {ECO:0000256|PIRNR:PIRNR000551}. Note=Translocated to plasma membrane
CC       in epithelial cells stimulated by HGF. Associated with the Golgi at the
CC       perinuclear site in pre-passage fibroblasts. In passaging cells,
CC       translocated to the cell periphery. Translocated to the nucleus in PMA-
CC       treated cells. {ECO:0000256|PIRNR:PIRNR000551}.
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   RefSeq; XP_010362610.1; XM_010364308.1.
DR   AlphaFoldDB; A0A2K6NZ12; -.
DR   STRING; 61622.ENSRROP00000009524; -.
DR   Ensembl; ENSRROT00000033614.1; ENSRROP00000009524.1; ENSRROG00000029195.1.
DR   GeneID; 104663184; -.
DR   KEGG; rro:104663184; -.
DR   CTD; 5581; -.
DR   GeneTree; ENSGT00940000154711; -.
DR   OMA; VARICTC; -.
DR   OrthoDB; 841660at2759; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0071889; F:14-3-3 protein binding; IEA:Ensembl.
DR   GO; GO:0003785; F:actin monomer binding; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004699; F:diacylglycerol-dependent, calcium-independent serine/threonine kinase activity; IEA:Ensembl.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0035276; F:ethanol binding; IEA:Ensembl.
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:0030546; F:signaling receptor activator activity; IEA:Ensembl.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR   GO; GO:0002281; P:macrophage activation involved in immune response; IEA:Ensembl.
DR   GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR   GO; GO:0070254; P:mucus secretion; IEA:Ensembl.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:2001031; P:positive regulation of cellular glucuronidation; IEA:Ensembl.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; IEA:Ensembl.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR   GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR   GO; GO:0050996; P:positive regulation of lipid catabolic process; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0070257; P:positive regulation of mucus secretion; IEA:Ensembl.
DR   GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR   GO; GO:0090303; P:positive regulation of wound healing; IEA:Ensembl.
DR   GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR   GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; IEA:Ensembl.
DR   GO; GO:0035669; P:TRAM-dependent toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR   CDD; cd20835; C1_nPKC_epsilon-like_rpt1; 1.
DR   CDD; cd20838; C1_nPKC_epsilon-like_rpt2; 1.
DR   CDD; cd04014; C2_PKC_epsilon; 1.
DR   CDD; cd05591; STKc_nPKC_epsilon; 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; IPR034669; nPKC_epsilon.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR027274; PKC_epsilon.
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; PTHR24351:SF182; PROTEIN KINASE C EPSILON TYPE; 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; PIRSF000551; PKC_delta; 1.
DR   PIRSF; PIRSF501106; Protein_kin_C_epsilon; 1.
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; 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   Cell adhesion {ECO:0000256|PIRNR:PIRNR000551};
KW   Cell cycle {ECO:0000256|PIRNR:PIRNR000551};
KW   Cell division {ECO:0000256|PIRNR:PIRNR000551};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR000551};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000551};
KW   Cytoskeleton {ECO:0000256|PIRNR:PIRNR000551};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000551};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000551};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000551}; Nucleus {ECO:0000256|PIRNR:PIRNR000551};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200};
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          1..117
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          169..220
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          408..668
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          669..737
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          325..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        532
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000551-50"
FT   BINDING         414..422
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000551-51"
FT   BINDING         437
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000551-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   737 AA;  83650 MW;  EFC3294E0D5A5B7B CRC64;
     MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR IGQTATKQKT
     NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI QFEELLQNGS RHFEDWIDLE
     PEGRVYVIID LSGSSGEAPK DNEERVFRER MRPRKRQGAV RRRVHQVNGH KFMATYLRQP
     TYCSHCRDFI WGVIGKQGYQ CQVCTCVVHK RCHELIITKC AGLKKQETPD QVGSQRFSVN
     MPHKFGIHNY KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA
     KVLADLGVTP DKITNSGQRR KKLIAGAESP QPASGSSPSE EDRSKSAPTS PCDQEIKELE
     NNIRKALSFD NRGEEHRAAS SPDGQLMSPG ENGEVRQGQA KRLGLDEFNF IKVLGKGSFG
     KVMLAELKGK DEVYAVKVLK KDVILQDDDV DCTMTEKRIL ALARKHPYLT QLYCCFQTKD
     RLFFVMEYVN GGDLMFQIQR SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL
     DAEGHCKLAD FGMCKEGILN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM
     MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPLKRL GCVASQNGED
     AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ DFTREEPVLT LVDEAIVKQI
     NQEEFKGFSY FGEDLMP
//
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