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O19111

- KPCZ_RABIT

UniProt

O19111 - KPCZ_RABIT

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Protein

Protein kinase C zeta type

Gene

PRKCZ

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. Necessary and sufficient for LTP maintenance in hippocampal CA1 pyramidal cells. In vein endothelial cells treated with the oxidant peroxynitrite, phosphorylates STK11 leading to nuclear export of STK11, subsequent inhibition of PI3K/Akt signaling, and increased apoptosis (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Atypical PKCs (PRKCI and PRKCZ) exhibit an elevated basal enzymatic activity (that may be due to the interaction with SMG1 or SQSTM1) and are not regulated by diacylglycerol, phosphatidylserine, phorbol esters or calcium ions. Two specific sites, Thr-409 (activation loop of the kinase domain) and Thr-559 (turn motif), need to be phosphorylated for its full activation. Phosphatidylinositol 3,4,5-trisphosphate might be a physiological activator (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei280 – 2801ATPPROSITE-ProRule annotation
Active sitei375 – 3751Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri130 – 18051Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST
Nucleotide bindingi257 – 2659ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein kinase C activity Source: UniProtKB-EC
  3. protein serine/threonine kinase activity Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. establishment of cell polarity Source: UniProtKB
  2. inflammatory response Source: UniProtKB-KW
  3. intracellular signal transduction Source: InterPro
  4. long-term synaptic potentiation Source: UniProtKB
  5. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  6. positive regulation of excitatory postsynaptic membrane potential Source: UniProtKB
  7. positive regulation of insulin receptor signaling pathway Source: UniProtKB
  8. positive regulation of interleukin-10 secretion Source: UniProtKB
  9. positive regulation of interleukin-13 secretion Source: UniProtKB
  10. positive regulation of interleukin-4 production Source: UniProtKB
  11. positive regulation of interleukin-5 secretion Source: UniProtKB
  12. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  13. positive regulation of T-helper 2 cell cytokine production Source: UniProtKB
  14. positive regulation of T-helper 2 cell differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Inflammatory response

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.11.13. 1749.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein kinase C zeta type (EC:2.7.11.13)
Alternative name(s):
nPKC-zeta
Gene namesi
Name:PRKCZ
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

Cytoplasm By similarity. Endosome By similarity. Cell junction By similarity
Note: In the retina, localizes in the terminals of the rod bipolar cells. Associated with endosomes. Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction (By similarity).By similarity

GO - Cellular componenti

  1. cell-cell junction Source: UniProtKB
  2. endosome Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Endosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591Protein kinase C zeta typePRO_0000055703Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei409 – 4091Phosphothreonine; by PDPK1 and PI3KBy similarity
Modified residuei559 – 5591PhosphothreonineBy similarity

Post-translational modificationi

CDH5 is required for its phosphorylation at Thr-409. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2. Phosphorylation at Thr-409 by PI3K activates the kinase (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Interacts with PARD6A, PARD6B and PARD6G. Part of a complex with PARD3, PARD6A or PARD6B or PARD6G and CDC42 or RAC1. Interacts with ADAP1/CENTA1. Interacts directly with SQSTM1. Forms a ternary complex with SQSTM1 and KCNAB2. Forms another ternary complex with SQSTM1 and GABRR3. Forms a complex with SQSTM1 and MAP2K5. Interacts (via the protein kinase domain) with WWC1. Forms a tripartite complex with WWC1 and DDR1, but predominantly in the absence of collagen. Component of the Par polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1. Interacts with PDPK1 (via N-terminal region) (By similarity).By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000006125.

Structurei

3D structure databases

ProteinModelPortaliO19111.
SMRiO19111. Positions 12-98, 246-583.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 9884OPRAdd
BLAST
Domaini251 – 517267Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini518 – 58972AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 14567Interaction with SQSTM1By similarityAdd
BLAST

Domaini

The OPR domain mediates mutually exclusive interactions with SQSTM1 and PARD6B.By similarity
The C1 domain does not bind the diacylglycerol (DAG).

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 OPR domain.Curated
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri130 – 18051Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG108317.
InParanoidiO19111.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR002219. PE/DAG-bd.
IPR012233. PKC_zeta.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24357:SF60. PTHR24357:SF60. 1 hit.
PfamiPF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000554. PKC_zeta. 1 hit.
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O19111-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MPSRAGPKMD GSGGRVRLKA HYSGDIFITS VDAATTFEEL CEEVRDMCGL
60 70 80 90 100
HQHHPLTLKW VDSEGDPRTV SSQMELGEAF RLAGQHRDDG LILHVFPSTP
110 120 130 140 150
EQPGMPCPGE DKSIYRRGAR RWRKLYRANG HLFQAKRFNR RAYCGQCSER
160 170 180 190 200
IWGLARQGYR CINCKLLVHK RCHGLVPLTC RRHMDSVMPS QEPPVADKSD
210 220 230 240 250
DADLPSQETD GIAFISTRKQ DSGQEDAEDL KPVIDGVDGI KISQGLGLQD
260 270 280 290 300
FDLIRVIGRG SYAKVLLVRL KKNGQVYAMK VVKKELVHDD EDIDWVQTEK
310 320 330 340 350
HVFEQASGNP FLVGLHSCFQ TTSRLFLVIE YVNGGDLMFH MQRQRKLPEE
360 370 380 390 400
HARFYAAEIC IALNFLHERG IIYRDLKLDN VLLDADGHIK LTDYGMCKEG
410 420 430 440 450
LGPGDTTSTF CGTPNYIAPE ILRGEEYGFS VDWWALGVLM FEMMAGRSPF
460 470 480 490 500
DIITDNPDMN TEDYLFQVIL EKPIRIPRFL SVKASHVLKG FLNKDPKERL
510 520 530 540 550
GCRPQTGFSD IKSHAFFRSI DWDLLEKKQA LPPFQPQITD DYGLDNSDTQ
560 570 580 590
FTSEPVQLTP DDEDVIKRID QSEFEGFEYI NPLLLSTEES V
Length:591
Mass (Da):67,095
Last modified:January 1, 1998 - v1
Checksum:i83D32A8744CADDB6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78768 mRNA. Translation: AAB67317.1.
RefSeqiNP_001076227.1. NM_001082758.1.
UniGeneiOcu.2166.

Genome annotation databases

GeneIDi100009538.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78768 mRNA. Translation: AAB67317.1 .
RefSeqi NP_001076227.1. NM_001082758.1.
UniGenei Ocu.2166.

3D structure databases

ProteinModelPortali O19111.
SMRi O19111. Positions 12-98, 246-583.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000006125.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009538.

Organism-specific databases

CTDi 5590.

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG108317.
InParanoidi O19111.

Enzyme and pathway databases

BRENDAi 2.7.11.13. 1749.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR000270. OPR_PB1.
IPR002219. PE/DAG-bd.
IPR012233. PKC_zeta.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
PANTHERi PTHR24357:SF60. PTHR24357:SF60. 1 hit.
Pfami PF00130. C1_1. 1 hit.
PF00564. PB1. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000554. PKC_zeta. 1 hit.
PRINTSi PR00008. DAGPEDOMAIN.
SMARTi SM00109. C1. 1 hit.
SM00666. PB1. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: New Zealand white.
    Tissue: Kidney.

Entry informationi

Entry nameiKPCZ_RABIT
AccessioniPrimary (citable) accession number: O19111
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3