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Protein

cGMP-dependent protein kinase egl-4

Gene

egl-4

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Promotes chemoreceptor gene expression in response to increased cGMP levels by antagonizing the gene repression functions of the class II HDAC hda-4 and the mef-2 transcription factor (PubMed:18832350). Regulates gene expression via recruitment of a histone deacetylase complex containing hda-2, saeg-1 and saeg-2 (PubMed:21573134). Represses body size and lifespan through the dbl-1 and insulin pathways, respectively (PubMed:12571101, PubMed:15330854). May also signal through daf-3 and/or daf-5. Role in egg-laying, dauer formation and motility (PubMed:12571101, PubMed:11181837, PubMed:21573134). Regulates behavioral responses to various chemosensory stimuli in sensory neurons (PubMed:10978280, PubMed:22319638, PubMed:23874221). Required for the initiation of long term adaptation to prolonged odor exposure which results in a decrease in odor seeking behavior (PubMed:12495623, PubMed:20220099). May regulate this process by phosphorylating tax-2, a subunit of cyclic nucleotide-gated channel tax-2/tax-4 (PubMed:12495623). In ASH sensory neurons, negatively regulates avoidance behavior to some bitter tastants, such as quinine, probably by phosphorylating rgs-2 and rgs-3 which are 2 regulator of G-protein signaling proteins (PubMed:23874221). In AWB sensory neurons, involved in avoidance behavior to some repellent odors (PubMed:23954825). In ASE left (ASEL) sensory neuron, involved in the sensing of environmental alkalinity downstream of receptor-type guanylate cyclase gcy-14 (PubMed:23664973). In sensory neurons, involved in the signaling pathway downstream of insulin, TGF-beta and receptor-type guanylate cyclase responsible for inducing quiescence after food intake (PubMed:18316030).1 Publication12 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Mg2+2 Publications

Enzyme regulationi

Binding of cGMP results in enzyme activation.2 Publications

Kineticsi

    1. Vmax=2.1 µmol/min/mg enzyme towards cGMP (Isoform c at pH 6.8 and 30 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei499 – 4991ATPPROSITE-ProRule annotationBy similarity
    Active sitei593 – 5931Proton acceptorPROSITE-ProRule annotationBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi201 – 316116cNMP 1Sequence analysisAdd
    BLAST
    Nucleotide bindingi319 – 441123cNMP 2Sequence analysisAdd
    BLAST
    Nucleotide bindingi475 – 4839ATPPROSITE-ProRule annotationBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • chemosensory behavior Source: UniProtKB
    • chemotaxis Source: UniProtKB-KW
    • determination of adult lifespan Source: UniProtKB
    • insulin receptor signaling pathway Source: WormBase
    • larval feeding behavior Source: UniProtKB
    • negative regulation of calcium-mediated signaling Source: UniProtKB
    • negative regulation of cell growth Source: WormBase
    • negative regulation of cGMP biosynthetic process Source: UniProtKB
    • negative regulation of cyclic nucleotide-gated ion channel activity Source: WormBase
    • negative regulation of dauer larval development Source: WormBase
    • negative regulation of multicellular organism growth Source: WormBase
    • negative regulation of organ growth Source: WormBase
    • negative regulation of transforming growth factor beta receptor signaling pathway Source: WormBase
    • peptidyl-serine phosphorylation Source: WormBase
    • positive regulation of cGMP-mediated signaling Source: WormBase
    • positive regulation of cyclic-nucleotide phosphodiesterase activity Source: WormBase
    • protein phosphorylation Source: WormBase
    • regulation of eating behavior Source: UniProtKB
    • regulation of gene expression Source: UniProtKB
    • regulation of oviposition Source: WormBase
    • response to hydrogen peroxide Source: UniProtKB
    • response to odorant Source: UniProtKB
    • response to oxygen levels Source: WormBase
    • sensory perception of bitter taste Source: UniProtKB
    • sleep Source: WormBase
    Complete GO annotation...

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Chemotaxis

    Keywords - Ligandi

    ATP-binding, cGMP, cGMP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiR-CEL-392517. Rap1 signalling.
    SABIO-RKO76360.
    SignaLinkiO76360.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cGMP-dependent protein kinase egl-42 Publications (EC:2.7.11.12)
    Alternative name(s):
    Egg-laying defective protein 4
    Gene namesi
    Name:egl-4
    Synonyms:cgr-11 Publication, odr-91 Publication
    ORF Names:F55A8.2
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    Proteomesi
    • UP000001940 Componenti: Chromosome IV

    Organism-specific databases

    WormBaseiF55A8.2a; CE19897; WBGene00001173; egl-4.
    F55A8.2b; CE19898; WBGene00001173; egl-4.
    F55A8.2c; CE31541; WBGene00001173; egl-4.
    F55A8.2d; CE37718; WBGene00001173; egl-4.
    F55A8.2e; CE37241; WBGene00001173; egl-4.
    F55A8.2f; CE37242; WBGene00001173; egl-4.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: WormBase
    • nucleus Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Increased size and extended lifespan. Defects in chemosensory behavior, egg-laying, synaptic transmission, and dauer formation (PubMed:11181837, PubMed:12571101, PubMed:18832350). Impaired movement of adult animals in response to sensory stimuli (PubMed:10978280). Loss of adaptive behavior to long lasting exposure to attractive odorants. Normal initial chemotaxis response during a first and short exposure to attractive odorants (PubMed:20220099). Loss of chemotaxis response to the repellent odor 2-nonanone (PubMed:23954825). Increased basal cGMP levels (PubMed:24015261).7 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi162 – 1621K → N: Constitutively active. Undergoes autophosphorylation in vitro. 1 Publication
    Mutagenesisi276 – 2761T → A: Loss of nuclear translocation mediated by cGMP. Loss of nuclear translocation upon prolonged exposure to attractive odorants. 2 Publications
    Mutagenesisi362 – 3621G → R: Loss of body size, reduced locomotion in the presence of food, a pale intestine, increased intestinal fat storage, and a decreased propensity to form dauer larvae. 1 Publication
    Mutagenesisi497 – 4971A → T: No obvious phenotype. May cause partial loss of kinase activity. 1 Publication
    Mutagenesisi499 – 4991K → A: Loss of kinase activity. 1 Publication
    Mutagenesisi502 – 5021K → E: Loss of adaptive behavior upon prolonged exposure to attractive odorants. 1 Publication
    Mutagenesisi611 – 6111D → N: Loss of nuclear translocation upon prolonged exposure to attractive odorants. 1 Publication
    Mutagenesisi682 – 6821G → R: No obvious phenotype. May cause partial loss of kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 780780cGMP-dependent protein kinase egl-4PRO_0000390491Add
    BLAST

    Post-translational modificationi

    Autophosphorylated.1 Publication

    Proteomic databases

    EPDiO76360.
    PaxDbiO76360.
    PRIDEiO76360.

    Expressioni

    Tissue specificityi

    Expressed in AWC sensory neurons (at protein level) (PubMed:20220099). Mainly expressed in head neurons, hypodermis, intestine and body wall muscles. L2 and L3 larvae show extensive expression, lower levels are observed in L4 larvae, later embryos and adults. Isoform c is expressed in a subset of neurons in the head, nerve ring, and ventral nerve cord including some motor neurons, also in several neurons in the tail, the pharyngeal marginal cells, body muscle, intestine, vulval muscles, and spermatheca (PubMed:11181837, PubMed:12571101, PubMed:15330854).4 Publications

    Gene expression databases

    ExpressionAtlasiO76360. baseline.

    Interactioni

    Subunit structurei

    When phosphorylated, interacts with saeg-2. May interact with saeg-1.1 Publication

    Protein-protein interaction databases

    STRINGi6239.F55A8.2a.1.

    Structurei

    3D structure databases

    ProteinModelPortaliO76360.
    SMRiO76360. Positions 131-772.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini469 – 729261Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini730 – 78051AGC-kinase C-terminalSequence analysisAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili61 – 12767Sequence analysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi492 – 50413Nuclear localization signalSequence analysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi10 – 3627Gly-richSequence analysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Sequence analysis
    Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiKOG0616. Eukaryota.
    ENOG410XPQQ. LUCA.
    GeneTreeiENSGT00810000125385.
    HOGENOMiHOG000233033.
    InParanoidiO76360.
    OMAiWIVKLYK.
    PhylomeDBiO76360.

    Family and domain databases

    Gene3Di2.60.120.10. 2 hits.
    InterProiIPR000961. AGC-kinase_C.
    IPR002374. cGMP_dep_kinase.
    IPR018490. cNMP-bd-like.
    IPR018488. cNMP-bd_CS.
    IPR000595. cNMP-bd_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR014710. RmlC-like_jellyroll.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00027. cNMP_binding. 2 hits.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000559. cGMP-dep_kinase. 1 hit.
    PRINTSiPR00104. CGMPKINASE.
    SMARTiSM00100. cNMP. 2 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF51206. SSF51206. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00888. CNMP_BINDING_1. 2 hits.
    PS00889. CNMP_BINDING_2. 2 hits.
    PS50042. CNMP_BINDING_3. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform a2 Publications (identifier: O76360-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MSSGSRPSSG GGGGGGGASG GAGGGAPGGG GGGIRGFFSK LRKPSDQPNG
    60 70 80 90 100
    NQVQVGTRTF EAHELQKLIP QLEEAISRKD AQLRQQQTIV EGHIKRISEL
    110 120 130 140 150
    EGEVTTLQRE CDKLRSVLEQ KAQSAASPGG QPPSPSPRTD QLGNDLQQKA
    160 170 180 190 200
    VLPADGVQRA KKIAVSAEPT NFENKPATLQ HYNKTVGAKQ MIRDAVQKND
    210 220 230 240 250
    FLKQLAKEQI IELVNCMYEM RARAGQWVIQ EGEPGDRLFV VAEGELQVSR
    260 270 280 290 300
    EGALLGKMRA GTVMGELAIL YNCTRTASVQ ALTDVQLWVL DRSVFQMITQ
    310 320 330 340 350
    RLGMERHSQL MNFLTKVSIF QNLSEDRISK MADVMDQDYY DGGHYIIRQG
    360 370 380 390 400
    EKGDAFFVIN SGQVKVTQQI EGETEPREIR VLNQGDFFGE RALLGEEVRT
    410 420 430 440 450
    ANIIAQAPGV EVLTLDRESF GKLIGDLESL KKDYGDKERL AQVVREPPSP
    460 470 480 490 500
    VKIVDDFREE FAQVTLKNVK RLATLGVGGF GRVELVCVNG DKAKTFALKA
    510 520 530 540 550
    LKKKHIVDTR QQEHIFAERN IMMETSTDWI VKLYKTFRDQ KFVYMLLEVC
    560 570 580 590 600
    LGGELWTTLR DRGHFDDYTA RFYVACVLEG LEYLHRKNIV YRDLKPENCL
    610 620 630 640 650
    LANTGYLKLV DFGFAKKLAS GRKTWTFCGT PEYVSPEIIL NKGHDQAADY
    660 670 680 690 700
    WALGIYICEL MLGRPPFQAS DPMKTYTLIL KGVDALEIPN RRIGKTATAL
    710 720 730 740 750
    VKKLCRDNPG ERLGSGSGGV NDIRKHRWFM GFDWEGLRSR TLKPPILPKV
    760 770 780
    SNPADVTNFD NYPPDNDVPP DEFSGWDEGF
    Length:780
    Mass (Da):86,742
    Last modified:November 1, 1999 - v2
    Checksum:i55E036AF50626DD2
    GO
    Isoform b2 Publications (identifier: O76360-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-43: Missing.
         44-52: PSDQPNGNQ → MKQQPPRIY

    Show »
    Length:737
    Mass (Da):83,354
    Checksum:iA3D63A797100B9C8
    GO
    Isoform c2 Publications (identifier: O76360-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-20: MSSGSRPSSGGGGGGGGASG → MYGSSRHHMDSFSSNDGGAFL
         21-52: Missing.

    Show »
    Length:749
    Mass (Da):84,498
    Checksum:iADE0B9F6354D93C6
    GO
    Isoform d1 Publication (identifier: O76360-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-188: Missing.
         189-275: KQMIRDAVQK...ELAILYNCTR → MLTCSTTTCQ...NLFYKRSHKK
         353-749: Missing.

    Note: No experimental confirmation available.Curated
    Show »
    Length:195
    Mass (Da):22,855
    Checksum:i37BEC2E725BBA168
    GO
    Isoform e1 Publication (identifier: O76360-5) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-37: Missing.
         38-52: FSKLRKPSDQPNGNQ → MCWKFNPLKALRVVE

    Note: No experimental confirmation available.Curated
    Show »
    Length:743
    Mass (Da):84,028
    Checksum:i05386588EABC90AB
    GO
    Isoform f1 Publication (identifier: O76360-6) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-310: Missing.
         311-316: MNFLTK → MKKVYV

    Note: No experimental confirmation available.Curated
    Show »
    Length:470
    Mass (Da):53,421
    Checksum:iB57D4D78EA028BCA
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 310310Missing in isoform f. 1 PublicationVSP_053170Add
    BLAST
    Alternative sequencei1 – 188188Missing in isoform d. 1 PublicationVSP_053171Add
    BLAST
    Alternative sequencei1 – 4343Missing in isoform b. 2 PublicationsVSP_053172Add
    BLAST
    Alternative sequencei1 – 3737Missing in isoform e. 1 PublicationVSP_053173Add
    BLAST
    Alternative sequencei1 – 2020MSSGS…GGASG → MYGSSRHHMDSFSSNDGGAF L in isoform c. 2 PublicationsVSP_053174Add
    BLAST
    Alternative sequencei21 – 5232Missing in isoform c. 2 PublicationsVSP_053175Add
    BLAST
    Alternative sequencei38 – 5215FSKLR…PNGNQ → MCWKFNPLKALRVVE in isoform e. 1 PublicationVSP_053176Add
    BLAST
    Alternative sequencei44 – 529PSDQPNGNQ → MKQQPPRIY in isoform b. 2 PublicationsVSP_053177
    Alternative sequencei189 – 27587KQMIR…YNCTR → MLTCSTTTCQISPAYPKFIE KLRRMIWGREPSTSYEFDEL AQQVALKSHRRNVDDGYYVE EIHFEPPQVVRKKQPTRNLF YKRSHKK in isoform d. 1 PublicationVSP_053178Add
    BLAST
    Alternative sequencei311 – 3166MNFLTK → MKKVYV in isoform f. 1 PublicationVSP_053179
    Alternative sequencei353 – 749397Missing in isoform d. 1 PublicationVSP_053180Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    FO081473 Genomic DNA. Translation: CCD71859.1.
    FO081473 Genomic DNA. Translation: CCD71860.1.
    FO081473 Genomic DNA. Translation: CCD71861.1.
    FO081473 Genomic DNA. Translation: CCD71862.1.
    FO081473 Genomic DNA. Translation: CCD71863.1.
    FO081473 Genomic DNA. Translation: CCD71864.1.
    RefSeqiNP_001023223.1. NM_001028052.2. [O76360-5]
    NP_001023224.1. NM_001028053.2. [O76360-6]
    NP_500141.1. NM_067740.4. [O76360-1]
    NP_500142.1. NM_067741.3. [O76360-2]
    NP_741329.1. NM_171279.3. [O76360-3]
    NP_741330.2. NM_171280.2. [O76360-4]
    UniGeneiCel.38682.

    Genome annotation databases

    EnsemblMetazoaiF55A8.2a.1; F55A8.2a.1; WBGene00001173. [O76360-1]
    F55A8.2a.2; F55A8.2a.2; WBGene00001173. [O76360-1]
    GeneIDi176991.
    UCSCiF55A8.2a.1. c. elegans. [O76360-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    FO081473 Genomic DNA. Translation: CCD71859.1.
    FO081473 Genomic DNA. Translation: CCD71860.1.
    FO081473 Genomic DNA. Translation: CCD71861.1.
    FO081473 Genomic DNA. Translation: CCD71862.1.
    FO081473 Genomic DNA. Translation: CCD71863.1.
    FO081473 Genomic DNA. Translation: CCD71864.1.
    RefSeqiNP_001023223.1. NM_001028052.2. [O76360-5]
    NP_001023224.1. NM_001028053.2. [O76360-6]
    NP_500141.1. NM_067740.4. [O76360-1]
    NP_500142.1. NM_067741.3. [O76360-2]
    NP_741329.1. NM_171279.3. [O76360-3]
    NP_741330.2. NM_171280.2. [O76360-4]
    UniGeneiCel.38682.

    3D structure databases

    ProteinModelPortaliO76360.
    SMRiO76360. Positions 131-772.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi6239.F55A8.2a.1.

    Proteomic databases

    EPDiO76360.
    PaxDbiO76360.
    PRIDEiO76360.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblMetazoaiF55A8.2a.1; F55A8.2a.1; WBGene00001173. [O76360-1]
    F55A8.2a.2; F55A8.2a.2; WBGene00001173. [O76360-1]
    GeneIDi176991.
    UCSCiF55A8.2a.1. c. elegans. [O76360-1]

    Organism-specific databases

    CTDi176991.
    WormBaseiF55A8.2a; CE19897; WBGene00001173; egl-4.
    F55A8.2b; CE19898; WBGene00001173; egl-4.
    F55A8.2c; CE31541; WBGene00001173; egl-4.
    F55A8.2d; CE37718; WBGene00001173; egl-4.
    F55A8.2e; CE37241; WBGene00001173; egl-4.
    F55A8.2f; CE37242; WBGene00001173; egl-4.

    Phylogenomic databases

    eggNOGiKOG0616. Eukaryota.
    ENOG410XPQQ. LUCA.
    GeneTreeiENSGT00810000125385.
    HOGENOMiHOG000233033.
    InParanoidiO76360.
    OMAiWIVKLYK.
    PhylomeDBiO76360.

    Enzyme and pathway databases

    ReactomeiR-CEL-392517. Rap1 signalling.
    SABIO-RKO76360.
    SignaLinkiO76360.

    Miscellaneous databases

    NextBioi894878.
    PROiO76360.

    Gene expression databases

    ExpressionAtlasiO76360. baseline.

    Family and domain databases

    Gene3Di2.60.120.10. 2 hits.
    InterProiIPR000961. AGC-kinase_C.
    IPR002374. cGMP_dep_kinase.
    IPR018490. cNMP-bd-like.
    IPR018488. cNMP-bd_CS.
    IPR000595. cNMP-bd_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR014710. RmlC-like_jellyroll.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00027. cNMP_binding. 2 hits.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000559. cGMP-dep_kinase. 1 hit.
    PRINTSiPR00104. CGMPKINASE.
    SMARTiSM00100. cNMP. 2 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF51206. SSF51206. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00888. CNMP_BINDING_1. 2 hits.
    PS00889. CNMP_BINDING_2. 2 hits.
    PS50042. CNMP_BINDING_3. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A cGMP-dependent protein kinase is implicated in wild-type motility in C. elegans."
      Stansberry J., Baude E.J., Taylor M.K., Chen P.J., Jin S.W., Ellis R.E., Uhler M.D.
      J. Neurochem. 76:1177-1187(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, DISRUPTION PHENOTYPE.
    2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
      Strain: Bristol N2.
    3. "egl-4 acts through a transforming growth factor-beta/SMAD pathway in Caenorhabditis elegans to regulate multiple neuronal circuits in response to sensory cues."
      Daniels S.A., Ailion M., Thomas J.H., Sengupta P.
      Genetics 156:123-141(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    4. "The cyclic GMP-dependent protein kinase EGL-4 regulates olfactory adaptation in C. elegans."
      L'Etoile N.D., Coburn C.M., Eastham J., Kistler A., Gallegos G., Bargmann C.I.
      Neuron 36:1079-1089(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF LYS-502.
    5. "Cyclic GMP-dependent protein kinase EGL-4 controls body size and lifespan in C elegans."
      Hirose T., Nakano Y., Nagamatsu Y., Misumi T., Ohta H., Ohshima Y.
      Development 130:1089-1099(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    6. "cGMP and a germ-line signal control body size in C. elegans through cGMP-dependent protein kinase EGL-4."
      Nakano Y., Nagamatsu Y., Ohshima Y.
      Genes Cells 9:773-779(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    7. "A novel gain-of-function mutant of the cyclic GMP-dependent protein kinase egl-4 affects multiple physiological processes in Caenorhabditis elegans."
      Raizen D.M., Cullison K.M., Pack A.I., Sundaram M.V.
      Genetics 173:177-187(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-362.
    8. "Insulin, cGMP, and TGF-beta signals regulate food intake and quiescence in C. elegans: a model for satiety."
      You Y.J., Kim J., Raizen D.M., Avery L.
      Cell Metab. 7:249-257(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The EGL-4 PKG acts with KIN-29 salt-inducible kinase and protein kinase A to regulate chemoreceptor gene expression and sensory behaviors in Caenorhabditis elegans."
      van der Linden A.M., Wiener S., You Y.J., Kim K., Avery L., Sengupta P.
      Genetics 180:1475-1491(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    10. "Nuclear entry of a cGMP-dependent kinase converts transient into long-lasting olfactory adaptation."
      Lee J.I., O'Halloran D.M., Eastham-Anderson J., Juang B.T., Kaye J.A., Scott Hamilton O., Lesch B., Goga A., L'Etoile N.D.
      Proc. Natl. Acad. Sci. U.S.A. 107:6016-6021(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF THR-276 AND ASP-611.
    11. "Nuclear cGMP-dependent kinase regulates gene expression via activity-dependent recruitment of a conserved histone deacetylase complex."
      Hao Y., Xu N., Box A.C., Schaefer L., Kannan K., Zhang Y., Florens L., Seidel C., Washburn M.P., Wiegraebe W., Mak H.Y.
      PLoS Genet. 7:E1002065-E1002065(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-162; ALA-497; LYS-499 AND GLY-682.
    12. "Changes in cGMP levels affect the localization of EGL-4 in AWC in Caenorhabditis elegans."
      O'Halloran D.M., Hamilton O.S., Lee J.I., Gallegos M., L'Etoile N.D.
      PLoS ONE 7:E31614-E31614(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-276.
    13. "Environmental alkalinity sensing mediated by the transmembrane guanylyl cyclase GCY-14 in C. elegans."
      Murayama T., Takayama J., Fujiwara M., Maruyama I.N.
      Curr. Biol. 23:1007-1012(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Nuclear PKG localization is regulated by G(0) alpha and is necessary in the AWB neurons to mediate avoidance in Caenorhabditis elegans."
      He C., O'Halloran D.M.
      Neurosci. Lett. 553:35-39(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. "The C. elegans cGMP-dependent protein kinase EGL-4 regulates nociceptive behavioral sensitivity."
      Krzyzanowski M.C., Brueggemann C., Ezak M.J., Wood J.F., Michaels K.L., Jackson C.A., Juang B.T., Collins K.D., Yu M.C., L'etoile N.D., Ferkey D.M.
      PLoS Genet. 9:E1003619-E1003619(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    16. "The receptor-bound guanylyl cyclase DAF-11 is the mediator of hydrogen peroxide-induced cGMP increase in Caenorhabditis elegans."
      Beckert U., Aw W.Y., Burhenne H., Forsterling L., Kaever V., Timmons L., Seifert R.
      PLoS ONE 8:E72569-E72569(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiEGL4_CAEEL
    AccessioniPrimary (citable) accession number: O76360
    Secondary accession number(s): Q688A8
    , Q688A9, Q7KPJ2, Q8MXG6, Q8MXG7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2009
    Last sequence update: November 1, 1999
    Last modified: May 11, 2016
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.