DLK1_CAEEL
ID DLK1_CAEEL Reviewed; 928 AA.
AC O01700; B3KYB4; Q7JKE7; Q7JKE9;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 4.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase dlk-1 {ECO:0000250|UniProtKB:O43283};
DE EC=2.7.11.25 {ECO:0000250|UniProtKB:O43283};
DE AltName: Full=DAP kinase-like kinase;
DE AltName: Full=Death-associated protein kinase-like kinase;
GN Name=dlk-1; ORFNames=F33E2.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CAB06544.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB06544.3};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND UBIQUITINATION.
RX PubMed=15707898; DOI=10.1016/j.cell.2004.12.017;
RA Nakata K., Abrams B., Grill B., Goncharov A., Huang X., Chisholm A.D.,
RA Jin Y.;
RT "Regulation of a DLK-1 and p38 MAP kinase pathway by the ubiquitin ligase
RT RPM-1 is required for presynaptic development.";
RL Cell 120:407-420(2005).
RN [3] {ECO:0000305}
RP ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17698012; DOI=10.1016/j.neuron.2007.07.009;
RA Grill B., Bienvenut W.V., Brown H.M., Ackley B.D., Quadroni M., Jin Y.;
RT "C. elegans RPM-1 regulates axon termination and synaptogenesis through the
RT Rab GEF GLO-4 and the Rab GTPase GLO-1.";
RL Neuron 55:587-601(2007).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=18224716; DOI=10.1002/dvdy.21446;
RA Abrams B., Grill B., Huang X., Jin Y.;
RT "Cellular and molecular determinants targeting the Caenorhabditis elegans
RT PHR protein RPM-1 to perisynaptic regions.";
RL Dev. Dyn. 237:630-639(2008).
RN [5]
RP FUNCTION.
RX PubMed=19737525; DOI=10.1016/j.cell.2009.06.023;
RA Yan D., Wu Z., Chisholm A.D., Jin Y.;
RT "The DLK-1 kinase promotes mRNA stability and local translation in C.
RT elegans synapses and axon regeneration.";
RL Cell 138:1005-1018(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19164707; DOI=10.1126/science.1165527;
RA Hammarlund M., Nix P., Hauth L., Jorgensen E.M., Bastiani M.;
RT "Axon regeneration requires a conserved MAP kinase pathway.";
RL Science 323:802-806(2009).
RN [7] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-144; 166-GLN--ILE-928; 181-GLN--ILE-928;
RP ASP-246 AND GLY-308.
RX PubMed=21368137; DOI=10.1073/pnas.1101360108;
RA Bounoutas A., Kratz J., Emtage L., Ma C., Nguyen K.C., Chalfie M.;
RT "Microtubule depolymerization in Caenorhabditis elegans touch receptor
RT neurons reduces gene expression through a p38 MAPK pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:3982-3987(2011).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23000142; DOI=10.1016/j.devcel.2012.08.010;
RA Ghosh-Roy A., Goncharov A., Jin Y., Chisholm A.D.;
RT "Kinesin-13 and tubulin posttranslational modifications regulate
RT microtubule growth in axon regeneration.";
RL Dev. Cell 23:716-728(2012).
RN [9]
RP FUNCTION (ISOFORMS A AND C), ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR
RP LOCATION (ISOFORMS A AND C), ALTERNATIVE POLYADENYLATION, DOMAIN, MOTIF,
RP PHOSPHORYLATION AT SER-874 AND SER-878, AND MUTAGENESIS OF
RP 312-TRP--ILE-928; ARG-363; 449-LEU--LEU-480; LEU-459; 605-SER--ASP-814;
RP 523-ARG--ILE-928; 631-GLY--ILE-928; 816-ARG--ILE-928; GLY-870; SER-874;
RP SER-878 AND 874-SER--ASP-879.
RX PubMed=23141066; DOI=10.1016/j.neuron.2012.08.043;
RA Yan D., Jin Y.;
RT "Regulation of DLK-1 kinase activity by calcium-mediated dissociation from
RT an inhibitory isoform.";
RL Neuron 76:534-548(2012).
RN [10]
RP ALTERNATIVE POLYADENYLATION.
RX PubMed=26588990; DOI=10.1101/gad.266650.115;
RA Chen F., Zhou Y., Qi Y.B., Khivansara V., Li H., Chun S.Y., Kim J.K.,
RA Fu X.D., Jin Y.;
RT "Context-dependent modulation of Pol II CTD phosphatase SSUP-72 regulates
RT alternative polyadenylation in neuronal development.";
RL Genes Dev. 29:2377-2390(2015).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26657059; DOI=10.1371/journal.pgen.1005733;
RA van der Vaart A., Rademakers S., Jansen G.;
RT "DLK-1/p38 MAP Kinase signaling controls cilium length by regulating RAB-5
RT mediated endocytosis in Caenorhabditis elegans.";
RL PLoS Genet. 11:E1005733-E1005733(2015).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27123983; DOI=10.1371/journal.pgen.1006010;
RA D'Souza S.A., Rajendran L., Bagg R., Barbier L., van Pel D.M., Moshiri H.,
RA Roy P.J.;
RT "The MADD-3 LAMMER kinase interacts with a p38 MAP kinase pathway to
RT regulate the display of the EVA-1 guidance receptor in Caenorhabditis
RT elegans.";
RL PLoS Genet. 12:E1006010-E1006010(2016).
CC -!- FUNCTION: Component of a MAP kinase pathway that functions
CC presynaptically to regulate synaptic architecture and presynaptic
CC differentiation (PubMed:15707898). Phosphorylates and activates mkk-4
CC (PubMed:15707898). Has a role in axonal regrowth following injury and
CC synaptogenesis (PubMed:19737525, PubMed:19164707). Plays a role in
CC modulating polymerization of neuronal microtubules (PubMed:21368137).
CC Also promotes tubulin post-translational modifications that protect
CC microtubules (PubMed:23000142). Plays a role in cilium length
CC regulation, possibly by reducing rab-5 mediated endocytosis, and may
CC also have a role in intraflagellar transport in cilia
CC (PubMed:26657059). Plays a role in the formation of muscle connections,
CC also called muscle arm extensions, between the body wall and the motor
CC axons in the dorsal and ventral cord (PubMed:27123983).
CC {ECO:0000269|PubMed:15707898, ECO:0000269|PubMed:19164707,
CC ECO:0000269|PubMed:19737525, ECO:0000269|PubMed:23000142,
CC ECO:0000269|PubMed:26657059, ECO:0000269|PubMed:27123983}.
CC -!- FUNCTION: [Isoform a]: Has a role in synapse and axon development, and
CC in axonal regrowth following injury. {ECO:0000269|PubMed:23141066}.
CC -!- FUNCTION: [Isoform c]: By forming heterooligomers with isoform a, acts
CC as an inhibitor of isoform a activation. Its inhibitory function is
CC independent of its catalytic activity. {ECO:0000269|PubMed:23141066}.
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=2.7.11.25;
CC Evidence={ECO:0000250|UniProtKB:O43283};
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=2.7.11.25; Evidence={ECO:0000250|UniProtKB:O43283};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O43283};
CC -!- ACTIVITY REGULATION: [Isoform a]: Inactive when associated with isoform
CC c. Dissociation from isoform c, which is dependent on the
CC phosphorylation of the C-terminal hexapeptide, results in self-
CC association and activation. Transient increase in Ca(2+) levels caused
CC by axonal injury or synaptic activity triggers the dissociation of
CC isoform a from isoform c; the dissociation may be influenced by the
CC phosphorylation status of the C-terminal hexapeptide.
CC {ECO:0000269|PubMed:23141066}.
CC -!- SUBUNIT: Homooligomer (via leucine zipper domain and hexapeptide motif)
CC (PubMed:23141066). Isoform a (via leucine zipper domain) forms a
CC heterooligomer with isoform c (via leucine zipper domain)
CC (PubMed:23141066). Isoform c does not self-associate (PubMed:23141066).
CC {ECO:0000269|PubMed:23141066}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:15707898,
CC ECO:0000269|PubMed:18224716, ECO:0000269|PubMed:23000142}. Cytoplasm
CC {ECO:0000269|PubMed:26657059}. Cell projection, axon
CC {ECO:0000269|PubMed:26657059}. Cell projection, dendrite
CC {ECO:0000269|PubMed:26657059}. Cell projection, cilium
CC {ECO:0000269|PubMed:26657059}. Note=Observed in the periactive zone of
CC the presynaptic terminal which surrounds the synaptic vesicle clusters
CC and active zones. {ECO:0000269|PubMed:15707898}.
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Synapse
CC {ECO:0000269|PubMed:23141066}. Cell projection, axon
CC {ECO:0000269|PubMed:23141066}. Note=Co-localizes with isoform c in
CC synapses and axons; however, isoform a localization is independent on
CC its interaction with isoform c. During axonal injury, recruited to the
CC injured site. {ECO:0000269|PubMed:23141066}.
CC -!- SUBCELLULAR LOCATION: [Isoform c]: Synapse
CC {ECO:0000269|PubMed:23141066}. Cell projection, axon
CC {ECO:0000269|PubMed:23141066}. Note=Co-localizes with isoform c in
CC synapses and axons; however, localization is dependent of its
CC interaction with isoform a. {ECO:0000269|PubMed:23141066}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=a {ECO:0000312|WormBase:F33E2.2a}; Synonyms=DLK-1L
CC {ECO:0000303|PubMed:23141066};
CC IsoId=O01700-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F33E2.2b};
CC IsoId=O01700-2; Sequence=VSP_052967;
CC Name=c {ECO:0000312|WormBase:F33E2.2c}; Synonyms=DLK-1S
CC {ECO:0000303|PubMed:23141066};
CC IsoId=O01700-3; Sequence=VSP_052965, VSP_052966;
CC Name=d {ECO:0000312|WormBase:F33E2.2d};
CC IsoId=O01700-4; Sequence=VSP_052964;
CC -!- TISSUE SPECIFICITY: Expressed in nerve ring, nerve cord, neurons, and
CC pharynx. {ECO:0000269|PubMed:15707898, ECO:0000269|PubMed:23000142}.
CC -!- DOMAIN: [Isoform a]: The C-terminal hexapeptide motif is required for
CC homooligomerization and for its activation.
CC {ECO:0000269|PubMed:23141066}.
CC -!- DOMAIN: [Isoform a]: The C-terminal domain is important for
CC localization to synapses and axons. {ECO:0000269|PubMed:23141066}.
CC -!- PTM: Ubiquitinated by rpm-1. Negatively regulated by ubiquitination by
CC fsn-1 bound rpm-1, followed by degradation.
CC {ECO:0000269|PubMed:15707898}.
CC -!- PTM: [Isoform a]: Phosphorylation at Ser-874 and/or at Ser-878
CC abolishes interaction with isoform c and promotes binding to isoform a
CC kinase domain (likely in trans) resulting in isoform a self-association
CC and activation. {ECO:0000269|PubMed:23141066}.
CC -!- DISRUPTION PHENOTYPE: Overcome the lack of synaptogenesis caused by the
CC loss of rpm-1 ubiquitin ligase activity (PubMed:17698012). Defects in
CC axonal microtubule development (PubMed:19164707, PubMed:23000142).
CC Double knockout with dlk-1 also suppresses the eva-1 receptor
CC expression defect in the madd-3 single knockout (PubMed:27123983).
CC Triple knockout with madd-3 and unc-54 results in paralysis (as in the
CC unc-54 single knockout), and suppresses the lethality phenotype in the
CC double madd-3 and unc-54 mutant (PubMed:27123983).
CC {ECO:0000269|PubMed:17698012, ECO:0000269|PubMed:19164707,
CC ECO:0000269|PubMed:23000142, ECO:0000269|PubMed:27123983}.
CC -!- MISCELLANEOUS: [Isoform c]: Produced by alternative polyadenylation.
CC The alternative polyadenylation site is in intron 7. In neurons, the
CC usage of this polyadenylation site is regulated by the antagonist
CC action of sydn-1 and ssup-72. {ECO:0000269|PubMed:23141066,
CC ECO:0000269|PubMed:26588990}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000250|UniProtKB:O43283}.
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DR EMBL; BX284601; CAB06544.3; -; Genomic_DNA.
DR EMBL; AL022593; CAB06544.3; JOINED; Genomic_DNA.
DR EMBL; BX284601; CAE54890.1; -; Genomic_DNA.
DR EMBL; BX284601; CAE54891.1; -; Genomic_DNA.
DR EMBL; AL022593; CAE54891.1; JOINED; Genomic_DNA.
DR EMBL; BX284601; CAQ76474.1; -; Genomic_DNA.
DR EMBL; AL022593; CAQ76474.1; JOINED; Genomic_DNA.
DR PIR; B87950; B87950.
DR PIR; T20082; T20082.
DR RefSeq; NP_001021443.1; NM_001026272.3. [O01700-1]
DR RefSeq; NP_001021444.1; NM_001026273.5. [O01700-2]
DR RefSeq; NP_001021445.1; NM_001026274.3. [O01700-3]
DR RefSeq; NP_001129769.1; NM_001136297.2. [O01700-4]
DR AlphaFoldDB; O01700; -.
DR SMR; O01700; -.
DR BioGRID; 38525; 3.
DR DIP; DIP-26475N; -.
DR IntAct; O01700; 4.
DR STRING; 6239.F33E2.2a; -.
DR iPTMnet; O01700; -.
DR EPD; O01700; -.
DR PaxDb; O01700; -.
DR PRIDE; O01700; -.
DR EnsemblMetazoa; F33E2.2a.1; F33E2.2a.1; WBGene00001008. [O01700-1]
DR EnsemblMetazoa; F33E2.2b.1; F33E2.2b.1; WBGene00001008. [O01700-2]
DR EnsemblMetazoa; F33E2.2c.1; F33E2.2c.1; WBGene00001008. [O01700-3]
DR EnsemblMetazoa; F33E2.2d.1; F33E2.2d.1; WBGene00001008. [O01700-4]
DR GeneID; 173128; -.
DR KEGG; cel:CELE_F33E2.2; -.
DR UCSC; F33E2.2b; c. elegans.
DR CTD; 173128; -.
DR WormBase; F33E2.2a; CE36153; WBGene00001008; dlk-1. [O01700-1]
DR WormBase; F33E2.2b; CE36154; WBGene00001008; dlk-1. [O01700-2]
DR WormBase; F33E2.2c; CE36155; WBGene00001008; dlk-1. [O01700-3]
DR WormBase; F33E2.2d; CE23702; WBGene00001008; dlk-1. [O01700-4]
DR eggNOG; KOG4721; Eukaryota.
DR GeneTree; ENSGT00940000159006; -.
DR InParanoid; O01700; -.
DR OMA; RETPYAN; -.
DR OrthoDB; 938929at2759; -.
DR PhylomeDB; O01700; -.
DR SignaLink; O01700; -.
DR PRO; PR:O01700; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001008; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; O01700; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:WormBase.
DR GO; GO:0048677; P:axon extension involved in regeneration; IMP:WormBase.
DR GO; GO:0031103; P:axon regeneration; IGI:UniProtKB.
DR GO; GO:0048689; P:formation of growth cone in injured axon; IMP:WormBase.
DR GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
DR GO; GO:0038066; P:p38MAPK cascade; IMP:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; IGI:WormBase.
DR GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:InterPro.
DR GO; GO:1905868; P:regulation of 3'-UTR-mediated mRNA stabilization; IGI:UniProtKB.
DR GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IGI:UniProtKB.
DR GO; GO:0050807; P:regulation of synapse organization; IGI:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017419; MAP3K12_MAP3K13.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038165; MAPKKK12_MAPKKK13; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cytoplasm; Kinase;
KW Magnesium; Metal-binding; Neurogenesis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Synapse; Transferase;
KW Ubl conjugation.
FT CHAIN 1..928
FT /note="Mitogen-activated protein kinase kinase kinase dlk-
FT 1"
FT /id="PRO_0000353198"
FT DOMAIN 135..377
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..480
FT /note="Leucine-zipper"
FT /evidence="ECO:0000269|PubMed:23141066"
FT REGION 483..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..814
FT /note="Important for interaction between isoform a and
FT isoform c"
FT /evidence="ECO:0000269|PubMed:23141066"
FT REGION 644..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 874..879
FT /note="SDGLSD hexapeptide"
FT /evidence="ECO:0000269|PubMed:23141066"
FT COMPBIAS 1..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 246
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43283,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 141..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43283,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O43283,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:23141066"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:23141066"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052964"
FT VAR_SEQ 567..577
FT /note="KILRNDAIRHS -> SEYIFPEKLNI (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052965"
FT VAR_SEQ 578..928
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052966"
FT VAR_SEQ 674..681
FT /note="GVISCSSP -> A (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052967"
FT MUTAGEN 144
FT /note="G->R: In u816; Suppresses microtubule disruption in
FT touch receptor neurons caused by colchicine."
FT /evidence="ECO:0000269|PubMed:21368137"
FT MUTAGEN 166..928
FT /note="Missing: In u818; Suppresses microtubule disruption
FT in touch receptor neurons caused by colchicine."
FT /evidence="ECO:0000269|PubMed:21368137"
FT MUTAGEN 181..928
FT /note="Missing: In u817; Suppresses microtubule disruption
FT in touch receptor neurons caused by colchicine."
FT /evidence="ECO:0000269|PubMed:21368137"
FT MUTAGEN 246
FT /note="D->N: In u820; Suppresses microtubule disruption in
FT touch receptor neurons caused by colchicine."
FT /evidence="ECO:0000269|PubMed:21368137"
FT MUTAGEN 308
FT /note="G->E: In u815; Suppresses microtubule disruption in
FT touch receptor neurons caused by colchicine."
FT /evidence="ECO:0000269|PubMed:21368137"
FT MUTAGEN 312..928
FT /note="Missing: In ju588; restores motor neuron normal
FT presynapse morphology and number in a rpm-1 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:23141066"
FT MUTAGEN 363
FT /note="R->H: In ju586; restores motor neuron normal
FT presynapse morphology and number in a rpm-1 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:23141066"
FT MUTAGEN 449..480
FT /note="Missing: Prevents self-association or interaction
FT with isoform c."
FT /evidence="ECO:0000269|PubMed:23141066"
FT MUTAGEN 459
FT /note="L->F: In ju591; restores normal motor neuron
FT presynapse morphology and number in a rpm-1 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:23141066"
FT MUTAGEN 523..928
FT /note="Missing: In ju598; restores normal motor neuron
FT presynaspe morphology and number in a rpm-1 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:23141066"
FT MUTAGEN 605..814
FT /note="Missing: Prevents interaction with isoform c."
FT /evidence="ECO:0000269|PubMed:23141066"
FT MUTAGEN 631..928
FT /note="Missing: In ju476; does not affect c mRNA levels.
FT Restores normal motor neuron presynapse morphology and
FT number in a rpm-1 mutant background. Suppresses microtubule
FT disruption in touch receptor neurons caused by colchicine."
FT /evidence="ECO:0000269|PubMed:21368137,
FT ECO:0000269|PubMed:23141066"
FT MUTAGEN 816..928
FT /note="Missing: In ju636; restores normal motor neuron
FT presynapse morphology and number in a rpm-1 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:23141066"
FT MUTAGEN 870
FT /note="G->E: In ju620; restores normal motor neuron
FT presynapse morphology and number in a rpm-1 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:23141066"
FT MUTAGEN 874..879
FT /note="Missing: Abolishes self-association and enhances
FT interaction with isoform c."
FT /evidence="ECO:0000269|PubMed:23141066"
FT MUTAGEN 874
FT /note="S->A: Prevents phosphorylation. Enhances binding to
FT isoform c; when associated with A-878."
FT /evidence="ECO:0000269|PubMed:23141066"
FT MUTAGEN 874
FT /note="S->E: Phosphomimetic mutant. Enhances self-
FT association and increases binding of the hexapeptide motif
FT to the kinase domain; when associated with E-878."
FT /evidence="ECO:0000269|PubMed:23141066"
FT MUTAGEN 878
FT /note="S->A: Prevents phosphorylation. Enhances binding to
FT isoform c; when associated with A-874."
FT /evidence="ECO:0000269|PubMed:23141066"
FT MUTAGEN 878
FT /note="S->E: Phosphomimetic mutant. Enhances self-
FT association and increases binding of the hexapeptide motif
FT to the kinase domain; when associated with E-874."
FT /evidence="ECO:0000269|PubMed:23141066"
SQ SEQUENCE 928 AA; 103483 MW; EE071636ACAADBD4 CRC64;
MTSTTMVTTL DLVTPTSEEQ PGPAPESSDF STVVLSPDGS ELVTQSAPNT PIQHREQANA
EFGQKEGSPD PKNMVAATGN ASKPSLNSFY ADGLGQLRNG LFSCFQPVFG YFGTKTTVEI
EKSEDELWEI PFDAISELEW LGSGSQGAVF RGQLENRTVA VKKVNQLKET EIKHLRHLRH
QNIIEFLGVC SKSPCYCIVM EYCSKGQLCT VLKSRNTITR ELFAQWVKEI ADGMHYLHQN
KVIHRDLKSP NILISAEDSI KICDFGTSHM QKKMDSTMMS FCGTVSWMAP EMIKKQPCNE
KVDVYSFGVV LWEMLTRETP YANIAQMAII FGVGTNILSL PMPEEAPKGL VLLIKQCLSQ
KGRNRPSFSH IRQHWEIFKP ELFEMTEEEW QLAWDSYREF AKCIQYPSTV TRDHGGPKSA
FAMEEEIQRK RHEQLNHIKD IRNMYEMKLK RTNKMYDKLQ GCFTELKLKE SELAEWEKDL
TEREQWHNQN SPKAVAAPRA QLRGYPNEGY DDMSSDEDVQ PCRGSPYRCS NTSSSSGVQS
SPFSRQSSSR SSAGQQTRRS EGANPPKILR NDAIRHSGSY WETLGGARGS PARDSGFSQD
SGMWSAGAGS CTAINGGGQQ VCYSQTLYRN GDGRWSDGRI ASRRRVSTSV NKSTAVPGQP
VFFTRDSPSR VPHGVISCSS PRSSSKLNRS SYPSRNAPHQ LEDGCCCAHA RAPRAKSIAV
PMTSSSRARS PTPYDNDFEN AESFVDPESP KNLKNLEKIV NLPESTSYDE ALCNSDVTMN
PIYTSPITTY SNPCHVELVD EENANDVDLT SSMDSRRSRS DDADVESSEE DEGNGNNILN
TSMESEDLRY RIDTSQSTMM SSLERSLEIG ATRSDGLSDN EMRVQAVKMS IKTHRRTGSN
PQALIHQCID EYTTSATDDS DDAGAVRI
