DCLK_CAEEL
ID DCLK_CAEEL Reviewed; 802 AA.
AC Q95QC4; Q9U1S0;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Serine/threonine-protein kinase zyg-8;
DE EC=2.7.11.1;
DE AltName: Full=Doublecortin-like and CAM kinase-like protein;
GN Name=zyg-8 {ECO:0000312|WormBase:Y79H2A.11}; ORFNames=Y79H2A.11;
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:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11702948; DOI=10.1016/s1534-5807(01)00046-6;
RA Gonczy P., Bellanger J.M., Kirkham M., Pozniakowski A., Baumer K.,
RA Phillips J.B., Hyman A.A.;
RT "zyg-8, a gene required for spindle positioning in C. elegans, encodes a
RT doublecortin-related kinase that promotes microtubule assembly.";
RL Dev. Cell 1:363-375(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH TAC-1.
RX PubMed=17666432; DOI=10.1242/jcs.004812;
RA Bellanger J.M., Carter J.C., Phillips J.B., Canard C., Bowerman B.,
RA Gonczy P.;
RT "ZYG-9, TAC-1 and ZYG-8 together ensure correct microtubule function
RT throughout the cell cycle of C. elegans embryos.";
RL J. Cell Sci. 120:2963-2973(2007).
CC -!- FUNCTION: Plays a role in spindle positioning during asymmetric
CC division of one-cell stage embryos. Affects spindle position by
CC promoting microtubule assembly during anaphase.
CC {ECO:0000269|PubMed:11702948, ECO:0000269|PubMed:17666432}.
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=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:O15075};
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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O15075};
CC -!- SUBUNIT: Interacts with tac-1. {ECO:0000269|PubMed:17666432}.
CC -!- INTERACTION:
CC Q95QC4; G5ECG0: tac-1; NbExp=3; IntAct=EBI-331795, EBI-320612;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:11702948}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:11702948}. Note=Enriched at
CC microtubule asters throughout the cell cycle and is present on the
CC spindle during mitosis. {ECO:0000269|PubMed:11702948}.
CC -!- DISRUPTION PHENOTYPE: Maternal-effect embryonic lethal resulting in
CC dramatic spindle positioning defects in one-cell stage embryos.
CC {ECO:0000269|PubMed:11702948}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000255}.
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DR EMBL; AJ319870; CAC67459.1; -; mRNA.
DR EMBL; AL110501; CAB54507.2; -; Genomic_DNA.
DR EMBL; AL033514; CAB54507.2; JOINED; Genomic_DNA.
DR PIR; T27429; T27429.
DR RefSeq; NP_499571.2; NM_067170.5.
DR AlphaFoldDB; Q95QC4; -.
DR SMR; Q95QC4; -.
DR BioGRID; 41819; 40.
DR ComplexPortal; CPX-374; Zyg-8/Tac-1 complex.
DR DIP; DIP-25008N; -.
DR IntAct; Q95QC4; 23.
DR STRING; 6239.Y79H2A.11; -.
DR EPD; Q95QC4; -.
DR PaxDb; Q95QC4; -.
DR PeptideAtlas; Q95QC4; -.
DR EnsemblMetazoa; Y79H2A.11a.1; Y79H2A.11a.1; WBGene00006993.
DR GeneID; 176639; -.
DR KEGG; cel:CELE_Y79H2A.11; -.
DR UCSC; Y79H2A.11; c. elegans.
DR CTD; 176639; -.
DR WormBase; Y79H2A.11; CE31133; WBGene00006993; zyg-8.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG3757; Eukaryota.
DR GeneTree; ENSGT00940000168856; -.
DR HOGENOM; CLU_000288_94_0_1; -.
DR InParanoid; Q95QC4; -.
DR OMA; MPNRNES; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q95QC4; -.
DR SignaLink; Q95QC4; -.
DR PRO; PR:Q95QC4; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006993; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; Q95QC4; baseline and differential.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0072687; C:meiotic spindle; EXP:ComplexPortal.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:WormBase.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:WormBase.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:WormBase.
DR GO; GO:0004672; F:protein kinase activity; ISS:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:WormBase.
DR GO; GO:0007017; P:microtubule-based process; IDA:ComplexPortal.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:WormBase.
DR Gene3D; 3.10.20.230; -; 2.
DR InterPro; IPR003533; Doublecortin_dom.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF03607; DCX; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00537; DCX; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF89837; SSF89837; 2.
DR PROSITE; PS50309; DC; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cytoplasm; Cytoskeleton; Developmental protein;
KW Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..802
FT /note="Serine/threonine-protein kinase zyg-8"
FT /id="PRO_0000400091"
FT DOMAIN 211..298
FT /note="Doublecortin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 340..423
FT /note="Doublecortin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 482..743
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 604
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 488..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 802 AA; 90038 MW; 25326AA5527D60A5 CRC64;
MPQTSAWQLN DTTARPPPPP PPPGSEAGGS DGASMNGANT LPRVSKRVSA AGKTSNIPRF
KRPHLPHSTR PLSAVLTSSS SPVVHRKISP SSSAPSTSSA HRRFSHLPQQ HFHHHIHHNQ
TAVISEETLT TPRASTLNLN QTSVFPTAIS QGSMPNSGTN TAEASMTSSV CAMETEGTNG
DELAESRDMV SEMQRRCRIG PSGYPHLLKA KRLRFYRNGD QYFKGIQYAL QSDRVKSMQP
LMEDLMKTVI CDSTALPHGI RHIFTIDGAQ RITSVDQFED GGGYVCSSTD AFKPVDYSRA
AEPSWRLTLA NRYNRHLETK KLALSVVEPC HENTDFVFPR IIKVIRNGVK PRRISRHLLN
KKTARSFDQV LRDLTFVVKL DSGAIRKLFT LSGRPVLSLQ DFFRDDDVFV AYGGNEKMAA
DDLLVASEEH KSVGSGTSSN MRRTSRRSTM PNRNESLRHD RSGSVIPDQD QQRLPPLLDE
KFQLVRLIGD GNTAVVYEVI DKTNNDDRKA MKVIARENVI GKEHLIEMEL AILQKIDHTF
IVQLYDHWFV DDSYYLSLEL IEMGDLFEHL RIVRRVPERD AVRMMTCLGQ ALEYIHELGI
VHRDVKLENL LIVKDEFGEL GVKLADFGLA AEMPKDFGVL STICGTPTYV APEVLNKTGY
GCKVDIWAAG VILYAILVGF PPFQSSDGSE QDLFSAIMSG EFSFPSPSWD DVSWSVRHLI
MCLIHTDPFH RYSAGELLND EWMVNLGDVD PEYEEWAHRF VQSKMHVEEE QETPYEYYTS
RRTSMDELSE SAAVEFSYSC ES
