SULU_CAEEL
ID SULU_CAEEL Reviewed; 982 AA.
AC P46549; Q8MPX1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/threonine-protein kinase SULU;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q0KHQ5};
DE AltName: Full=Protein kinase 18;
GN Name=kin-18; Synonyms=sulu; ORFNames=T17E9.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
RA Cope M.J.T.V., Kendrick-Jones A.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11733138; DOI=10.1016/s0378-1119(01)00752-1;
RA Berman K.S., Hutchison M., Avery L., Cobb M.H.;
RT "kin-18, a C. elegans protein kinase involved in feeding.";
RL Gene 279:137-147(2001).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23064028; DOI=10.1016/j.ydbio.2012.10.001;
RA Spiga F.M., Prouteau M., Gotta M.;
RT "The TAO kinase KIN-18 regulates contractility and establishment of
RT polarity in the C. elegans embryo.";
RL Dev. Biol. 373:26-38(2013).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF 47-ALA--THR-642.
RX PubMed=26510792; DOI=10.1534/genetics.115.177295;
RA Yin Y., Donlevy S., Smolikove S.;
RT "Coordination of Recombination with Meiotic Progression in the
RT Caenorhabditis elegans Germline by KIN-18, a TAO Kinase That Regulates the
RT Timing of MPK-1 Signaling.";
RL Genetics 202:45-59(2016).
CC -!- FUNCTION: Acts as a negative regulator of cortical contractions during
CC early embryonic cell division, possibly by regulating rho-1-dependent
CC actomyosin contractility (PubMed:23064028). Plays a role in polarity
CC establishment in early embryos by regulating the size of the anterior
CC and posterior cortex in the first asymmetric cell division
CC (PubMed:23064028). Might play a role in cell cycle progression
CC (PubMed:23064028). In the germline, involved in the regulation of
CC meiotic progression during oogenesis, possibly by modulating the timing
CC of mpk-1 activation (PubMed:26510792). Plays a role in meiotic
CC recombination events (PubMed:26510792). Involved in pharyngeal pumping
CC (PubMed:11733138). {ECO:0000269|PubMed:11733138,
CC ECO:0000269|PubMed:23064028, ECO:0000269|PubMed:26510792}.
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:Q0KHQ5};
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:Q0KHQ5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q0KHQ5};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23064028}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:23064028}. Note=Localized to the anterior cortex in
CC embryos; localization to the anterior cortex depends on par-3 and rho-
CC 1. {ECO:0000269|PubMed:23064028}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P46549-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P46549-2; Sequence=VSP_020524, VSP_020525;
CC -!- TISSUE SPECIFICITY: Expressed in the pharynx, including the pharyngeal
CC muscle of the metacorpus, the isthmus, and the terminal bulb; in the
CC intestine, including the pharyngeointestinal valve between the pharynx
CC and the intestine, a structure near the anus likely to be the anal
CC sphincter and the excretory cell and in several ring neurons.
CC {ECO:0000269|PubMed:11733138}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis (PubMed:23064028).
CC Expressed in adults (PubMed:11733138). {ECO:0000269|PubMed:11733138,
CC ECO:0000269|PubMed:23064028}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown leads to embryonic
CC lethality (PubMed:23064028). Increased and prolonged cortical
CC contractility leading to a more persistent pseudocleavage in surviving
CC embryos (PubMed:23064028). Decrease in rho-1 anterior cortex
CC localization and increase in posterior cortex localization, leading to
CC a loss of asymmetric rho-1 cortex localization during early embryonic
CC cell division (PubMed:23064028). Increased cortical nmy-2 network
CC between the foci, suggesting that the enhanced contractions are due to
CC increased actomyosin contractility (PubMed:23064028). Reduction in the
CC size of the anterior cortex and increase in the size of the posterior
CC cortex during polarity establishment in the early embryo
CC (PubMed:23064028). Leads to a delay in embryonic cell cycle progression
CC (PubMed:23064028). Double RNAi-mediated knockdown with rho-1 results in
CC loss of cortical contractility (PubMed:23064028).
CC {ECO:0000269|PubMed:23064028}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; U32275; AAA75370.1; -; mRNA.
DR EMBL; FO080363; CCD63180.1; -; Genomic_DNA.
DR EMBL; FO080363; CCD63181.1; -; Genomic_DNA.
DR PIR; T18576; T18576.
DR RefSeq; NP_001022767.1; NM_001027596.2. [P46549-1]
DR RefSeq; NP_741172.2; NM_171151.3.
DR AlphaFoldDB; P46549; -.
DR SMR; P46549; -.
DR BioGRID; 41083; 12.
DR STRING; 6239.T17E9.1a.2; -.
DR ChEMBL; CHEMBL5197; -.
DR iPTMnet; P46549; -.
DR EPD; P46549; -.
DR PaxDb; P46549; -.
DR PeptideAtlas; P46549; -.
DR EnsemblMetazoa; T17E9.1a.1; T17E9.1a.1; WBGene00002201. [P46549-1]
DR EnsemblMetazoa; T17E9.1b.1; T17E9.1b.1; WBGene00002201.
DR GeneID; 175862; -.
DR KEGG; cel:CELE_T17E9.1; -.
DR UCSC; T17E9.1a; c. elegans. [P46549-1]
DR CTD; 175862; -.
DR WormBase; T17E9.1a; CE01405; WBGene00002201; kin-18. [P46549-1]
DR WormBase; T17E9.1b; CE32936; WBGene00002201; kin-18. [P46549-2]
DR eggNOG; KOG0577; Eukaryota.
DR GeneTree; ENSGT00940000168060; -.
DR HOGENOM; CLU_000288_2_2_1; -.
DR InParanoid; P46549; -.
DR OMA; YYARCLV; -.
DR OrthoDB; 617606at2759; -.
DR PhylomeDB; P46549; -.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR PRO; PR:P46549; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002201; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0007631; P:feeding behavior; IMP:WormBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:WormBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0060631; P:regulation of meiosis I; IMP:WormBase.
DR GO; GO:0043051; P:regulation of pharyngeal pumping; IMP:WormBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..982
FT /note="Serine/threonine-protein kinase SULU"
FT /id="PRO_0000086726"
FT DOMAIN 30..289
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 331..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 36..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 351..353
FT /note="ANS -> NHG (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020524"
FT VAR_SEQ 354..982
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020525"
FT MUTAGEN 47..642
FT /note="Missing: In ok395; accelerated prophase I
FT progression, aberrant oocyte development and ectopic
FT apoptosis in the germline. Shorter gonads, reduction in
FT nuclei, increase in mitotic index, decrease in early
FT meiotic nuclei and sterility. Increase in and premature
FT chromosomal loading of rad-51 and cosa-1 during meiosis.
FT Increased and ectopic phosphorylation levels of mapk-1
FT (isoform a)."
FT /evidence="ECO:0000269|PubMed:26510792"
SQ SEQUENCE 982 AA; 112871 MW; 745CE1E2F890977D CRC64;
MAPAVLQKPG VIKDPSIAAL FSNKDPEQRY QDLREIGHGS FGAVYFAYDK KNEQTVAIKK
MNFSGKQAVE KWNDILKEVS FLNTVVHPHI VDYKACFLKD TTCWLVMEYC IGSAADIVDV
LRKGMREVEI AAICSQTLDA LRYLHSLKRI HRDIKAGNIL LSDHAIVKLA DFGSASLVDP
AQTFIGTPFF MAPEVILAMD EGHYTDRADI WSLGITCIEL AERRPPLFSM NAMSALYHIA
QNDPPTLSPI DTSEQPEWSL EFVQFIDKCL RKPAEERMSA EECFRHPFIQ RSRPSDTIQE
LIQRTKNMVL ELDNFQYKKM RKLMYLDETE GKEGSEGNGA SDDLDFHGNE ANSIGRAGDS
ASSRSASLTS FRSMQSSGGA GLLVSTNTTG AMDNVHGSSG YGNGSSSTTS SARRRPPIPS
QMLSSTSTSG VGTMPSHGSV GASITAIAVN PTPSPSEPIP TSQPTSKSES SSILETAHDD
PLDTSIRAPV KDLHMPHRAV KERIATLQNH KFATLRSQRI INQEQEEYTK ENNMYEQMSK
YKHLRQAHHK ELQQFEERCA LDREQLRVKM DRELEQLTTT YSKEKMRVRC SQNNELDKRK
KDIEDGEKKM KKTKNSQNQQ QMKLYSAQQL KEYKYNKEAQ KTRLRSLNMP RSTYENAMKE
VKADLNRVKD ARENDFDEKL RAELEDEIVR YRRQQLSNLH QLEEQLDDED VNVQERQMDT
RHGLLSKQHE MTRDLEIQHL NELHAMKKRH LETQHEAESA SQNEYTQRQQ DELRKKHAMQ
SRQQPRDLKI QEAQIRKQYR QVVKTQTRQF KLYLTQMVQV VPKDEQKELT SRLKQDQMQK
VALLASQYES QIKKMVQDKT VKLESWQEDE QRVLSEKLEK ELEELIAYQK KTRATLEEQI
KKERTALEER IGTRRAMLEQ KIIEEREQMG EMRRLKKEQI RDRHSQERHR LENHFVRTGS
TSRSSGGIAP GVGNSSSIQM AM
