WARTS_CAEEL
ID WARTS_CAEEL Reviewed; 908 AA.
AC O45797;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Serine/threonine-protein kinase WARTS homolog {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:O95835};
DE AltName: Full=LATS kinase homolog {ECO:0000305|PubMed:19605499};
GN Name=wts-1 {ECO:0000312|WormBase:T20F10.1};
GN ORFNames=T20F10.1 {ECO:0000312|WormBase:T20F10.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19737560; DOI=10.1016/j.febslet.2009.09.002;
RA Cai Q., Wang W., Gao Y., Yang Y., Zhu Z., Fan Q.;
RT "Ce-wts-1 plays important roles in Caenorhabditis elegans development.";
RL FEBS Lett. 583:3158-3164(2009).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=19605499; DOI=10.1242/dev.035485;
RA Kang J., Shin D., Yu J.R., Lee J.;
RT "Lats kinase is involved in the intestinal apical membrane integrity in the
RT nematode Caenorhabditis elegans.";
RL Development 136:2705-2715(2009).
RN [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH YAP-1.
RX PubMed=23396260; DOI=10.1016/j.yexcr.2013.01.020;
RA Iwasa H., Maimaiti S., Kuroyanagi H., Kawano S., Inami K., Timalsina S.,
RA Ikeda M., Nakagawa K., Hata Y.;
RT "Yes-associated protein homolog, YAP-1, is involved in the thermotolerance
RT and aging in the nematode Caenorhabditis elegans.";
RL Exp. Cell Res. 319:931-945(2013).
CC -!- FUNCTION: Phosphorylates yap-1 which may negatively regulate yap-1
CC nuclear localization (PubMed:23396260). Plays an essential role in
CC larval development (PubMed:19737560, PubMed:19605499). Regulates
CC growth, the formation of gut granules, lifespan and cell and body sizes
CC probably in synergy with the TGF-beta sma/mab pathway
CC (PubMed:19737560). Does not appear to regulate apoptosis and
CC proliferation (PubMed:19605499). In addition, may synergize with the
CC TGF-beta daf-7 dauer pathway to regulate entry into the dauer stage
CC (PubMed:19737560). Maintains the cellular integrity of intestinal cells
CC by regulating the localization of apical actin and junctional proteins
CC (PubMed:19605499). {ECO:0000269|PubMed:19605499,
CC ECO:0000269|PubMed:19737560, ECO:0000269|PubMed:23396260}.
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:O95835};
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:O95835};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O95835};
CC -!- SUBUNIT: Interacts (via N-terminus) with yap-1 (via WW domain).
CC {ECO:0000269|PubMed:23396260}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19605499,
CC ECO:0000269|PubMed:19737560}. Apical cell membrane
CC {ECO:0000269|PubMed:19605499, ECO:0000269|PubMed:19737560}. Note=In
CC epithelial cells, localized near the plasma membrane. In intestinal
CC cells, localized in the subapical membrane region (PubMed:19605499,
CC PubMed:19737560). Membrane localization starts in the late embryo
CC (PubMed:19605499). {ECO:0000269|PubMed:19605499,
CC ECO:0000269|PubMed:19737560}.
CC -!- TISSUE SPECIFICITY: Expressed in muscles and epithelial tissues
CC including pharynx, intestine and hypodermis (PubMed:19605499).
CC Expressed in vulval and spermathecal seam cells (PubMed:19737560).
CC {ECO:0000269|PubMed:19605499, ECO:0000269|PubMed:19737560}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the embryonic comma stage and during
CC all the larval stages and in adults. {ECO:0000269|PubMed:19605499}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in larval
CC lethality in 50 percent of the animals (PubMed:19737560,
CC PubMed:19605499). Surviving knockdown animals have several defects
CC including a slower growth and a partial distortion of the pharynx. In
CC surviving L3 animals seam cells are 30 percent smaller
CC (PubMed:19737560). {ECO:0000269|PubMed:19605499,
CC ECO:0000269|PubMed:19737560}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; Z81594; CAB04745.1; -; Genomic_DNA.
DR PIR; T25035; T25035.
DR RefSeq; NP_492699.1; NM_060298.4.
DR AlphaFoldDB; O45797; -.
DR SMR; O45797; -.
DR DIP; DIP-26953N; -.
DR IntAct; O45797; 2.
DR STRING; 6239.T20F10.1; -.
DR EPD; O45797; -.
DR PaxDb; O45797; -.
DR PeptideAtlas; O45797; -.
DR EnsemblMetazoa; T20F10.1.1; T20F10.1.1; WBGene00007047.
DR GeneID; 172896; -.
DR KEGG; cel:CELE_T20F10.1; -.
DR UCSC; T20F10.1; c. elegans.
DR CTD; 172896; -.
DR WormBase; T20F10.1; CE13844; WBGene00007047; wts-1.
DR eggNOG; KOG0608; Eukaryota.
DR GeneTree; ENSGT00940000170511; -.
DR HOGENOM; CLU_014539_0_0_1; -.
DR InParanoid; O45797; -.
DR OMA; YHTSMDK; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; O45797; -.
DR Reactome; R-CEL-2028269; Signaling by Hippo.
DR PRO; PR:O45797; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00007047; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IMP: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:0001223; F:transcription coactivator binding; IPI:WormBase.
DR GO; GO:0045176; P:apical protein localization; IMP:WormBase.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0035329; P:hippo signaling; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0061067; P:negative regulation of dauer larval development; IGI:UniProtKB.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0060465; P:pharynx development; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:UniProtKB.
DR GO; GO:0048621; P:post-embryonic digestive tract morphogenesis; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IMP:WormBase.
DR GO; GO:0046620; P:regulation of organ growth; IBA:GO_Central.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR028742; LATS2.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF149; PTHR24356:SF149; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Coiled coil; Cytoplasm; Developmental protein;
KW Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..908
FT /note="Serine/threonine-protein kinase WARTS homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000432473"
FT DOMAIN 502..807
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 808..874
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..70
FT /evidence="ECO:0000255"
FT COILED 439..470
FT /evidence="ECO:0000255"
FT COMPBIAS 115..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 625
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 508..516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 908 AA; 102792 MW; 8B878BC297D00B0C CRC64;
MRPAAPGTTP NGASSDIRHQ RGVAPIPFGS TNSAIDAHHN SEIRVGRHRA KLDEIRESLK
AYEHEAGLLS SHVALGSLAT PSSSSVSHSD ITNDNAEVMN FSSSSSNAAA TTTTVSSAAV
SNSNSFRTEG GGHKMRITPM PQRHLMMDTG ANETVFRSGK EMIRNGNPST TISSTPSTTT
EESIRIHPAG YRYDMPTPAY HMNNNAPQYS PGYSRPPPPA YDSSPVNTRM TPVATDNYRT
HLHMKVHPVV KAPPPNPTML NHNKNMAPPP PPPAKSTISI ETMSEERKAD NIQRLYHTSM
DKKTASSVVS INVASPHTTK VNVGDSPLPS KSFIIGPRYT ADVDRKNFVN YKDELRPDPR
LIPSTSDANH EDFRPILFKP RNLEITMKSR AQPPPPQYNQ PSEPPPKRVS SPIDRTLLEP
YIKNTRRVQP CKPNMLRFYM EQHVERLLQQ YKEREKRMKQ LEKEMVSAQL PDIMRNKMLG
LLQQKESKYT RLRRQKMSKS HFTVISHIGV GAFGKVSLVR KNDTRKVYAM KSLEKADVIM
KQQAAHVKAE RDILAEADSP WIVRLFFSFQ DDACLYFIME YVPGGDMMTL LIQKGIFEED
LARFYIAELA CAIEYVHNVG FIHRDLKPDN ILIDQHGHIK LTDFGLCTGL RWTHDRRYYG
PENDHHRVDS FSLPPEVAAI DKSVKVLNVR QQTRRITAHS LVGTGNYMAP EVIAKTGHNQ
SCDWWSTGVI LYEMVFGRVP FHDDTPGGTQ HRIKNWRNFL DFTYCGNLSK ECLMMIQQLI
CDASSRLGSH GKDVAERTAQ VKNHPWFRGI DWVNLRKLRA DYIYIPRVTH DEDTSNFETF
QDNDRADKPN VRGLHNPAFY EFTYRHFFDT DSVGCPSLRP SRRRSLRPLL ENGTFNESVS
EEDSSSHI
