FLR4_CAEEL
ID FLR4_CAEEL Reviewed; 570 AA.
AC Q9NLA1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Serine/threonine-protein kinase flr-4;
DE EC=2.7.11.1;
DE AltName: Full=Fluoride-resistant protein 4;
GN Name=flr-4; ORFNames=F09B12.6;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF PRO-223; GLY-248 AND GLY-494.
RC STRAIN=Bristol N2;
RX PubMed=15647385; DOI=10.1091/mbc.e04-04-0273;
RA Take-Uchi M., Kobayashi Y., Kimura K.D., Ishihara T., Katsura I.;
RT "FLR-4, a novel serine/threonine protein kinase, regulates defecation
RT rhythm in Caenorhabditis elegans.";
RL Mol. Biol. Cell 16:1355-1365(2005).
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).
CC -!- FUNCTION: Probable serine-threonine protein kinase involved in the
CC control of defecation rhythms. Required to increase the length of
CC defecation cycle period. Acts in a cell-functional rather than
CC developmental aspect in the regulation of defecation rhythms.
CC {ECO:0000269|PubMed:15647385}.
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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:15647385}; Multi-
CC pass membrane protein {ECO:0000305|PubMed:15647385}.
CC -!- TISSUE SPECIFICITY: Present in the intestinal cells from comma-stage
CC embryos through the adult stage, although the intestinal expression is
CC weaker after the L1 stage. Accumulates at the cell membrane of
CC intestinal cells, especially the lateral membrane intervening the
CC intestinal cells. Also detected in the muscles of the pharyngeal
CC isthmus from the 3-fold embryonic stage, and in a pair of head neurons,
CC which correspond to the AUA neurons, from the late L1 stage (at protein
CC level). {ECO:0000269|PubMed:15647385}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB012700; BAA89795.1; -; mRNA.
DR EMBL; Z83104; CAC35810.1; -; Genomic_DNA.
DR RefSeq; NP_510508.1; NM_078107.3.
DR AlphaFoldDB; Q9NLA1; -.
DR SMR; Q9NLA1; -.
DR STRING; 6239.F09B12.6; -.
DR PaxDb; Q9NLA1; -.
DR EnsemblMetazoa; F09B12.6.1; F09B12.6.1; WBGene00001468.
DR GeneID; 181604; -.
DR KEGG; cel:CELE_F09B12.6; -.
DR UCSC; F09B12.6; c. elegans.
DR CTD; 181604; -.
DR WormBase; F09B12.6; CE26710; WBGene00001468; flr-4.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_478368_0_0_1; -.
DR InParanoid; Q9NLA1; -.
DR OMA; LFSCCMV; -.
DR OrthoDB; 609123at2759; -.
DR PhylomeDB; Q9NLA1; -.
DR PRO; PR:Q9NLA1; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001468; Expressed in embryo and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0030421; P:defecation; 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:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:WormBase.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Biological rhythms; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..570
FT /note="Serine/threonine-protein kinase flr-4"
FT /id="PRO_0000085953"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 40..331
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 338..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 46..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 223
FT /note="P->S: In n2259; induces very short defecation cycle
FT periods."
FT /evidence="ECO:0000269|PubMed:15647385"
FT MUTAGEN 248
FT /note="G->R: In sa201; induces very short defecation cycle
FT periods."
FT /evidence="ECO:0000269|PubMed:15647385"
FT MUTAGEN 494
FT /note="G->R: In u7; weak antimorph that induces very short
FT defecation cycle periods."
FT /evidence="ECO:0000269|PubMed:15647385"
SQ SEQUENCE 570 AA; 64561 MW; 93CC1A5E1C16E994 CRC64;
MPINYNRNAV ELKLSSQLLQ WLDQRLPLGD PMRIPSIDSY KYIQDLGKGR FGTVCKFSNG
NTFETVKKVD LTIFNHWTQS ETKVSNRLDT FLYEFRHLHK VTNDNNRIVN FLGIYADSNQ
MYIMSEYLPR GSVKDLLVKE TLGEDTAIKY LMETVEALDY LHNLSPPVIH RDIKAANLLI
TSNDSIKLAN FGLVRDLAVD GFGIAIASEI TLDFRATLLY VAPEVLSSAL GPGNRNAYEL
PADIWALGCT FIEMLLKRPP HFEYFGHIDE IPKVLLGYAK SEDGKVLPYT SEVLVPSSSN
CVQKIVDLVF IKSPEHRPNT HKLRIQIKKI LDDDSESEEE TDISHPISNS NTDSSTAISH
NHSNDRKVGR AGTCLPIESM EYAAVRKELK KRSKPKSNNI MQIFVASGYY LSRILYFLNI
LTRSICYLLL FLSLGITALG SFLLISYFVV RFVRYLIAIN CNCDLMQPQY LIISGILIVL
MFALLFSCCM VALGEYKFRM ANQTLDGSKF YLPRPQKSAV LCGITVITGK EDAKDTAQNM
EEEIHLTPSV RRNHDDYYYD ESSGPANEEN
