WNK_CAEEL
ID WNK_CAEEL Reviewed; 1850 AA.
AC X5M5N0; H2L282; H2L283; H2L284; H2L285; H2L286; H2L288; H2L289; H2L290;
AC H2L291; H2L292; H2L293; Q18657; Q8I127; X5LPT1; X5LPT5; X5LV40; X5LV44;
AC X5LX64; X5M5N6; X5M8T1; X5M8T5;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Serine/threonine-protein kinase WNK {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:18049475};
DE AltName: Full=Protein kinase with no lysine 1 {ECO:0000305|PubMed:17596296};
GN Name=wnk-1 {ECO:0000312|WormBase:C46C2.1n};
GN ORFNames=C46C2.1 {ECO:0000312|WormBase:C46C2.1n};
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:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, INTERACTION
RP WITH GCK-3, AND DISRUPTION PHENOTYPE.
RX PubMed=17596296; DOI=10.1152/ajpcell.00126.2007;
RA Choe K.P., Strange K.;
RT "Evolutionarily conserved WNK and Ste20 kinases are essential for acute
RT volume recovery and survival after hypertonic shrinkage in Caenorhabditis
RT elegans.";
RL Am. J. Physiol. 293:C915-927(2007).
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH GCK-3, AND MUTAGENESIS OF
RP LYS-346; SER-497; PHE-1133 AND PHE-1222.
RX PubMed=18049475; DOI=10.1038/sj.embor.7401128;
RA Hisamoto N., Moriguchi T., Urushiyama S., Mitani S., Shibuya H.,
RA Matsumoto K.;
RT "Caenorhabditis elegans WNK-STE20 pathway regulates tube formation by
RT modulating ClC channel activity.";
RL EMBO Rep. 9:70-75(2008).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=23076791; DOI=10.1152/ajpcell.00294.2012;
RA Lee E.C., Strange K.;
RT "GCN-2 dependent inhibition of protein synthesis activates osmosensitive
RT gene transcription via WNK and Ste20 kinase signaling.";
RL Am. J. Physiol. 303:C1269-1277(2012).
CC -!- FUNCTION: Serine/threonine-protein kinase which phosphorylates gck-3
CC (PubMed:18049475). Plays a role in osmotic stress responses during
CC which it increases gpdh-1 translation, likely by phosphorylating gck-3
CC (PubMed:23076791). Essential for larval development and the tubular
CC formation of the excretory canals (PubMed:18049475).
CC {ECO:0000269|PubMed:18049475, ECO:0000269|PubMed:23076791}.
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:0000269|PubMed:18049475};
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:0000269|PubMed:18049475};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18049475};
CC -!- SUBUNIT: Interacts with gck-3 (via C-terminus).
CC {ECO:0000269|PubMed:17596296, ECO:0000269|PubMed:18049475}.
CC -!- INTERACTION:
CC X5M5N0; G5EEN4: gck-3; NbExp=3; IntAct=EBI-6540721, EBI-7713242;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=22;
CC Name=n {ECO:0000312|WormBase:C46C2.1n};
CC IsoId=X5M5N0-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C46C2.1a};
CC IsoId=X5M5N0-2; Sequence=VSP_057685, VSP_057686, VSP_057688;
CC Name=b {ECO:0000312|WormBase:C46C2.1b};
CC IsoId=X5M5N0-3; Sequence=VSP_057685, VSP_057686, VSP_057687,
CC VSP_057688;
CC Name=c {ECO:0000312|WormBase:C46C2.1c};
CC IsoId=X5M5N0-4; Sequence=VSP_057684, VSP_057685, VSP_057686,
CC VSP_057688;
CC Name=d {ECO:0000312|WormBase:C46C2.1d};
CC IsoId=X5M5N0-5; Sequence=VSP_057686, VSP_057688;
CC Name=e {ECO:0000312|WormBase:C46C2.1e};
CC IsoId=X5M5N0-6; Sequence=VSP_057686, VSP_057687, VSP_057688;
CC Name=f {ECO:0000312|WormBase:C46C2.1f};
CC IsoId=X5M5N0-7; Sequence=VSP_057684, VSP_057686, VSP_057688;
CC Name=g {ECO:0000312|WormBase:C46C2.1g};
CC IsoId=X5M5N0-8; Sequence=VSP_057685, VSP_057688;
CC Name=h {ECO:0000312|WormBase:C46C2.1h};
CC IsoId=X5M5N0-9; Sequence=VSP_057685, VSP_057687, VSP_057688;
CC Name=i {ECO:0000312|WormBase:C46C2.1i};
CC IsoId=X5M5N0-10; Sequence=VSP_057684, VSP_057685, VSP_057688;
CC Name=j {ECO:0000312|WormBase:C46C2.1j};
CC IsoId=X5M5N0-11; Sequence=VSP_057688;
CC Name=k {ECO:0000312|WormBase:C46C2.1k};
CC IsoId=X5M5N0-12; Sequence=VSP_057687, VSP_057688;
CC Name=l {ECO:0000312|WormBase:C46C2.1l};
CC IsoId=X5M5N0-13; Sequence=VSP_057684, VSP_057688;
CC Name=m {ECO:0000312|WormBase:C46C2.1m};
CC IsoId=X5M5N0-14; Sequence=VSP_057685, VSP_057686;
CC Name=o {ECO:0000312|WormBase:C46C2.1o};
CC IsoId=X5M5N0-15; Sequence=VSP_057687;
CC Name=p {ECO:0000312|WormBase:C46C2.1p};
CC IsoId=X5M5N0-16; Sequence=VSP_057686;
CC Name=q {ECO:0000312|WormBase:C46C2.1q};
CC IsoId=X5M5N0-17; Sequence=VSP_057686, VSP_057687;
CC Name=r {ECO:0000312|WormBase:C46C2.1r};
CC IsoId=X5M5N0-18; Sequence=VSP_057685;
CC Name=s {ECO:0000312|WormBase:C46C2.1s};
CC IsoId=X5M5N0-19; Sequence=VSP_057685, VSP_057687;
CC Name=t {ECO:0000312|WormBase:C46C2.1t};
CC IsoId=X5M5N0-20; Sequence=VSP_057685, VSP_057686, VSP_057687;
CC Name=u {ECO:0000312|WormBase:C46C2.1u};
CC IsoId=X5M5N0-21; Sequence=VSP_057683, VSP_057688;
CC Name=v {ECO:0000312|WormBase:C46C2.1v};
CC IsoId=X5M5N0-22; Sequence=VSP_057683;
CC -!- TISSUE SPECIFICITY: Expressed in pharynx, nervous system, hypodermis,
CC spermatheca, excretory cell and canal and body wall muscles.
CC {ECO:0000269|PubMed:17596296}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes impaired survival
CC and slower volume recovery upon hypertonic stress.
CC {ECO:0000269|PubMed:17596296}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. WNK subfamily. {ECO:0000305}.
CC -!- CAUTION: Was named WNK/'with no lysine(K)' because key residues for
CC catalysis, including the lysine involved in ATP binding, are either not
CC conserved or differ compared to the residues described in other kinase
CC family proteins. {ECO:0000250|UniProtKB:Q9H4A3}.
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DR EMBL; BX284604; CAA92591.3; -; Genomic_DNA.
DR EMBL; BX284604; CAD59142.2; -; Genomic_DNA.
DR EMBL; BX284604; CCE71523.1; -; Genomic_DNA.
DR EMBL; BX284604; CCE71524.1; -; Genomic_DNA.
DR EMBL; BX284604; CCE71525.1; -; Genomic_DNA.
DR EMBL; BX284604; CCE71526.1; -; Genomic_DNA.
DR EMBL; BX284604; CCE71527.1; -; Genomic_DNA.
DR EMBL; BX284604; CCE71529.1; -; Genomic_DNA.
DR EMBL; BX284604; CCE71530.1; -; Genomic_DNA.
DR EMBL; BX284604; CCE71531.1; -; Genomic_DNA.
DR EMBL; BX284604; CCE71532.1; -; Genomic_DNA.
DR EMBL; BX284604; CCE71533.1; -; Genomic_DNA.
DR EMBL; BX284604; CCE71534.1; -; Genomic_DNA.
DR EMBL; BX284604; CDO41073.1; -; Genomic_DNA.
DR EMBL; BX284604; CDO41074.1; -; Genomic_DNA.
DR EMBL; BX284604; CDO41075.1; -; Genomic_DNA.
DR EMBL; BX284604; CDO41076.1; -; Genomic_DNA.
DR EMBL; BX284604; CDO41077.1; -; Genomic_DNA.
DR EMBL; BX284604; CDO41078.1; -; Genomic_DNA.
DR EMBL; BX284604; CDO41079.1; -; Genomic_DNA.
DR EMBL; BX284604; CDO41080.1; -; Genomic_DNA.
DR EMBL; BX284604; CDO41081.1; -; Genomic_DNA.
DR PIR; T19964; T19964.
DR RefSeq; NP_001255367.1; NM_001268438.1.
DR RefSeq; NP_001255368.1; NM_001268439.1. [X5M5N0-11]
DR RefSeq; NP_001255369.1; NM_001268440.1. [X5M5N0-12]
DR RefSeq; NP_001255370.1; NM_001268441.1. [X5M5N0-5]
DR RefSeq; NP_001255371.1; NM_001268442.1. [X5M5N0-6]
DR RefSeq; NP_001255372.1; NM_001268443.1. [X5M5N0-8]
DR RefSeq; NP_001255373.1; NM_001268444.1. [X5M5N0-9]
DR RefSeq; NP_001255374.1; NM_001268445.1. [X5M5N0-13]
DR RefSeq; NP_001255375.1; NM_001268446.1. [X5M5N0-7]
DR RefSeq; NP_001255376.1; NM_001268447.1. [X5M5N0-10]
DR RefSeq; NP_001255377.1; NM_001268448.1. [X5M5N0-4]
DR RefSeq; NP_001294032.1; NM_001307103.1. [X5M5N0-1]
DR RefSeq; NP_001294033.1; NM_001307104.1. [X5M5N0-15]
DR RefSeq; NP_001294034.1; NM_001307105.1.
DR RefSeq; NP_001294035.1; NM_001307106.1. [X5M5N0-17]
DR RefSeq; NP_001294036.1; NM_001307107.1. [X5M5N0-18]
DR RefSeq; NP_001294037.1; NM_001307108.1. [X5M5N0-19]
DR RefSeq; NP_001294038.1; NM_001307109.1. [X5M5N0-20]
DR RefSeq; NP_001294039.1; NM_001307110.1. [X5M5N0-21]
DR RefSeq; NP_001294040.1; NM_001307111.1. [X5M5N0-22]
DR RefSeq; NP_501603.3; NM_069202.5. [X5M5N0-2]
DR RefSeq; NP_872075.2; NM_182275.4. [X5M5N0-3]
DR AlphaFoldDB; X5M5N0; -.
DR SMR; X5M5N0; -.
DR IntAct; X5M5N0; 2.
DR MINT; X5M5N0; -.
DR STRING; 6239.C46C2.1m; -.
DR EPD; X5M5N0; -.
DR PaxDb; X5M5N0; -.
DR PeptideAtlas; X5M5N0; -.
DR EnsemblMetazoa; C46C2.1a.1; C46C2.1a.1; WBGene00006941. [X5M5N0-2]
DR EnsemblMetazoa; C46C2.1b.1; C46C2.1b.1; WBGene00006941. [X5M5N0-3]
DR EnsemblMetazoa; C46C2.1c.1; C46C2.1c.1; WBGene00006941. [X5M5N0-4]
DR EnsemblMetazoa; C46C2.1d.1; C46C2.1d.1; WBGene00006941. [X5M5N0-5]
DR EnsemblMetazoa; C46C2.1e.1; C46C2.1e.1; WBGene00006941. [X5M5N0-6]
DR EnsemblMetazoa; C46C2.1f.1; C46C2.1f.1; WBGene00006941. [X5M5N0-7]
DR EnsemblMetazoa; C46C2.1g.1; C46C2.1g.1; WBGene00006941. [X5M5N0-8]
DR EnsemblMetazoa; C46C2.1h.1; C46C2.1h.1; WBGene00006941. [X5M5N0-9]
DR EnsemblMetazoa; C46C2.1i.1; C46C2.1i.1; WBGene00006941. [X5M5N0-10]
DR EnsemblMetazoa; C46C2.1j.1; C46C2.1j.1; WBGene00006941. [X5M5N0-11]
DR EnsemblMetazoa; C46C2.1k.1; C46C2.1k.1; WBGene00006941. [X5M5N0-12]
DR EnsemblMetazoa; C46C2.1l.1; C46C2.1l.1; WBGene00006941. [X5M5N0-13]
DR EnsemblMetazoa; C46C2.1m.1; C46C2.1m.1; WBGene00006941. [X5M5N0-14]
DR EnsemblMetazoa; C46C2.1n.1; C46C2.1n.1; WBGene00006941. [X5M5N0-1]
DR EnsemblMetazoa; C46C2.1o.1; C46C2.1o.1; WBGene00006941. [X5M5N0-15]
DR EnsemblMetazoa; C46C2.1p.1; C46C2.1p.1; WBGene00006941. [X5M5N0-16]
DR EnsemblMetazoa; C46C2.1q.1; C46C2.1q.1; WBGene00006941. [X5M5N0-17]
DR EnsemblMetazoa; C46C2.1r.1; C46C2.1r.1; WBGene00006941. [X5M5N0-18]
DR EnsemblMetazoa; C46C2.1s.1; C46C2.1s.1; WBGene00006941. [X5M5N0-19]
DR EnsemblMetazoa; C46C2.1t.1; C46C2.1t.1; WBGene00006941. [X5M5N0-20]
DR EnsemblMetazoa; C46C2.1u.1; C46C2.1u.1; WBGene00006941. [X5M5N0-21]
DR EnsemblMetazoa; C46C2.1v.1; C46C2.1v.1; WBGene00006941. [X5M5N0-22]
DR GeneID; 177743; -.
DR KEGG; cel:CELE_C46C2.1; -.
DR UCSC; C46C2.1a; c. elegans.
DR CTD; 177743; -.
DR WormBase; C46C2.1a; CE37331; WBGene00006941; wnk-1. [X5M5N0-2]
DR WormBase; C46C2.1b; CE37332; WBGene00006941; wnk-1. [X5M5N0-3]
DR WormBase; C46C2.1c; CE46706; WBGene00006941; wnk-1. [X5M5N0-4]
DR WormBase; C46C2.1d; CE46603; WBGene00006941; wnk-1. [X5M5N0-5]
DR WormBase; C46C2.1e; CE46553; WBGene00006941; wnk-1. [X5M5N0-6]
DR WormBase; C46C2.1f; CE46627; WBGene00006941; wnk-1. [X5M5N0-7]
DR WormBase; C46C2.1g; CE46722; WBGene00006941; wnk-1. [X5M5N0-8]
DR WormBase; C46C2.1h; CE46797; WBGene00006941; wnk-1. [X5M5N0-9]
DR WormBase; C46C2.1i; CE46749; WBGene00006941; wnk-1. [X5M5N0-10]
DR WormBase; C46C2.1j; CE46831; WBGene00006941; wnk-1. [X5M5N0-11]
DR WormBase; C46C2.1k; CE46763; WBGene00006941; wnk-1. [X5M5N0-12]
DR WormBase; C46C2.1l; CE46557; WBGene00006941; wnk-1. [X5M5N0-13]
DR WormBase; C46C2.1m; CE46636; WBGene00006941; wnk-1. [X5M5N0-14]
DR WormBase; C46C2.1n; CE49690; WBGene00006941; wnk-1. [X5M5N0-1]
DR WormBase; C46C2.1o; CE49733; WBGene00006941; wnk-1. [X5M5N0-15]
DR WormBase; C46C2.1p; CE49626; WBGene00006941; wnk-1. [X5M5N0-16]
DR WormBase; C46C2.1q; CE49684; WBGene00006941; wnk-1. [X5M5N0-17]
DR WormBase; C46C2.1r; CE49717; WBGene00006941; wnk-1. [X5M5N0-18]
DR WormBase; C46C2.1s; CE49622; WBGene00006941; wnk-1. [X5M5N0-19]
DR WormBase; C46C2.1t; CE49653; WBGene00006941; wnk-1. [X5M5N0-20]
DR WormBase; C46C2.1u; CE49693; WBGene00006941; wnk-1. [X5M5N0-21]
DR WormBase; C46C2.1v; CE49732; WBGene00006941; wnk-1. [X5M5N0-22]
DR eggNOG; KOG0584; Eukaryota.
DR GeneTree; ENSGT01030000239929; -.
DR HOGENOM; CLU_001879_1_0_1; -.
DR OMA; MREICSH; -.
DR OrthoDB; 695382at2759; -.
DR Reactome; R-CEL-2672351; Stimuli-sensing channels.
DR PRO; PR:X5M5N0; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006941; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019869; F:chloride channel inhibitor activity; IBA:GO_Central.
DR GO; GO:0019870; F:potassium channel inhibitor activity; IBA:GO_Central.
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:0006972; P:hyperosmotic response; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; IMP:GO_Central.
DR GO; GO:0010766; P:negative regulation of sodium ion transport; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:GO_Central.
DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
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; Coiled coil; Developmental protein;
KW Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1850
FT /note="Serine/threonine-protein kinase WNK"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433218"
FT DOMAIN 334..596
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1721..1740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 693..749
FT /evidence="ECO:0000255"
FT COMPBIAS 10..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..769
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 483
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT BINDING 416..419
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT BINDING 466
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT VAR_SEQ 1..1650
FT /note="Missing (in isoform u and isoform v)"
FT /evidence="ECO:0000305"
FT /id="VSP_057683"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform c, isoform f, isoform i and
FT isoform l)"
FT /evidence="ECO:0000305"
FT /id="VSP_057684"
FT VAR_SEQ 82..83
FT /note="Missing (in isoform a, isoform b, isoform c, isoform
FT g, isoform h, isoform i, isoform m, isoform r, isoform s
FT and isoform t)"
FT /evidence="ECO:0000305"
FT /id="VSP_057685"
FT VAR_SEQ 1341..1343
FT /note="Missing (in isoform a, isoform b, isoform c, isoform
FT d, isoform e, isoform f, isoform m, isoform p, isoform q
FT and isoform t)"
FT /evidence="ECO:0000305"
FT /id="VSP_057686"
FT VAR_SEQ 1488..1648
FT /note="Missing (in isoform b, isoform e, isoform h, isoform
FT k, isoform o, isoform q, isoform s and isoform t)"
FT /evidence="ECO:0000305"
FT /id="VSP_057687"
FT VAR_SEQ 1735..1850
FT /note="IPDNEGQHHCNSFRCIGDPNDNVSIVNQIKQRLGIIPSSRQSVRSATSSSPS
FT TPPSSSSAPPKSLSSPTKSYVSHCSLSIGYGSTASSEQQQREPSPSATTSSFLSDPATG
FT VIENV -> TTKVNTTVIPSDVLATRMTMSQSSTKSSNVSVSSRHRDNQSAPPRHHHHQ
FT PHPPHHPHLQNHYHPPQNHTSATAPCPSAMVQLQAVSNNNVNPLHQPPHPVSSQIPPQA
FT (in isoform a, isoform b, isoform c, isoform d, isoform e,
FT isoform f, isoform g, isoform h, isoform i, isoform j,
FT isoform k, isoform l and isoform u)"
FT /evidence="ECO:0000305"
FT /id="VSP_057688"
FT MUTAGEN 346
FT /note="K->M: No catalytic activity. Arrest at L2 larval
FT stage and abnormal formation of the excretory canal."
FT /evidence="ECO:0000269|PubMed:18049475"
FT MUTAGEN 497
FT /note="S->A: No defect in the formation of the excretory
FT canal."
FT /evidence="ECO:0000269|PubMed:18049475"
FT MUTAGEN 1133
FT /note="F->A: Severe loss of interaction with gck-3 and
FT abnormal formation of the excretory canal; when associated
FT with A-1222."
FT /evidence="ECO:0000269|PubMed:18049475"
FT MUTAGEN 1222
FT /note="F->A: Severe loss of interaction with gck-3 and
FT abnormal formation of the excretory canal; when associated
FT with A-1133."
FT /evidence="ECO:0000269|PubMed:18049475"
SQ SEQUENCE 1850 AA; 199214 MW; 5345695376E5A527 CRC64;
MPDSITNGGR PPAPPSSVSS TTASTTGNFG TRRRLVNRIK KVDELHPAQE NPTMGSHWLS
EQERSRLEAV QQDWRRTRPM KFQWTSKKRP DDPTTSSPST VSISNALENS TPSLNNVSSI
TNSSSPFSLS SAATSTASAI IPFTSNVATN HPHLNHHVSR IPQAIVTGGT NGSLPPLLIS
PTSAAAATPL ISGKAGPMSP STGSPINVAA TVLQNAVSSP QHSIFDRSRL NKIPPNTSLA
SSSSPSDAAN NDKPIQQRHS ILSNVRTLTQ AMVNDGPRTL TGDDMDKMVS EEERARKEQE
KREEEEKAAR RIDVEDDFDA QEKPIDKSKN GRFLKFDEEL GRGSFKTVFR GLDTETGVAV
AWCELQESKL NKTERQRFRE EAEMLKDLQH PNIVRFYDYW ESADLCGKRK YIVLVTELMT
SGTLKMYLKR FKRINIKVLK SWCRQILKGL SFLHTRNPPV IHRDLKCDNI FITGTTGSVK
IGDLGLATLK NKSFAKSVIG TPEFMAPEMY EEMYDESVDV YAFGMCLLEM VTGEYPYSEC
MNPATIYRKV ISGVKPECFS RIPAQYPEIR EIIDRCIRVR REERSTVKQL LVDDFFTPED
LIGIRVEIKN RDADLNDLNV EIQMQLRVYD EKKRKQYRFK ENEGLQFAFD IENDSPDEVV
QQMIEQQHIP DEDTRMITKL IKDKVDAFRR DRDHRLLEIK RAKEEEERIR EEAEIKEELR
LRAEAKEKEK ERLEKERLEK KAAAAAAANP NPTPIPPTPA TPHSSAQQQP IPPPLSTQTS
AEIQQSAQQP SVPVTMIANI PAMSPTSAQP QPVLSPTSAA VPVPTTMIHV PKPSEIPVQN
VATTAAPVAA NNVPPSPAPF KTEDIQTPTL AQNTVPRTIS TDASGLVINT PASIASPSPA
PSATDVASTT APVTPAPTPT TTTDGGAAAA STTTENKEEK RKSNKRKVVM EILGCDESRN
FALVSCRLDT SHKSVTFQFA PGTDKPCTIA TKLLAEDCLL KVHVHIVEAQ LGEVIQLINS
DGKKGVGTKL ATVLDPNSTE PPTITAVMPK DSSAATASNT KPKIEIEKTP PTRDASQEPN
NVQVTNVRKV SQESNAESVQ SIPRPGGIIV MSPTNQTDSA PPPTGAAAKP SRFQVTKSAD
PIATPISSSI STATVIPIVA ATPTNITSEP VIVQPITAQV ITHLATPSPV SHSLSSNSSP
SATTHSNMSS IQSTTSVPGR RFTVQPVSQA ESGISSSIST PHPEPTPAIT SCPPPVPSVP
PVVSNGTLNL EVAPKQTPSA TNQNVDTQHS SSTASTATLV SETPATVHVT PISVPAPVQE
PLVIDHHSDV LTQLDSELRK CFQVSGVSHS ASPSTVVESL TSMTPQTIPL ACQTVPASIG
QAPAVIAAAH AASLIPNASV PQSPSRLDAE TGLAGLHEKL EALKMEQDRR EDMGDDAIGT
TTTDGKDEIP IDTLKGLAEA LGKVIHADGR ETTPMPPDHP DLTDASTQQL ISPSNPDVLT
TMSSAVEGSA SSTMIEDIDA STSAVDASMM NSMPPGAQNS TDQIPAAMTL SMDQECAQSM
TSSITRNTTG TKLATFENLE TALSSTLGTH IRQPNAPSSR DETTAPMTPS FTNERIGGGG
GGGATSFSIG TPPSHSPFPV SECDYDLKGQ MDLESEDPEV IQMIVRHRME QHKLLEKQRV
EIERLRSKIR VPRATSVNPE MIGDDEADTT LTALQSALGN ASLSLPASPP PNTEIPDNEG
QHHCNSFRCI GDPNDNVSIV NQIKQRLGII PSSRQSVRSA TSSSPSTPPS SSSAPPKSLS
SPTKSYVSHC SLSIGYGSTA SSEQQQREPS PSATTSSFLS DPATGVIENV
