RYK_CAEEL
ID RYK_CAEEL Reviewed; 583 AA.
AC G5EGT9;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Inactive tyrosine-protein kinase RYK {ECO:0000250|UniProtKB:P34925};
DE AltName: Full=Abnormal cell lineage protein 18 {ECO:0000312|WormBase:C16B8.1};
DE Flags: Precursor;
GN Name=lin-18 {ECO:0000312|WormBase:C16B8.1};
GN Synonyms=ryk {ECO:0000312|EMBL:AAD24877.1};
GN ORFNames=C16B8.1 {ECO:0000312|WormBase:C16B8.1};
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|EMBL:AAD24877.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAD24877.1};
RX PubMed=10066802; DOI=10.1074/jbc.274.11.7379;
RA Halford M.M., Oates A.C., Hibbs M.L., Wilks A.F., Stacker S.A.;
RT "Genomic structure and expression of the mouse growth factor receptor
RT related to tyrosine kinases (Ryk).";
RL J. Biol. Chem. 274:7379-7390(1999).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF 38-GLU--LEU-39.
RX PubMed=15369677; DOI=10.1016/j.cell.2004.09.001;
RA Inoue T., Oz H.S., Wiland D., Gharib S., Deshpande R., Hill R.J.,
RA Katz W.S., Sternberg P.W.;
RT "C. elegans LIN-18 is a Ryk ortholog and functions in parallel to LIN-
RT 17/Frizzled in Wnt signaling.";
RL Cell 118:795-806(2004).
RN [3] {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 [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=15649465; DOI=10.1016/j.ydbio.2004.10.020;
RA Deshpande R., Inoue T., Priess J.R., Hill R.J.;
RT "lin-17/Frizzled and lin-18 regulate POP-1/TCF-1 localization and cell type
RT specification during C. elegans vulval development.";
RL Dev. Biol. 278:118-129(2005).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=18622031; DOI=10.1534/genetics.108.090290;
RA Zinovyeva A.Y., Yamamoto Y., Sawa H., Forrester W.C.;
RT "Complex network of Wnt signaling regulates neuronal migrations during
RT Caenorhabditis elegans development.";
RL Genetics 179:1357-1371(2008).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=32053105; DOI=10.7554/elife.50986;
RA Haag A., Walser M., Henggeler A., Hajnal A.;
RT "The CHORD protein CHP-1 regulates EGF receptor trafficking and signaling
RT in C. elegans and in human cells.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Has no detectable kinase activity in vitro and is unlikely to
CC function as a tyrosine kinase in vivo (By similarity). Receptor which
CC may act as a receptor for Wnt ligand mom-2. Plays a role in controlling
CC P7.p vulva precursor cell lineage orientation during vulva development
CC (PubMed:15369677, PubMed:15649465). Regulates pop-1 asymmetric
CC distribution in P7.p and its daughter cells (PubMed:15649465). Plays a
CC role in the migration of ALM neurons during embryogenesis
CC (PubMed:18622031). {ECO:0000250|UniProtKB:P34925,
CC ECO:0000269|PubMed:15369677, ECO:0000269|PubMed:15649465,
CC ECO:0000269|PubMed:18622031}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15369677};
CC Single-pass type I membrane protein {ECO:0000305}. Basolateral cell
CC membrane {ECO:0000269|PubMed:32053105}; Single-pass type I membrane
CC protein {ECO:0000255}. Note=Localizes to the basolateral cell membrane
CC of vulval precursor cells. {ECO:0000269|PubMed:32053105}.
CC -!- DEVELOPMENTAL STAGE: Expressed in vulva cell precursors (VPC) P5.p,
CC P6.p and P7.p, and their descendants during L3 and L4 larval stages.
CC {ECO:0000269|PubMed:15369677}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: May lack kinase activity. The human ortholog has been shown to
CC have impaired catalytic activity with an inability to undergo
CC autophosphorylation or to phosphorylate substrates.
CC {ECO:0000250|UniProtKB:P34925, ECO:0000305|PubMed:15369677}.
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DR EMBL; AF133217; AAD24877.1; -; mRNA.
DR EMBL; BX284606; CCD64652.1; -; Genomic_DNA.
DR RefSeq; NP_508684.4; NM_076283.4.
DR AlphaFoldDB; G5EGT9; -.
DR SMR; G5EGT9; -.
DR STRING; 6239.C16B8.1.2; -.
DR EPD; G5EGT9; -.
DR PaxDb; G5EGT9; -.
DR PeptideAtlas; G5EGT9; -.
DR PRIDE; G5EGT9; -.
DR EnsemblMetazoa; C16B8.1.1; C16B8.1.1; WBGene00003007.
DR GeneID; 180679; -.
DR KEGG; cel:CELE_C16B8.1; -.
DR CTD; 180679; -.
DR WormBase; C16B8.1; CE44782; WBGene00003007; lin-18.
DR eggNOG; KOG1024; Eukaryota.
DR GeneTree; ENSGT00940000155119; -.
DR HOGENOM; CLU_000288_7_36_1; -.
DR InParanoid; G5EGT9; -.
DR OMA; PQEPQTW; -.
DR OrthoDB; 833475at2759; -.
DR PhylomeDB; G5EGT9; -.
DR PRO; PR:G5EGT9; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003007; Expressed in larva and 3 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:WormBase.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0048560; P:establishment of anatomical structure orientation; IMP:WormBase.
DR GO; GO:0040035; P:hermaphrodite genitalia development; IMP:WormBase.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:WormBase.
DR GO; GO:0010085; P:polarity specification of proximal/distal axis; IMP:WormBase.
DR GO; GO:1905488; P:positive regulation of anterior/posterior axon guidance; IGI:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:1905485; P:positive regulation of motor neuron migration; IGI:UniProtKB.
DR GO; GO:1905491; P:positive regulation of sensory neuron axon guidance; IGI:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IMP:WormBase.
DR GO; GO:0040028; P:regulation of vulval development; IMP:WormBase.
DR GO; GO:1904937; P:sensory neuron migration; IMP:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.2170; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR003306; WIF.
DR InterPro; IPR038677; WIF_sf.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF02019; WIF; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00469; WIF; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50814; WIF; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Neurogenesis; Nucleotide-binding; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..583
FT /note="Inactive tyrosine-protein kinase RYK"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434601"
FT TOPO_DOM 19..173
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..583
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..147
FT /note="WIF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00222"
FT DOMAIN 281..583
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 287..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 113..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00222"
FT MUTAGEN 38..39
FT /note="Missing: Formation of an ectopic vulval lumen."
FT /evidence="ECO:0000269|PubMed:15369677"
SQ SEQUENCE 583 AA; 65901 MW; FE6DFF8E47D24300 CRC64;
MILRYLIFFA QLWALCLANV NMFISKEEMN RTFGVKAELN YIEMGNVSSY STKFHYRVMA
NIDYLSFTWN AVGIVHYEVY VESDDSSVLP IVRIPLKGTV PESLQDFTVE YRCAGHRSGQ
FAVSLYFTFK YGNKEPLKVK LRQEKICASR DGRRGLNGGY EGHEVDDTDS IDKAFFVIIC
IAAAFLLIVA ATLICYFKRS KKEDMIPTRL PTSFRNSLKS TKSAQPFLLS TPRDGPPTLS
AISSAPCSSS SASGNSIIPS KPRNIDVRRA LLQLYQDRDA FQSLPLDMEG TFGEVRYAIW
RQVDDVLNGD VDDEEDTFCN QEAVYTKTLK NNASPIQLDR FLSDALLFYN ITPHQNLSQV
ACVASFGRFD RPETVTDFPL VCYRHQGFGN LKKFLTICRH GDKTKGAQTL RTHQLVSLAT
QVSSAVAHIH KYRIVHNDIA ARNCLIAEVN GRLQVQLCDS ALSRDLFPAD YHCLGDNENR
PLKWMSPEAI ANELYSSAAD VWSLGVLLWE LMSLGGSPHA EIDPEEVYTM ILKGKRLQQP
NNCPDQLYEV MLCCWRVLSE DRPSSEQVVH GLRDFNIQLS QYI
