CAM1_CAEEL
ID CAM1_CAEEL Reviewed; 928 AA.
AC G5EGK5; G5ECA5; Q38G54;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Tyrosine-protein kinase receptor cam-1 {ECO:0000305};
DE EC=2.7.10.1 {ECO:0000255|PIRNR:PIRNR000624, ECO:0000269|PubMed:25029443};
GN Name=cam-1 {ECO:0000312|WormBase:C01G6.8a};
GN Synonyms=kin-8 {ECO:0000312|EMBL:CAC29084.1};
GN ORFNames=C01G6.8 {ECO:0000312|WormBase:C01G6.8a};
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:CAC29084.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 624-LYS-LYS-625.
RX PubMed=10556063; DOI=10.1242/dev.126.23.5387;
RA Koga M., Take-uchi M., Tameishi T., Ohshima Y.;
RT "Control of DAF-7 TGF-(alpha) expression and neuronal process development
RT by a receptor tyrosine kinase KIN-8 in Caenorhabditis elegans.";
RL Development 126:5387-5398(1999).
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.
RX PubMed=9165130; DOI=10.1242/dev.124.9.1831;
RA Forrester W.C., Garriga G.;
RT "Genes necessary for C. elegans cell and growth cone migrations.";
RL Development 124:1831-1843(1997).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=9475729; DOI=10.1093/genetics/148.1.151;
RA Forrester W.C., Perens E., Zallen J.A., Garriga G.;
RT "Identification of Caenorhabditis elegans genes required for neuronal
RT differentiation and migration.";
RL Genetics 148:151-165(1998).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=10476968; DOI=10.1038/23722;
RA Forrester W.C., Dell M., Perens E., Garriga G.;
RT "A C. elegans Ror receptor tyrosine kinase regulates cell motility and
RT asymmetric cell division.";
RL Nature 400:881-885(1999).
RN [6] {ECO:0000305}
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF CYS-265.
RX PubMed=14651925; DOI=10.1016/j.ydbio.2003.09.007;
RA Kim C., Forrester W.C.;
RT "Functional analysis of the domains of the C elegans Ror receptor tyrosine
RT kinase CAM-1.";
RL Dev. Biol. 264:376-390(2003).
RN [7] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF CYS-265.
RX PubMed=14504222; DOI=10.1093/genetics/165.1.127;
RA Ailion M., Thomas J.H.;
RT "Isolation and characterization of high-temperature-induced Dauer formation
RT mutants in Caenorhabditis elegans.";
RL Genetics 165:127-144(2003).
RN [8] {ECO:0000305}
RP FUNCTION, AND DOMAIN.
RX PubMed=15371357; DOI=10.1534/genetics.104.031781;
RA Forrester W.C., Kim C., Garriga G.;
RT "The Caenorhabditis elegans Ror RTK CAM-1 inhibits EGL-20/Wnt signaling in
RT cell migration.";
RL Genetics 168:1951-1962(2004).
RN [9] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=15944127; DOI=10.1016/j.neuron.2005.04.010;
RA Francis M.M., Evans S.P., Jensen M., Madsen D.M., Mancuso J., Norman K.R.,
RA Maricq A.V.;
RT "The Ror receptor tyrosine kinase CAM-1 is required for ACR-16-mediated
RT synaptic transmission at the C. elegans neuromuscular junction.";
RL Neuron 46:581-594(2005).
RN [10] {ECO:0000305}
RP FUNCTION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=17942487; DOI=10.1242/dev.005363;
RA Green J.L., Inoue T., Sternberg P.W.;
RT "The C. elegans ROR receptor tyrosine kinase, CAM-1, non-autonomously
RT inhibits the Wnt pathway.";
RL Development 134:4053-4062(2007).
RN [11] {ECO:0000305}
RP FUNCTION, AND DOMAIN.
RX PubMed=19855022; DOI=10.1242/dev.038109;
RA Kennerdell J.R., Fetter R.D., Bargmann C.I.;
RT "Wnt-Ror signaling to SIA and SIB neurons directs anterior axon guidance
RT and nerve ring placement in C. elegans.";
RL Development 136:3801-3810(2009).
RN [12] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, AND MUTAGENESIS
RP OF 624-LYS-LYS-625.
RX PubMed=19561603; DOI=10.1038/nn.2347;
RA Hayashi Y., Hirotsu T., Iwata R., Kage-Nakadai E., Kunitomo H.,
RA Ishihara T., Iino Y., Kubo T.;
RT "A trophic role for Wnt-Ror kinase signaling during developmental pruning
RT in Caenorhabditis elegans.";
RL Nat. Neurosci. 12:981-987(2009).
RN [13] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, DOMAIN, AND MUTAGENESIS OF GLY-790.
RX PubMed=25373777; DOI=10.1016/j.devcel.2014.08.008;
RA Mentink R.A., Middelkoop T.C., Rella L., Ji N., Tang C.Y., Betist M.C.,
RA van Oudenaarden A., Korswagen H.C.;
RT "Cell intrinsic modulation of Wnt signaling controls neuroblast migration
RT in C. elegans.";
RL Dev. Cell 31:188-201(2014).
RN [14] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PHOSPHORYLATION, AND MUTAGENESIS OF GLY-599; LYS-624 AND ASP-744.
RX PubMed=25029443; DOI=10.1371/journal.pone.0102695;
RA Bainbridge T.W., DeAlmeida V.I., Izrael-Tomasevic A., Chalouni C., Pan B.,
RA Goldsmith J., Schoen A.P., Quinones G.A., Kelly R., Lill J.R., Sandoval W.,
RA Costa M., Polakis P., Arnott D., Rubinfeld B., Ernst J.A.;
RT "Evolutionary divergence in the catalytic activity of the CAM-1, ROR1 and
RT ROR2 kinase domains.";
RL PLoS ONE 9:E102695-E102695(2014).
RN [15] {ECO:0000305}
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF CYS-265; GLY-713 AND GLY-790.
RX PubMed=25917219; DOI=10.1016/j.ydbio.2015.04.015;
RA Chien S.C., Gurling M., Kim C., Craft T., Forrester W., Garriga G.;
RT "Autonomous and nonautonomous regulation of Wnt-mediated neuronal polarity
RT by the C. elegans Ror kinase CAM-1.";
RL Dev. Biol. 404:55-65(2015).
CC -!- FUNCTION: Tyrosine-protein kinase receptor for Wnt ligands egl-20, mom-
CC 2 and cwn-1 (PubMed:17942487, PubMed:25029443). Involved in the final
CC positioning of migrating ALM, CAN, BDU and HSN neurons during
CC development (PubMed:10476968, PubMed:9165130, PubMed:9475729,
CC PubMed:14651925). Involved in the anterior-posterior migration of QR
CC neuroblast descendants, QR.p and QR.pa, by maintaining QR.p cell
CC polarization, probably through mig-2 (PubMed:25373777). In addition,
CC plays a role in ASI sensory neuron positioning and functions
CC (PubMed:10556063). Regulates asymmetric division of V cells (seam
CC cells) and CA/CP neuroblast, and axon outgrowth (PubMed:10476968,
CC PubMed:14651925). Probably by acting as a receptor for Wnt ligand cwn-
CC 2, plays a role in the positioning of the nerve ring by controlling
CC axon guidance of SIA and SIB neurons (PubMed:19855022). Involved in
CC synapse plasticity by regulating delivery and/or stabilization of
CC acetylcholine receptor acr-16 at post-synaptic membrane sites and the
CC distribution of synaptic vesicles at pre-synaptic release sites
CC (PubMed:15944127). Probably by acting as a receptor for Wnt ligands
CC cwn-1 and cwn-2, negatively regulates developmental neurite pruning of
CC AIM neurons (PubMed:19561603). Plays a role in ALM neuron polarity
CC (PubMed:25917219). By binding Wnt ligands mom-2, cwn-1 and egl-20 and
CC thereby restricting their availability, negatively regulates Wnt
CC signaling. This mechanism is involved in HSN neuron and QR neuronal
CC descendent migration, and in vulva development (PubMed:15371357,
CC PubMed:17942487). Involved in dauer formation, locomotion, tail
CC morphology and egg-laying (PubMed:10556063, PubMed:9475729,
CC PubMed:14504222). May be involved in distal tip cell (DTC) migration
CC during the development of the posterior gonad (PubMed:10556063).
CC {ECO:0000269|PubMed:10476968, ECO:0000269|PubMed:10556063,
CC ECO:0000269|PubMed:14504222, ECO:0000269|PubMed:14651925,
CC ECO:0000269|PubMed:15371357, ECO:0000269|PubMed:15944127,
CC ECO:0000269|PubMed:17942487, ECO:0000269|PubMed:19561603,
CC ECO:0000269|PubMed:19855022, ECO:0000269|PubMed:25029443,
CC ECO:0000269|PubMed:25373777, ECO:0000269|PubMed:25917219,
CC ECO:0000269|PubMed:9165130, ECO:0000269|PubMed:9475729}.
CC -!- FUNCTION: [Isoform a]: Involved in the positioning of the nerve ring.
CC {ECO:0000269|PubMed:19855022}.
CC -!- FUNCTION: [Isoform b]: Involved in the positioning of the nerve ring.
CC {ECO:0000269|PubMed:19855022}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PIRNR:PIRNR000624,
CC ECO:0000269|PubMed:25029443};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25029443};
CC Note=Can use both Mg(2+) and Mn(2+) in vitro and shows higher activity
CC with Mn(2+) but Mg(2+) is likely to be the in vivo cofactor.
CC {ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.53 mM for ATP (in the presence of Mg(2+) at 20 degrees Celsius)
CC {ECO:0000269|PubMed:25029443};
CC KM=0.45 mM for ATP (in the presence of Mn(2+) at 20 degrees Celsius)
CC {ECO:0000269|PubMed:25029443};
CC Note=Autophosphorylation gives similar KM values for ATP.
CC {ECO:0000269|PubMed:25029443};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10476968,
CC ECO:0000269|PubMed:15944127}; Single-pass type I membrane protein
CC {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:10476968,
CC ECO:0000269|PubMed:15944127, ECO:0000269|PubMed:19561603}. Cell
CC projection, dendrite {ECO:0000269|PubMed:10476968,
CC ECO:0000269|PubMed:15944127, ECO:0000269|PubMed:19561603}. Perikaryon
CC {ECO:0000269|PubMed:15944127}. Synapse {ECO:0000269|PubMed:15944127}.
CC Note=Localizes in punctate structures along neuronal processes where it
CC partially colocalizes with synaptic vesicle marker snb-1
CC (PubMed:15944127). Localizes in punctate structures in the axons
CC forming the nerve ring and in proximal AIM neurites destined for
CC elimination (PubMed:19561603). Enriched at the distal tips of muscle
CC arms where they interact with ventral nerve cord (PubMed:15944127).
CC {ECO:0000269|PubMed:15944127, ECO:0000269|PubMed:19561603}.
CC -!- SUBCELLULAR LOCATION: [Isoform b]: Cell membrane
CC {ECO:0000269|PubMed:10556063}; Single-pass type I membrane protein
CC {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:10556063}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:C01G6.8a};
CC IsoId=G5EGK5-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C01G6.8b};
CC IsoId=G5EGK5-2; Sequence=VSP_057955;
CC Name=c {ECO:0000312|WormBase:C01G6.8c};
CC IsoId=G5EGK5-3; Sequence=VSP_057954;
CC -!- TISSUE SPECIFICITY: Expressed in AIM neurons and in several head
CC neurons (PubMed:19561603). Isoform a is expressed in some head muscles
CC and in several head neurons. Isoform b is expressed in several head
CC neurons, in procorpus and isthmus pharyngeal muscles, body wall
CC muscles, and to a lower extent in intestine, seam cells (V cells) and
CC distal tip cells (PubMed:10556063, PubMed:10476968, PubMed:15944127).
CC {ECO:0000269|PubMed:10476968, ECO:0000269|PubMed:10556063,
CC ECO:0000269|PubMed:15944127, ECO:0000269|PubMed:19561603}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 200-cell stage embryo
CC (PubMed:10476968). Expressed predominantly in QR neuroblast descendants
CC and to a lesser extent in QL neuroblast descendants during larval stage
CC (PubMed:25373777). {ECO:0000269|PubMed:10476968,
CC ECO:0000269|PubMed:25373777}.
CC -!- DOMAIN: The FZ domain is involved in binding to Wnt ligands egl-20,
CC cwn-1 and mom-2 (PubMed:15371357, PubMed:17942487). The domain is
CC required for the final positioning of migrating ALM, CAN, BDU and HSN
CC neurons, and maybe QR neuroblast descendants during development and for
CC neurite pruning of AIM neurons (PubMed:14651925, PubMed:19561603).
CC Required for the establishment of ALM polarity (PubMed:25917219).
CC {ECO:0000269|PubMed:14651925, ECO:0000269|PubMed:15371357,
CC ECO:0000269|PubMed:17942487, ECO:0000269|PubMed:19561603,
CC ECO:0000269|PubMed:25373777, ECO:0000269|PubMed:25917219}.
CC -!- DOMAIN: The domain is required to establish correct polarity in ALM
CC neurons (PubMed:25917219). May play a role in QR neuroblast descendant
CC migration (PubMed:25373777). The kinase domain is dispensable for ALM,
CC CAN, BDU and HSN neuron migration, V cell asymmetric division, acr-16
CC localization, for the positioning of the nerve ring and probably for
CC the negative regulation of neurite pruning of AIM neurons
CC (PubMed:14651925, PubMed:15944127, PubMed:19855022, PubMed:19561603).
CC {ECO:0000269|PubMed:14651925, ECO:0000269|PubMed:15944127,
CC ECO:0000269|PubMed:19561603, ECO:0000269|PubMed:19855022,
CC ECO:0000269|PubMed:25373777, ECO:0000269|PubMed:25917219}.
CC -!- DOMAIN: The cytoplasmic domain is required for the negative regulation
CC of neurite pruning of AIM neurons. {ECO:0000269|PubMed:19561603}.
CC -!- PTM: Autophosphorylated at tyrosine residues which are probably located
CC in the activation loop (residues 724-732). Autophosphorylation does not
CC increase kinase activity in vitro. {ECO:0000269|PubMed:25029443}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in a lin-17 n671 mutant
CC background causes 8 percent of animals to produce more than 22 vulval
CC cells (overinduction). {ECO:0000269|PubMed:17942487}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. ROR subfamily. {ECO:0000255|PIRNR:PIRNR000624}.
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DR EMBL; AJ132946; CAC29084.1; -; mRNA.
DR EMBL; AJ132947; CAC29085.1; -; mRNA.
DR EMBL; BX284602; CAA84639.2; -; Genomic_DNA.
DR EMBL; BX284602; CAD36478.1; -; Genomic_DNA.
DR EMBL; BX284602; CAJ34992.1; -; Genomic_DNA.
DR PIR; T18840; T18840.
DR RefSeq; NP_001021907.1; NM_001026736.4. [G5EGK5-1]
DR RefSeq; NP_001021908.1; NM_001026737.3. [G5EGK5-2]
DR RefSeq; NP_001033327.1; NM_001038238.2.
DR AlphaFoldDB; G5EGK5; -.
DR SMR; G5EGK5; -.
DR IntAct; G5EGK5; 3.
DR STRING; 6239.C01G6.8a; -.
DR EPD; G5EGK5; -.
DR PaxDb; G5EGK5; -.
DR PeptideAtlas; G5EGK5; -.
DR EnsemblMetazoa; C01G6.8a.1; C01G6.8a.1; WBGene00000289. [G5EGK5-1]
DR EnsemblMetazoa; C01G6.8b.1; C01G6.8b.1; WBGene00000289. [G5EGK5-2]
DR EnsemblMetazoa; C01G6.8c.1; C01G6.8c.1; WBGene00000289. [G5EGK5-3]
DR EnsemblMetazoa; C01G6.8c.2; C01G6.8c.2; WBGene00000289. [G5EGK5-3]
DR GeneID; 174473; -.
DR KEGG; cel:CELE_C01G6.8; -.
DR UCSC; C01G6.8a; c. elegans.
DR CTD; 174473; -.
DR WormBase; C01G6.8a; CE32563; WBGene00000289; cam-1. [G5EGK5-1]
DR WormBase; C01G6.8b; CE24774; WBGene00000289; cam-1. [G5EGK5-2]
DR WormBase; C01G6.8c; CE39126; WBGene00000289; cam-1. [G5EGK5-3]
DR eggNOG; KOG1026; Eukaryota.
DR GeneTree; ENSGT00940000166767; -.
DR InParanoid; G5EGK5; -.
DR OMA; HGHSESM; -.
DR OrthoDB; 471114at2759; -.
DR PhylomeDB; G5EGK5; -.
DR Reactome; R-CEL-170968; Frs2-mediated activation.
DR Reactome; R-CEL-170984; ARMS-mediated activation.
DR SignaLink; G5EGK5; -.
DR PRO; PR:G5EGK5; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000289; Expressed in pharyngeal muscle cell (C elegans) and 12 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0042995; C:cell projection; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:WormBase.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
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:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0005109; F:frizzled binding; IPI:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038062; F:protein tyrosine kinase collagen receptor activity; IBA:GO_Central.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:WormBase.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:WormBase.
DR GO; GO:0007411; P:axon guidance; IMP:WormBase.
DR GO; GO:0016477; P:cell migration; IMP:WormBase.
DR GO; GO:0045200; P:establishment of neuroblast polarity; IMP:WormBase.
DR GO; GO:1904936; P:interneuron migration; IGI:UniProtKB.
DR GO; GO:0097475; P:motor neuron migration; IGI:UniProtKB.
DR GO; GO:0097402; P:neuroblast migration; IMP:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:WormBase.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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 CDD; cd07459; CRD_TK_ROR_like; 1.
DR CDD; cd00108; KR; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR041775; Ror-like_CRD.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016247; Tyr_kinase_rcpt_ROR.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000624; TyrPK_TMrec_ROR; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase; Kringle;
KW Magnesium; Membrane; Metal-binding; Neurogenesis; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Synapse; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
KW Wnt signaling pathway.
FT CHAIN 1..928
FT /note="Tyrosine-protein kinase receptor cam-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434557"
FT TOPO_DOM 1..466
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..928
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..126
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 200..332
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 353..429
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 590..870
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 726
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 596..604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 624
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 24
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 CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 59..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 205..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 213..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 256..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 284..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 288..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 354..429
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DISULFID 375..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DISULFID 401..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT VAR_SEQ 1..159
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057954"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057955"
FT MUTAGEN 265
FT /note="C->Y: In sa692; constitutive dauer formation at high
FT temperature and impaired migration of ALM, BDU, CAN and HSN
FT neurons, and QR neuroblast descendants during development.
FT Moderate defect in ALM polarity."
FT /evidence="ECO:0000269|PubMed:14504222,
FT ECO:0000269|PubMed:14651925, ECO:0000269|PubMed:25917219"
FT MUTAGEN 599
FT /note="G->C,D: Moderate loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:25029443"
FT MUTAGEN 624..625
FT /note="KK->MM: Probable loss of kinase activity. Abnormal
FT locomotion. No increase in dauer formation."
FT /evidence="ECO:0000269|PubMed:10556063"
FT MUTAGEN 624..625
FT /note="KK->RR: Probable loss of kinase activity. Increased
FT number of interconnected AIM neurons when expressed in a
FT wild type background."
FT /evidence="ECO:0000269|PubMed:19561603"
FT MUTAGEN 624
FT /note="K->R: No effect on kinase activity."
FT /evidence="ECO:0000269|PubMed:25029443"
FT MUTAGEN 713
FT /note="G->R: In cw82; mild defect in ALM polarity."
FT /evidence="ECO:0000269|PubMed:25917219"
FT MUTAGEN 744
FT /note="D->N: Severe loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:25029443"
FT MUTAGEN 790
FT /note="G->E: In xd13; mild defect in ALM polarity and in QR
FT neuroblast descendant migration."
FT /evidence="ECO:0000269|PubMed:25373777,
FT ECO:0000269|PubMed:25917219"
SQ SEQUENCE 928 AA; 103864 MW; F13B8C9BCAB30D20 CRC64;
MSPRPEDDDL VIEPADDEGL HYGNASMEGT STGQRPYIRL TSQLRNATKS SGDEVRFKCE
ALGTPPLKFI WLKNNGPVEK TKRVKIRDKE NSSRLVITQL DVLDSGYYQC IVSNPAASVN
TTSVLRVNNV PDAVKLSQKK GSHHSTKHIA FDEYEDYEMM DRGRLPDEED ADLYRVPDSA
AGSNYAPVAV SERWLDGIKY RVGDCVQYRG EACRQYLSNK FVMMTNESRE EMYDIDRNLR
AAMLFINGAP TISQKCRQLS QAVACHHMYK VCESDSNNQI VSICKHDCDV IQNDECPSEL
ALAAQHELVG DTPKALFPLC SRLSSTSNCI PVMSTALQSS PVAEVNRGHL THWCYVNSGT
QYEGTVAQTS SGKQCAPWID STSRDFNVHR FPELMNSKNY CRNPGGKKSR PWCYSKPMGQ
EEYCDVPQCP SDMYPHLNDK KVEGSTKGGV SESVTALWDS LDPTMQVALV GGGVFFSLLL
LLLFCCACCC RAKKKSQKTR HQNAHCSSAP SVINSAANSA YYRKLNGTST PIMGRVPPHV
EMTSLLPSAQ HLGPPPYPMD QHLQQARRFP SQEPIDDNSY KVFEITPSQL SVREKIGEGQ
FGVVHSGIYT SGLFAPEPMA VAVKKCRHDA TNAERAQLEQ EIRAVATFDH PNVIKLIGVC
YMDNSLLAVF EYMVHGDLHE LLKVRVPPAD HDMGGITEAN AEFLYIATQI ALGMEYLASM
SFVHRDLATR NCLVGDTRTI KIADFGLMRT SYGSDYYKML HRSWMPVRWM SKEAIEQGRF
SEASDVWSFG VTLWEIWSFG RQPYEGASNQ QVIELVANRH LLECPHNCPT NIYSLMVECW
HENIERRPTF SEIRSRLQSW SLASPAHSIL QQHNNRAGSH SGSSGAGRPP THQRGYPSQK
LHRRVEGASP LMKRHDANYA YSEDGDSD
