UNC5_CAEEL
ID UNC5_CAEEL Reviewed; 947 AA.
AC Q26261; O44171; Q26262; Q7JPT6; Q7KPX0; V6CK86; V6CLG6; V6CLK6; V6CLL7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Netrin receptor unc-5;
DE AltName: Full=Uncoordinated protein 5;
DE Flags: Precursor;
GN Name=unc-5 {ECO:0000312|WormBase:B0273.4c};
GN ORFNames=B0273.4 {ECO:0000312|WormBase:B0273.4c};
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 [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A AND C),
RP AND FUNCTION.
RX PubMed=1384987; DOI=10.1016/0092-8674(92)90357-i;
RA Leung-Hagesteijn C., Spence A.M., Stern B.D., Zhou Y., Su M.-W.,
RA Hedgecock E.M., Culotti J.G.;
RT "UNC-5, a transmembrane protein with immunoglobulin and thrombospondin type
RT 1 domains, guides cell and pioneer axon migrations in C. elegans.";
RL Cell 71:289-299(1992).
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).
RN [3]
RP FUNCTION.
RX PubMed=8332188; DOI=10.1038/364327a0;
RA Hamelin M., Zhou Y., Su M.-W., Scott I.M., Culotti J.G.;
RT "Expression of the UNC-5 guidance receptor in the touch neurons of C.
RT elegans steers their axons dorsally.";
RL Nature 364:327-330(1993).
RN [4]
RP FUNCTION.
RX PubMed=9473333; DOI=10.1006/dbio.1997.8790;
RA Colavita A., Culotti J.G.;
RT "Suppressors of ectopic UNC-5 growth cone steering identify eight genes
RT involved in axon guidance in Caenorhabditis elegans.";
RL Dev. Biol. 194:72-85(1998).
RN [5]
RP FUNCTION.
RX PubMed=10631179; DOI=10.1242/dev.127.3.585;
RA Su M.-W., Merz D.C., Killeen M.T., Zhou Y., Zheng H., Kramer J.M.,
RA Hedgecock E.M., Culotti J.G.;
RT "Regulation of the UNC-5 netrin receptor initiates the first reorientation
RT of migrating distal tip cells in Caenorhabditis elegans.";
RL Development 127:585-594(2000).
RN [6]
RP FUNCTION.
RX PubMed=11454756; DOI=10.1093/genetics/158.3.1071;
RA Merz D.C., Zheng H., Killeen M.T., Krizus A., Culotti J.G.;
RT "Multiple signaling mechanisms of the UNC-6/netrin receptors UNC-5 and UNC-
RT 40/DCC in vivo.";
RL Genetics 158:1071-1080(2001).
RN [7]
RP PHOSPHORYLATION.
RX PubMed=11533026; DOI=10.1074/jbc.m103872200;
RA Tong J., Killeen M., Steven R., Binns K.L., Culotti J., Pawson T.;
RT "Netrin stimulates tyrosine phosphorylation of the UNC-5 family of netrin
RT receptors and induces Shp2 binding to the RCM cytodomain.";
RL J. Biol. Chem. 276:40917-40925(2001).
RN [8]
RP PHOSPHORYLATION AT TYR-510, TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-209;
RP 415-TYR-TYR-416; TYR-445; TYR-467; TYR-510; TYR-566 AND TYR-719.
RX PubMed=12435363; DOI=10.1006/dbio.2002.0825;
RA Killeen M., Tong J., Krizus A., Steven R., Scott I., Pawson T., Culotti J.;
RT "UNC-5 function requires phosphorylation of cytoplasmic tyrosine 482, but
RT its UNC-40-independent functions also require a region between the ZU-5 and
RT death domains.";
RL Dev. Biol. 251:348-366(2002).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=16251208; DOI=10.1242/dev.02103;
RA Itoh B., Hirose T., Takata N., Nishiwaki K., Koga M., Ohshima Y., Okada M.;
RT "SRC-1, a non-receptor type of protein tyrosine kinase, controls the
RT direction of cell and growth cone migration in C. elegans.";
RL Development 132:5161-5172(2005).
RN [10]
RP INTERACTION WITH SRC-1, AND PHOSPHORYLATION.
RX PubMed=16024786; DOI=10.1128/mcb.25.15.6485-6495.2005;
RA Lee J., Li W., Guan K.L.;
RT "SRC-1 mediates UNC-5 signaling in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 25:6485-6495(2005).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF CYS-209 AND 311-TRP--PRO-947.
RX PubMed=17716643; DOI=10.1016/j.ydbio.2007.07.014;
RA Zheng H., Coudiere L., Camia C., Colavita A., Culotti J.G., Merz D.C.;
RT "C. elegans seu-1 encodes novel nuclear proteins that regulate responses to
RT UNC-6/netrin guidance cues.";
RL Dev. Biol. 310:44-53(2007).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [13]
RP INTERACTION WITH UNC-129, AND MUTAGENESIS OF 311-TRP--PRO-947.
RX PubMed=19169249; DOI=10.1038/nn.2256;
RA MacNeil L.T., Hardy W.R., Pawson T., Wrana J.L., Culotti J.G.;
RT "UNC-129 regulates the balance between UNC-40 dependent and independent
RT UNC-5 signaling pathways.";
RL Nat. Neurosci. 12:150-155(2009).
RN [14]
RP GLYCOSYLATION AT TRP-305 AND TRP-308.
RX PubMed=23562325; DOI=10.1016/j.molcel.2013.03.003;
RA Buettner F.F., Ashikov A., Tiemann B., Lehle L., Bakker H.;
RT "C. elegans DPY-19 is a C-mannosyltransferase glycosylating thrombospondin
RT repeats.";
RL Mol. Cell 50:295-302(2013).
RN [15]
RP INTERACTION WITH MADD-4.
RX PubMed=25122090; DOI=10.1371/journal.pgen.1004521;
RA Chan K.K., Seetharaman A., Bagg R., Selman G., Zhang Y., Kim J., Roy P.J.;
RT "EVA-1 functions as an UNC-40 Co-receptor to enhance attraction to the
RT MADD-4 guidance cue in Caenorhabditis elegans.";
RL PLoS Genet. 10:E1004521-E1004521(2014).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26292279; DOI=10.1371/journal.pgen.1005446;
RA Levy-Strumpf N., Krizus M., Zheng H., Brown L., Culotti J.G.;
RT "The Wnt frizzled receptor MOM-5 regulates the UNC-5 Netrin receptor
RT through small GTPase-dependent signaling to determine the polarity of
RT migrating cells.";
RL PLoS Genet. 11:E1005446-E1005446(2015).
CC -!- FUNCTION: Receptor for netrin (unc-6) required for axon guidance
CC (PubMed:8332188, PubMed:11454756). Mediates axon repulsion of neuronal
CC growth cones in the developing nervous system upon ligand binding
CC (PubMed:1384987, PubMed:8332188, PubMed:11454756, PubMed:9473333). Axon
CC migration is mediated by the secreted unc-6, which promotes attraction
CC of neurons and axons through binding to the unc-40 receptor, while
CC repulsion requires both unc-5 and unc-40 receptors (PubMed:11454756,
CC PubMed:9473333). Involved in the ventral-dorsal and anterior-posterior
CC migration of distal tip cells along the body, which may be mediated by
CC Wnt receptor mom-5, ced-10/Rac, ced-12/ELMO and mig-2/RhoG
CC (PubMed:10631179, PubMed:26292279, PubMed:17716643).
CC {ECO:0000269|PubMed:10631179, ECO:0000269|PubMed:11454756,
CC ECO:0000269|PubMed:1384987, ECO:0000269|PubMed:17716643,
CC ECO:0000269|PubMed:26292279, ECO:0000269|PubMed:8332188,
CC ECO:0000269|PubMed:9473333}.
CC -!- SUBUNIT: Interacts (via cytoplasmic domain) with src-1 (via SH2 domain
CC and SH3 domain) (PubMed:16024786). Interacts with madd-4
CC (PubMed:25122090). Interacts with unc-129; the interaction is direct
CC (PubMed:19169249). {ECO:0000269|PubMed:16024786,
CC ECO:0000269|PubMed:19169249, ECO:0000269|PubMed:25122090}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O08721};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:O08721}.
CC Membrane raft {ECO:0000250|UniProtKB:O08721}. Cell projection, neuron
CC projection {ECO:0000250|UniProtKB:O08721}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=c {ECO:0000312|WormBase:B0273.4c};
CC IsoId=Q26261-2; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:B0273.4a};
CC IsoId=Q26261-1; Sequence=VSP_061199;
CC Name=b {ECO:0000312|WormBase:B0273.4b};
CC IsoId=Q26261-3; Sequence=VSP_061199, VSP_061200, VSP_061201;
CC Name=d {ECO:0000312|WormBase:B0273.4d};
CC IsoId=Q26261-4; Sequence=VSP_061198;
CC Name=e {ECO:0000312|WormBase:B0273.4e};
CC IsoId=Q26261-5; Sequence=VSP_061197;
CC Name=f {ECO:0000312|WormBase:B0273.4f};
CC IsoId=Q26261-6; Sequence=VSP_061196;
CC -!- TISSUE SPECIFICITY: Expressed in cell bodies and axons of the VNC motor
CC neurons that extend axons to the dorsal midline and within the ventral
CC nerve cord (PubMed:12435363). Expressed in gonadal distal tip cells
CC (DTC) (PubMed:16251208). {ECO:0000269|PubMed:12435363,
CC ECO:0000269|PubMed:16251208}.
CC -!- PTM: Phosphorylated on different cytoplasmic tyrosine residues
CC (PubMed:11533026, PubMed:12435363, PubMed:16024786). May be
CC phosphorylated on tyrosine residues by src-1 (PubMed:16024786).
CC Tyrosine phosphorylation is unc-6-dependent (PubMed:11533026).
CC {ECO:0000269|PubMed:11533026, ECO:0000269|PubMed:12435363,
CC ECO:0000269|PubMed:16024786}.
CC -!- PTM: Glycosylated via C-mannosylation by dpy-19 at Trp-305 and Trp-308.
CC {ECO:0000269|PubMed:17761667, ECO:0000269|PubMed:23562325}.
CC -!- DISRUPTION PHENOTYPE: Failed distal tip cell migration along the
CC dorsal-ventral axis of the body. RNAi-mediated knockdown in mom-5, ced-
CC 10, ced-12 or mig-2 mutant backgrounds suppresses the migratory defect
CC of distal tip cells in the respective single mutants.
CC {ECO:0000269|PubMed:26292279}.
CC -!- SIMILARITY: Belongs to the unc-5 family. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, it lacks a
CC canonical signal sequence; the existence of the signal sequence is
CC therefore unsure. {ECO:0000305}.
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DR EMBL; AH004080; AAB23866.2; -; Genomic_DNA.
DR EMBL; S47135; AAB23866.2; JOINED; Genomic_DNA.
DR EMBL; S47136; AAB23866.2; JOINED; Genomic_DNA.
DR EMBL; S47137; AAB23866.2; JOINED; Genomic_DNA.
DR EMBL; S47164; AAB23866.2; JOINED; Genomic_DNA.
DR EMBL; S47165; AAB23866.2; JOINED; Genomic_DNA.
DR EMBL; S47166; AAB23866.2; JOINED; Genomic_DNA.
DR EMBL; S47167; AAB23866.2; JOINED; Genomic_DNA.
DR EMBL; AH004080; AAB23867.2; -; Genomic_DNA.
DR EMBL; S47134; AAB23867.2; JOINED; Genomic_DNA.
DR EMBL; S47135; AAB23867.2; JOINED; Genomic_DNA.
DR EMBL; S47136; AAB23867.2; JOINED; Genomic_DNA.
DR EMBL; S47137; AAB23867.2; JOINED; Genomic_DNA.
DR EMBL; S47164; AAB23867.2; JOINED; Genomic_DNA.
DR EMBL; S47165; AAB23867.2; JOINED; Genomic_DNA.
DR EMBL; S47166; AAB23867.2; JOINED; Genomic_DNA.
DR EMBL; S47167; AAB23867.2; JOINED; Genomic_DNA.
DR EMBL; BX284604; CCD61588.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD61589.1; -; Genomic_DNA.
DR EMBL; BX284604; CDK13451.1; -; Genomic_DNA.
DR EMBL; BX284604; CDK13452.1; -; Genomic_DNA.
DR EMBL; BX284604; CDK13453.1; -; Genomic_DNA.
DR EMBL; BX284604; CDK13454.1; -; Genomic_DNA.
DR PIR; B44294; B44294.
DR PIR; T32541; T32541.
DR RefSeq; NP_500822.2; NM_068421.4. [Q26261-1]
DR RefSeq; NP_500823.1; NM_068422.5. [Q26261-2]
DR AlphaFoldDB; Q26261; -.
DR SMR; Q26261; -.
DR BioGRID; 42456; 7.
DR STRING; 6239.B0273.4a; -.
DR iPTMnet; Q26261; -.
DR PaxDb; Q26261; -.
DR PeptideAtlas; Q26261; -.
DR EnsemblMetazoa; B0273.4a.1; B0273.4a.1; WBGene00006745. [Q26261-1]
DR EnsemblMetazoa; B0273.4b.1; B0273.4b.1; WBGene00006745. [Q26261-3]
DR EnsemblMetazoa; B0273.4c.1; B0273.4c.1; WBGene00006745. [Q26261-2]
DR EnsemblMetazoa; B0273.4d.1; B0273.4d.1; WBGene00006745. [Q26261-4]
DR EnsemblMetazoa; B0273.4d.2; B0273.4d.2; WBGene00006745. [Q26261-4]
DR EnsemblMetazoa; B0273.4e.1; B0273.4e.1; WBGene00006745. [Q26261-5]
DR EnsemblMetazoa; B0273.4f.1; B0273.4f.1; WBGene00006745. [Q26261-6]
DR GeneID; 177334; -.
DR UCSC; B0273.4a; c. elegans. [Q26261-1]
DR CTD; 36703; -.
DR WormBase; B0273.4a; CE16790; WBGene00006745; unc-5. [Q26261-1]
DR WormBase; B0273.4b; CE37693; WBGene00006745; unc-5. [Q26261-3]
DR WormBase; B0273.4c; CE16791; WBGene00006745; unc-5. [Q26261-2]
DR WormBase; B0273.4d; CE49241; WBGene00006745; unc-5. [Q26261-4]
DR WormBase; B0273.4e; CE49455; WBGene00006745; unc-5. [Q26261-5]
DR WormBase; B0273.4f; CE49300; WBGene00006745; unc-5. [Q26261-6]
DR eggNOG; KOG1480; Eukaryota.
DR GeneTree; ENSGT00950000182815; -.
DR HOGENOM; CLU_014383_0_0_1; -.
DR InParanoid; Q26261; -.
DR OMA; CECQAWS; -.
DR OrthoDB; 334938at2759; -.
DR PhylomeDB; Q26261; -.
DR Reactome; R-CEL-373752; Netrin-1 signaling.
DR PRO; PR:Q26261; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006745; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q26261; baseline and differential.
DR GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:WormBase.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005042; F:netrin receptor activity; IMP:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0061643; P:chemorepulsion of axon; IMP:UniProtKB.
DR GO; GO:0071679; P:commissural neuron axon guidance; IMP:UniProtKB.
DR GO; GO:0097628; P:distal tip cell migration; IMP:UniProtKB.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IMP:UniProtKB.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:UniProtKB.
DR GO; GO:0035262; P:gonad morphogenesis; IMP:UniProtKB.
DR GO; GO:0008078; P:mesodermal cell migration; IMP:WormBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:UniProtKB.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IMP:UniProtKB.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IGI:WormBase.
DR GO; GO:0038007; P:netrin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:1905488; P:positive regulation of anterior/posterior axon guidance; IMP:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:WormBase.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:1905815; P:regulation of dorsal/ventral axon guidance; IMP:UniProtKB.
DR GO; GO:0007419; P:ventral cord development; IMP:UniProtKB.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.20.100.10; -; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR037936; UNC5.
DR InterPro; IPR033772; UPA.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR12582; PTHR12582; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF00090; TSP_1; 1.
DR Pfam; PF17217; UPA; 1.
DR Pfam; PF00791; ZU5; 1.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00209; TSP1; 2.
DR SMART; SM00218; ZU5; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50092; TSP1; 2.
DR PROSITE; PS51145; ZU5; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection;
KW Developmental protein; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..947
FT /note="Netrin receptor unc-5"
FT /id="PRO_0000036081"
FT TOPO_DOM ?..368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..141
FT /note="Ig-like"
FT DOMAIN 139..226
FT /note="Ig-like C2-type"
FT DOMAIN 230..300
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 302..354
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 530..658
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 857..938
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT MOD_RES 510
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:12435363"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 305
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:23562325"
FT CARBOHYD 308
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:23562325"
FT DISULFID 53..112
FT /evidence="ECO:0000250|UniProtKB:Q6ZN44"
FT DISULFID 160..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 243..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 247..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 273..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT VAR_SEQ 1..290
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_061196"
FT VAR_SEQ 1..195
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_061197"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_061198"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform a and isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061199"
FT VAR_SEQ 581..595
FT /note="PIESALSPVIVIGQC -> RECKKILKIYISKIS (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061200"
FT VAR_SEQ 596..947
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061201"
FT MUTAGEN 209
FT /note="C->Y: In ev585; temperature-sensitive allele leading
FT to distal tip cells migration defects. The distal tip cell
FT migration defects are enhanced in seu-1 ev520 or seu-1
FT ev529 mutants."
FT /evidence="ECO:0000269|PubMed:12435363,
FT ECO:0000269|PubMed:17716643"
FT MUTAGEN 311..947
FT /note="Missing: In e53; Disregulates axon guidance and
FT migration. Distal tip cell migration defects. On an unc-129
FT mutant background, does not contribute to an increase in
FT axonal guidance defects. The distal tip cell migration
FT defects are enhanced in seu-1 ev520 or seu-1 ev529
FT mutants."
FT /evidence="ECO:0000269|PubMed:17716643,
FT ECO:0000269|PubMed:19169249"
FT MUTAGEN 415..416
FT /note="YY->FF: Induces a strong decrease in tyrosine
FT phosphorylation but only weakly affects function in vivo;
FT when associated with F-445; F-467; F-566 and F-719."
FT /evidence="ECO:0000269|PubMed:12435363"
FT MUTAGEN 445
FT /note="Y->F: Induces a strong decrease in tyrosine
FT phosphorylation but only weakly affects function in vivo;
FT when associated with F-415; F-416; F-467; F-566 and F-719."
FT /evidence="ECO:0000269|PubMed:12435363"
FT MUTAGEN 467
FT /note="Y->F: Induces a strong decrease in tyrosine
FT phosphorylation but only weakly affects function in vivo;
FT when associated with F-415; F-416; F-445; F-566 and F-719."
FT /evidence="ECO:0000269|PubMed:12435363"
FT MUTAGEN 510
FT /note="Y->F: Loss of function and induces a strong decrease
FT in tyrosine phosphorylation."
FT /evidence="ECO:0000269|PubMed:12435363"
FT MUTAGEN 566
FT /note="Y->F: Induces a strong decrease in tyrosine
FT phosphorylation but only weakly affects function in vivo;
FT when associated with F-415; F-416; F-445; F-467 and F-719."
FT /evidence="ECO:0000269|PubMed:12435363"
FT MUTAGEN 719
FT /note="Y->F: Induces a strong decrease in tyrosine
FT phosphorylation but only weakly affects function in vivo;
FT when associated with F-415; F-416; F-445; F-467 and F-566."
FT /evidence="ECO:0000269|PubMed:12435363"
FT CONFLICT 642
FT /note="V -> L (in Ref. 1; AAB23866/AAB23867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 947 AA; 104729 MW; A60286D544A2F187 CRC64;
MEDDTPDVSS DSNGDAAYSD YFLDYKSIMD EITITTQPKS GYVIRNKPLR LQCRANHATK
IRYKCSSKWI DDSRIEKLIG TDSTSGVGYI DASVDISRID VDTSGHVDAF QCQCYASGDD
DQDVVASDVA TVHLAYMRKH FLKSPVAQRV QEGTTLQLPC QAPESDPKAE LTWYKDGVVV
QPDANVIRAS DGSLIMSAAR LSDSGNYTCE ATNVANSRKT DPVEVQIYVD GGWSEWSPWI
GTCHVDCPLL RQHAHRIRDP HDVLPHQRRT RTCNNPAPLN DGEYCKGEEE MTRSCKVPCK
LDGGWSSWSD WSACSSSCHR YRTRACTVPP PMNGGQPCFG DDLMTQECPA QLCTADSSRI
VISDTAVYGS VASIFIVASF ILAILAMFCC KRGNSKKSKP LKPQKMNSEK AGGIYYSEPP
GVRRLLLEHQ HGTLLGEKIS SCSQYFEPPP LPHSTTLRSG KSAFSGYSST RNAGSRAALI
QECSSSSSGS GGKRTMLRTS SSNCSDDDNY ATLYDYMEDK SVLGLDTSQN IVAAQIDSNG
ARLSLSKSGA RLIVPELAVE GEKMLYLAVS DTLTDQPHLK PIESALSPVI VIGQCDVSMS
AHDNILRRPV VVSFRHCAST FPRDNWQFTL YADEGSGWQK AVTIGEENLN TNMFVQFEQP
GKKNDGFGWC HVMTYSLARL MLAGHPRRNS LSAAKRVHLA VFGPTEMSAY RRPFELRVYC
VPETGAAMES VWKQEDGSRL LCESNDFILN EKGNLCICIE DVIPGFSCDG PEVVEISETQ
HRFVAQNGLH CSLKFRPKEI NGSQFSTRVI VYQKASSTEP MVMEVSNEPE LYDATSEERE
KGSVCVEFRL PFGVKDELAR LLDMPNESHS DWRGLAKKLH YDRYLQFFAS FPDCSPTSLL
LDLWEASSSG SARAVPDLLQ TLRVMGRPDA VMVLERFLSA FPQIVSP
