CELR_CAEEL
ID CELR_CAEEL Reviewed; 2596 AA.
AC G5EDK5; A0A0K3ARX2; A0A0K3AUS4;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cadherin EGF LAG seven-pass G-type receptor fmi-1 {ECO:0000305};
DE AltName: Full=Protein flamingo homolog {ECO:0000305};
DE Flags: Precursor;
GN Name=fmi-1 {ECO:0000312|WormBase:F15B9.7a};
GN ORFNames=F15B9.7 {ECO:0000312|WormBase:F15B9.7a};
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:AAQ84880.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mastwal S.S., Yu D., Hedgecock E.M.;
RT "Molecular and Evolutionary Characterization of family B G-protein coupled
RT receptors in Caenorhabditis elegans.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF 725-GLN--GLU-2596; GLY-842; GLY-1481 AND
RP 2184-TRP--GLU-2596.
RX PubMed=20876647; DOI=10.1242/dev.054320;
RA Steimel A., Wong L., Najarro E.H., Ackley B.D., Garriga G., Hutter H.;
RT "The Flamingo ortholog FMI-1 controls pioneer-dependent navigation of
RT follower axons in C. elegans.";
RL Development 137:3663-3673(2010).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 725-GLN--GLU-2596; GLY-842; GLY-1481 AND 2150-VAL--GLU-2596.
RX PubMed=22442082; DOI=10.1523/jneurosci.3094-11.2012;
RA Najarro E.H., Wong L., Zhen M., Carpio E.P., Goncharov A., Garriga G.,
RA Lundquist E.A., Jin Y., Ackley B.D.;
RT "Caenorhabditis elegans flamingo cadherin fmi-1 regulates GABAergic
RT neuronal development.";
RL J. Neurosci. 32:4196-4211(2012).
RN [5] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 725-GLN--GLU-2596.
RX PubMed=23376536; DOI=10.1016/j.ydbio.2013.01.014;
RA Huarcaya Najarro E., Ackley B.D.;
RT "C. elegans fmi-1/flamingo and Wnt pathway components interact genetically
RT to control the anteroposterior neurite growth of the VD GABAergic
RT neurons.";
RL Dev. Biol. 377:224-235(2013).
RN [6] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 725-GLN--GLU-2596.
RX PubMed=28846083; DOI=10.1038/nn.4630;
RA Rapti G., Li C., Shan A., Lu Y., Shaham S.;
RT "Glia initiate brain assembly through noncanonical Chimaerin-Furin axon
RT guidance in C. elegans.";
RL Nat. Neurosci. 20:1350-1360(2017).
CC -!- FUNCTION: During ventral cord development, required for axon
CC fasciculation and navigation, mediating both pioneer and follower axon
CC extension, guidance and track formation (PubMed:20876647,
CC PubMed:22442082, PubMed:23376536, PubMed:28846083). Acts in CEPsh glia
CC and SubL neurons to guide follower axons into the nerve ring
CC (PubMed:28846083). Promotes motorneuron development by positively
CC regulating the extension of the anterior neurite of ventral D-type
CC GABAergic motorneurons along the anterior-posterior axis of the ventral
CC nerve cord (PubMed:23376536). Plays a role in synaptogenesis by
CC regulating synaptic vesicle accumulation at GABAergic and cholinergic
CC neuromuscular junctions (PubMed:22442082).
CC {ECO:0000269|PubMed:20876647, ECO:0000269|PubMed:22442082,
CC ECO:0000269|PubMed:23376536, ECO:0000269|PubMed:28846083}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}. Cell projection, axon
CC {ECO:0000269|PubMed:20876647}. Cell projection, dendrite
CC {ECO:0000269|PubMed:20876647}. Note=In embryos, localizes to axons in
CC the nerve ring, the tail and along dendrites of sensory neurons.
CC {ECO:0000269|PubMed:20876647}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:F15B9.7a};
CC IsoId=G5EDK5-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F15B9.7b};
CC IsoId=G5EDK5-2; Sequence=VSP_060646;
CC Name=c {ECO:0000312|WormBase:F15B9.7c};
CC IsoId=G5EDK5-3; Sequence=VSP_060645;
CC -!- TISSUE SPECIFICITY: Expressed in a region of neuropil around the nerve
CC ring and the ventral cord (at protein level) (PubMed:22442082).
CC Expressed in the head, tail, ventral cord, nerve ring and neurons
CC including HSN neurons (PubMed:20876647). Expressed in DA, VA, and VB
CC and weakly in the DB cholinergic neurons (PubMed:22442082). Not
CC expressed in ventral D-type GABAergic motorneurons (PubMed:22442082).
CC {ECO:0000269|PubMed:20876647, ECO:0000269|PubMed:22442082}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development
CC (PubMed:20876647). In embryos, first expressed in neuronal precursor
CC cells during gastrulation (PubMed:20876647). At the comma and 1.5-fold
CC embryonic stage, expressed in neurons in the head, the tail and along
CC the ventral cord (PubMed:20876647). In 1.5-fold stage embryos,
CC expressed in the nerve ring bundle (PubMed:28846083). At the L1 larval
CC stage, expressed in the ventral nerve cord and in a subset of dorsal D-
CC type GABAergic motorneurons (PubMed:22442082, PubMed:23376536). At the
CC L2 larval stage, expressed along the ventral nerve cord
CC (PubMed:23376536). Not expressed in ventral D-type GABAergic
CC motorneurons at the L2 larval stage (PubMed:23376536).
CC {ECO:0000269|PubMed:20876647, ECO:0000269|PubMed:22442082,
CC ECO:0000269|PubMed:23376536, ECO:0000269|PubMed:28846083}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
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DR EMBL; AY314773; AAQ84880.1; -; mRNA.
DR EMBL; BX284605; CAB01427.3; -; Genomic_DNA.
DR EMBL; BX284605; CTQ86770.1; -; Genomic_DNA.
DR EMBL; BX284605; CTQ86771.1; -; Genomic_DNA.
DR RefSeq; NP_001300071.1; NM_001313142.1. [G5EDK5-2]
DR RefSeq; NP_001300072.1; NM_001313143.1. [G5EDK5-3]
DR RefSeq; NP_506256.3; NM_073855.4. [G5EDK5-1]
DR AlphaFoldDB; G5EDK5; -.
DR SMR; G5EDK5; -.
DR IntAct; G5EDK5; 1.
DR STRING; 6239.F15B9.7; -.
DR EPD; G5EDK5; -.
DR PaxDb; G5EDK5; -.
DR PeptideAtlas; G5EDK5; -.
DR EnsemblMetazoa; F15B9.7a.1; F15B9.7a.1; WBGene00001475. [G5EDK5-1]
DR EnsemblMetazoa; F15B9.7b.1; F15B9.7b.1; WBGene00001475. [G5EDK5-2]
DR EnsemblMetazoa; F15B9.7c.1; F15B9.7c.1; WBGene00001475. [G5EDK5-3]
DR GeneID; 179788; -.
DR KEGG; cel:CELE_F15B9.7; -.
DR CTD; 179788; -.
DR WormBase; F15B9.7a; CE42459; WBGene00001475; fmi-1. [G5EDK5-1]
DR WormBase; F15B9.7b; CE50507; WBGene00001475; fmi-1. [G5EDK5-2]
DR WormBase; F15B9.7c; CE50392; WBGene00001475; fmi-1. [G5EDK5-3]
DR eggNOG; KOG4289; Eukaryota.
DR GeneTree; ENSGT00940000168029; -.
DR HOGENOM; CLU_231552_0_0_1; -.
DR InParanoid; G5EDK5; -.
DR OMA; EDTDERC; -.
DR OrthoDB; 23882at2759; -.
DR PhylomeDB; G5EDK5; -.
DR SignaLink; G5EDK5; -.
DR PRO; PR:G5EDK5; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001475; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; G5EDK5; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0033564; P:anterior/posterior axon guidance; IMP:WormBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0097376; P:interneuron axon guidance; IMP:UniProtKB.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF111418; SSF111418; 1.
DR SUPFAM; SSF49313; SSF49313; 9.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Neurogenesis;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..2596
FT /note="Cadherin EGF LAG seven-pass G-type receptor fmi-1"
FT /id="PRO_5015091945"
FT TOPO_DOM 23..2229
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2230..2250
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2251..2261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2262..2282
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2283..2292
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2293..2313
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2314..2326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2327..2347
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2348..2356
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2357..2377
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2378..2401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 2402..2422
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2423..2437
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2438..2458
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2459..2596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 166..270
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 271..375
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 376..479
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 480..581
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 582..682
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 683..784
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 785..892
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 893..1000
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1251..1287
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1333..1526
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1529..1568
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1577..1732
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1734..1771
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1776..1808
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2171..2218
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 824
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1030
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1965
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1992
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 1255..1266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1260..1275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1277..1286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1497..1526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 1533..1546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1540..1555
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1557..1567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1709..1732
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 1738..1750
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1744..1759
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1761..1770
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1780..1785
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1798..1807
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..1014
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060645"
FT VAR_SEQ 1..359
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060646"
FT MUTAGEN 725..2596
FT /note="Missing: In rh308; synaptic defects. Axon guidance
FT defects. In 81% of animals, the PVPR axon irregularly
FT crosses the ventral midline and joins the right axon track.
FT PVQ axons irregularly cross the ventral midline multiple
FT times and often stop prematurely before reaching the nerve
FT ring. In the majority of animals, HSN axon guidance is
FT disrupted along the ventral nerve cord (VNC) axon tracks
FT where HSN axons circle the vulva and HSN axons often
FT project to the posterior instead of the anterior side after
FT leaving the vulva region. HSN axons also often cross the
FT ventral midline outside the vulva region and the HSN axons
FT that extended along the VNC often stop before reaching the
FT nerve ring. Dorsal D-type and ventral D-type GABAergic
FT motorneurons erroneously guided axons into the left VNC
FT axon track. Guidance of the commissures of the dorsal D-
FT type and ventral D-type GABAergic and the cholinergic DA/DB
FT motoneurons were partially disrupted. Irregular midline
FT crossing of command interneuron axons. Defects in neurite
FT positioning along the anterior posterior axis with ventral
FT D-type GABAergic neurons displaying posterior neurites,
FT instead of anterior neurites, which results in ventrodorsal
FT commissures positioned on the posterior side of their cell
FT body. Defective guidance of the AIY axon into the nerve
FT ring, which impairs nerve ring assembly."
FT /evidence="ECO:0000269|PubMed:20876647,
FT ECO:0000269|PubMed:22442082, ECO:0000269|PubMed:23376536,
FT ECO:0000269|PubMed:28846083"
FT MUTAGEN 842
FT /note="G->R: In gm188; synaptic defects. HSN axon guidance
FT defects. Does not display PVP axon guidance defects."
FT /evidence="ECO:0000269|PubMed:20876647,
FT ECO:0000269|PubMed:22442082"
FT MUTAGEN 1481
FT /note="G->E: In ju43; synaptic defects caused by disrupted
FT neuromuscular junction formation whereby aberrantly shaped
FT and enlarged snb-1-positive synaptic vesicles abnormally
FT cluster at GABAergic and cholinergic neuromuscular
FT junctions. Defective snb-1-positive vesicle clustering is
FT more severe at GABAergic neuromuscular junctions. PVP and
FT HSN axon guidance defects. Does not display PVQ axon
FT guidance defects."
FT /evidence="ECO:0000269|PubMed:20876647,
FT ECO:0000269|PubMed:22442082"
FT MUTAGEN 2150..2596
FT /note="Missing: In ju58; synaptic defects caused by
FT disrupted neuromuscular junction formation whereby
FT aberrantly shaped and enlarged snb-1-positive synaptic
FT vesicles abnormally cluster at dorsal D-type and ventral D-
FT type GABAergic and cholinergic neuromuscular junctions.
FT Defective snb-1-positive vesicle clustering is more severe
FT at GABAergic neuromuscular junctions. Incomplete axon
FT extension of dorsal D-type GABAergic motorneurons.
FT GABAergic motorneurons exit the ventral cord on the
FT incorrect side and have defects in axon extension."
FT /evidence="ECO:0000269|PubMed:22442082"
FT MUTAGEN 2184..2596
FT /note="Missing: In hd121; axon guidance defects."
FT /evidence="ECO:0000269|PubMed:20876647"
SQ SEQUENCE 2596 AA; 288351 MW; 659A425FDD3C73BC CRC64;
MMLDRIMFLL FFILSLVIGS FSEYLDDKYY STNSIDVVCK PCAVPSSNSV IWLPASRPPC
LHPGQPIIHW PDLSDNLACP VPGLPDSVHS SQISLLEGEG LLLTKERICF FDGPIDFHYD
YVCDGKLYRS KMRIGHSIAS KKKLETRRTK RWARRRNPDA NAVHFQQEKY VKELPEDTPI
ETIIASVKAS HASSQPLYYS MVAPQDSRSQ NLFTLDTMSG EIRLAKSMDR EVLDKHILKV
TAYERVDPTI SASTTVVVHV LDVQDNSPIF EKDSYFGEIR EDAPIGTTVL SVFARDLDSG
ENGEIEYSLG EGNGKNLLAI NAKSGVIQTA APLDRETLSL IRLDVIASDK GTPKRESTAM
VEITVVDVND NAPVFASDSY NVTILENITI PAVIATVKAT DEDFGTNGKV HYSMASSSGI
GGLTIDYSTG EVTLRERIDA KNSPITAVIR AKDGAQPALS STVPLTINVI DINDHAPTLI
AAQKMITLEE NVAIGEEVGR VYAIDEDSGP NGIIKYSMEG SEDFIIDEDS GLIKTTKLLD
RETTARYSLK VTARDMGTPS LNTSTTIAVV LKDINDNAPT FDKKEYNVTI SEEMPRGSQI
ITLKAVDNDE DQKITYRIEE ADREVFSILD IGDQGAILSV SGELKRQDHK VRVEISATDQ
GGLQGRCVVN VFIDDVNSAP YFNDHPFSVK IPEHSPIGYP VITLKAEDHD RGDNARIVYS
IDSSQFFRID PSSGDISVSS DLDREDRATF SVIVTASDHA SPPLNTSTQI EVILDDINDN
SPQFTSSSYA ATISEDIPVG TSFLQVSAID ADIGPNGIVD YFLNESSSSP SIQLFRLDRT
SGTLRVSSKL DREQFAVIVL PIFARDRGTP SLSAASEITL TLSDVNDNAP TFEQLSYDLY
IAENSPVGST VGTIVARDAD EGDNADISFR IFGGADAKLF DIEEDAEQNG VVRILTRAEF
DYEAKANKFF FELQASSGQL SSTVPVRIHV SDVNDNKPAL KDFVILMNRF DNVQMARQIG
FIPAFDPDQN ATLEYFLEEN DLIEAEKYTG KILVKQEWKR NMDVSFKTCV SDGANTECST
CRFIHVLVEP EWLSESFTLS LARMTVDDFW DPLVFQRFRD AMSTLSNWKP SDIHVIGVKQ
HLDDVIYINI AITDHGRVVR GWRAIELVKE SIKKLEKMTL LQVEVIRDES CANEPCSHMA
KCRQTQKFVG EMKAHETDNF IARTLNTVNT FVCECPSGFT SSGAHGDCDT RIDECYRGRC
SNNSTCVAFE NTYQCECKPG WIGRHCEISV HALTCVPGYC MSDSLCELDG NQMKCRHCKY
HGEDTDERCR LRSVSFDGEG LLNVNLDLPR TQWTMKFRVS TIAHNGVLVF TGDKRSDFVE
VSVVDRVLKV QFSLGGEKID AKMENDVENR INDGEWHTVA LEYSNKQITM SLDDCETNPS
LLLNTSPNCA IRAKLNLEKK CEDPTVPCYR YLDISNGLFL GGRPGTSKQI EKAFSGCISD
LSVDKEDVDF STIKEMHKVG QVHEGCKHRK DFCSTSDGQC SATSKCVNRW GGRICSCPQS
VHSTGECVGA LGTQDLRGHS LFEEESFVLY QPSQVSVPFE VSFEFRTSRA DMQVFALEFT
QRSVHYNLEV DDGTLKYNIG DSEVELPAPE VTSKHWMNVV IKFEADSVAT SINGIYSAEA
KASISDMNLE SLYFGIAPGT GHPSRFEGCI RNVLVDGRSI SVKKKGKTRA GCVVPNRCSV
DSICPAESTC HRAWNKHKCK CHKSFVGDTC LPVCSVANVC SSGTCVSSNT TAGYECICPA
GKTGKNCQLE APKQMCPSGW WGTFPRCRRC SCAQTKDYEA QCDKKTGACQ CKKSHFSTIN
GCVKCECGFG ADSTECSADG HCKCNGDAVG RRCDRCSRFD HQLDSKTLKC RPVSGKCPSE
IEYSIQWPAS QKGSIVRQSC PVGESGLATR KCLETGRWSD VNAWNCTRPE YSIMVNKFEI
LEPSKLLTMV ANATNTESSI RGRNQQIAAE ALSRLVDYEQ SMPMKGRAHI KDMKFTEKLI
ESLGRVMSEQ PADEYSTLIS KLWNYAETVA EIHENVNFLS PFFVANDHIV FASDKLDFGN
ILPKFNNFVD LRPTGFPRVR AIVTGTTQVV YSIVPYPRCN RCENPMIAIV ANTSDPVIVE
FEIEEDDGWK YPECVRFDEK SGTWTARGAA LIGLNLTHAA CEYNRIGVFT MFVNDQSSSI
VRVAQMDNMT SPAIAGVALF LCFLSILLTL SRRSLKTHSV RIGFILFFAI NILNLFFVHK
TAINQAYCPV RNAMLSFTSS APFAWLFLYG LYIYRMLADG SSSPSLTTSL LVGIVFPCLI
SFTTFFVTDQ CSLSPHLWLF WCIILPIGLF LLLSFYAAAT SVLVSLHKKY DVFVAKYNVK
RAVFQHFILT IFTLGMTLTG LFANQLPLPM EIMEISQSII YLIAALVIFL WCVCDITTKA
SDSNPSMWLD NQKSVMAEST MADPQCASPL LSPRHQHHEV PMDSEWVPDV NPSNHYHTSI
NEPDTPRRLL LPQNRDVINI LSSPDQILNE GVGHVYRNNM GSLPRLRSAQ DEADDAYYTY
TASRKYKNTT STFNRE
