FKPC1_CAEEL
ID FKPC1_CAEEL Reviewed; 692 AA.
AC O17798; O17797; Q17325;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Furin-like protease kpc-1 {ECO:0000303|PubMed:23932402};
DE EC=3.4.21.- {ECO:0000305|PubMed:24671950};
DE AltName: Full=CelfurPC protein {ECO:0000303|PubMed:9174171};
DE Flags: Precursor;
GN Name=kpc-1 {ECO:0000312|WormBase:F11A6.1a};
GN ORFNames=F11A6.1 {ECO:0000312|WormBase:F11A6.1a};
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 [MRNA].
RC STRAIN=BA713;
RX PubMed=9174171; DOI=10.1089/dna.1997.16.663;
RA Gomez-Saladin E., Luebke A.E., Wilson D.L., Dickerson I.M.;
RT "Isolation of a cDNA encoding a Kex2-like endoprotease with homology to
RT furin from the nematode Caenorhabditis elegans.";
RL DNA Cell Biol. 16:663-669(1997).
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF PRO-440.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:23932402};
RX PubMed=23932402; DOI=10.1016/j.cub.2013.06.058;
RA Schroeder N.E., Androwski R.J., Rashid A., Lee H., Lee J., Barr M.M.;
RT "Dauer-specific dendrite arborization in C. elegans is regulated by KPC-
RT 1/Furin.";
RL Curr. Biol. 23:1527-1535(2013).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=24671950; DOI=10.1242/dev.103846;
RA Hung W.L., Wang Y., Chitturi J., Zhen M.;
RT "A Caenorhabditis elegans developmental decision requires insulin
RT signaling-mediated neuron-intestine communication.";
RL Development 141:1767-1779(2014).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-263 AND ARG-265.
RX PubMed=25232734; DOI=10.1371/journal.pgen.1004657;
RA Salzberg Y., Ramirez-Suarez N.J., Buelow H.E.;
RT "The proprotein convertase KPC-1/furin controls branching and self-
RT avoidance of sensory dendrites in Caenorhabditis elegans.";
RL PLoS Genet. 10:E1004657-E1004657(2014).
RN [6]
RP FUNCTION, INTERACTION WITH DMA-1, DISRUPTION PHENOTYPE, PROTEOLYTIC
RP CLEAVAGE, AND MUTAGENESIS OF ARG-136; ARG-143 AND PRO-440.
RX PubMed=26974341; DOI=10.7554/elife.11008;
RA Dong X., Chiu H., Park Y.J., Zou W., Zou Y., Oezkan E., Chang C., Shen K.;
RT "Precise regulation of the guidance receptor DMA-1 by KPC-1/Furin instructs
RT dendritic branching decisions.";
RL Elife 5:0-0(2016).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF SER-579.
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: Furin-like protease which cleaves proproteins at the RX(K/R)R
CC consensus motif (PubMed:24671950). During neuronal development,
CC regulates the formation and extension of dendrite branches and cellular
CC positioning of various type of neurons (PubMed:23932402,
CC PubMed:25232734, PubMed:26974341, PubMed:28846083). Together with chin-
CC 1 and cdc-42, plays a role in the development of the neuropil and is
CC required for the guidance of axons from neurons, including SubL pioneer
CC neurons and AIY interneurons, into the nerve ring (PubMed:28846083).
CC Its role in axon guidance in glia and pioneer neurons may be through
CC ensuring the fmi-1 protein is correctly localized to the nerve ring
CC (PubMed:28846083). Promotes the formation, extension and self-avoidance
CC of dendritic branches of PVD and FLP mechanosensory neurons
CC (PubMed:23932402, PubMed:25232734, PubMed:26974341). In PVD neurons,
CC regulates plasma membrane levels of branching receptor dma-1 by
CC targeting it to late endosomes and thus promotes normal dendrite
CC branching and dendrite self-avoidance (PubMed:26974341). Also controls
CC dendrite extension in AIY and D-type motoneurons, dendrite branching in
CC AQR sensory neurons and VC4/5 motoneurons, the normal number of
CC dendritic branches in AVL neurons and the positioning of HSN and
CC ALM/PLM neurons (PubMed:25232734). Dispensable for maintaining dendrite
CC branching in adults (PubMed:25232734). Also regulates dauer-specific
CC dendritic branching of IL2 neurons and dauer-specific nictation
CC behavior (PubMed:23932402). Under adverse environmental conditions, may
CC promote dauer formation by processing insulin-like proteins ins-1 and
CC ins-18, two daf-2/InsR antagonists (PubMed:24671950).
CC {ECO:0000269|PubMed:23932402, ECO:0000269|PubMed:24671950,
CC ECO:0000269|PubMed:25232734, ECO:0000269|PubMed:26974341,
CC ECO:0000269|PubMed:28846083}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P09958};
CC Note=Binds 3 calcium ions per subunit. {ECO:0000250|UniProtKB:P09958};
CC -!- SUBUNIT: Interacts (via extracellular domain) with receptor dma-1 (via
CC extracellular domain); the interaction promotes dma-1 internalization.
CC {ECO:0000269|PubMed:26974341}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:26974341};
CC Single-pass type I membrane protein {ECO:0000305}. Perikaryon
CC {ECO:0000269|PubMed:23932402}. Cell projection, axon
CC {ECO:0000269|PubMed:23932402}. Note=In most neurons, localizes
CC exclusively within the cell bodies, but in ventral cord neurons,
CC localizes in both the neuronal cell bodies and processes.
CC {ECO:0000269|PubMed:23932402}.
CC -!- TISSUE SPECIFICITY: Expressed in the nervous system including the
CC ventral nerve cord, the nerve ring and the retrovesicular ganglion, and
CC in epithelial cells (PubMed:23932402, PubMed:24671950,
CC PubMed:25232734). Expressed in IL2 neurons (PubMed:23932402). Expressed
CC in PVD mechanosensory neurons (PubMed:25232734). Expressed in pharynx
CC with strong expression in the g2 pharyngeal gland cells and vpi
CC pharyngeal intestinal valve cells (PubMed:23932402, PubMed:25232734).
CC Expressed in intestine (PubMed:24671950). {ECO:0000269|PubMed:23932402,
CC ECO:0000269|PubMed:24671950, ECO:0000269|PubMed:25232734}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults
CC (PubMed:25232734). Broadly expressed in embryos (PubMed:28846083).
CC Expressed broadly in neuronal and epithelial cells throughout the head
CC during the dauer stage (PubMed:23932402). {ECO:0000269|PubMed:23932402,
CC ECO:0000269|PubMed:25232734, ECO:0000269|PubMed:28846083}.
CC -!- DISRUPTION PHENOTYPE: Several defects in neuron development
CC (PubMed:25232734, PubMed:26974341). In PVD mechanosensory neurons,
CC tertiary and quaternary branching is decreased, secondary and ectopic
CC tertiary branching is increased, the length of dendritic branches is
CC also reduced and branches tend to overlap (PubMed:25232734,
CC PubMed:26974341). Secondary dendrite branches are trapped next to
CC primary branches (PubMed:26974341). In a sax-7 (nj48) or dma-1 (wy686)
CC mutant background, significantly less secondary dendrites are trapped
CC (PubMed:26974341). Increased dma-1 protein levels in PVD neuron
CC dendrites (PubMed:26974341). In addition, abnormal dendrite branches in
CC FLP neurons, reduced axonal extension in AIY interneurons, abnormal
CC positioning of touch receptor ALM and HSN motoneuron, formation of
CC ectopic branching in AVL, loss of sensory AQR branching in the nerve
CC ring, and impaired extension and formation of branches near the vulva
CC in VC4/5 motoneurons (PubMed:26974341). RNAi-mediated knockdown at the
CC L1 larval stage but not at the L4 larval stage causes defects in the
CC dendritic branching of PVD neurons (PubMed:26974341).
CC {ECO:0000269|PubMed:25232734, ECO:0000269|PubMed:26974341}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000255}.
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DR EMBL; U12682; AAB63525.1; -; mRNA.
DR EMBL; BX284601; CAB04086.1; -; Genomic_DNA.
DR PIR; T20759; T20759.
DR PIR; T20760; T20760.
DR RefSeq; NP_492974.2; NM_060573.5.
DR AlphaFoldDB; O17798; -.
DR SMR; O17798; -.
DR BioGRID; 38457; 2.
DR STRING; 6239.F11A6.1b; -.
DR MEROPS; S08.047; -.
DR EPD; O17798; -.
DR PaxDb; O17798; -.
DR PeptideAtlas; O17798; -.
DR EnsemblMetazoa; F11A6.1a.1; F11A6.1a.1; WBGene00002232.
DR EnsemblMetazoa; F11A6.1a.2; F11A6.1a.2; WBGene00002232.
DR GeneID; 173051; -.
DR KEGG; cel:CELE_F11A6.1; -.
DR UCSC; F11A6.1a.2; c. elegans.
DR CTD; 173051; -.
DR WormBase; F11A6.1a; CE17653; WBGene00002232; kpc-1.
DR GeneTree; ENSGT00940000167869; -.
DR HOGENOM; CLU_002976_4_1_1; -.
DR InParanoid; O17798; -.
DR OMA; FREWAFM; -.
DR OrthoDB; 473018at2759; -.
DR PhylomeDB; O17798; -.
DR BRENDA; 3.4.21.75; 1045.
DR Reactome; R-CEL-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-CEL-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR Reactome; R-CEL-186797; Signaling by PDGF.
DR PRO; PR:O17798; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002232; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:WormBase.
DR GO; GO:0070593; P:dendrite self-avoidance; IMP:UniProtKB.
DR GO; GO:0010467; P:gene expression; IMP:UniProtKB.
DR GO; GO:0030070; P:insulin processing; IMP:WormBase.
DR GO; GO:1905910; P:negative regulation of dauer entry; IGI:UniProtKB.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:0016486; P:peptide hormone processing; IBA:GO_Central.
DR GO; GO:1900006; P:positive regulation of dendrite development; IMP:UniProtKB.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IMP:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IGI:UniProtKB.
DR GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:1903859; P:regulation of dendrite extension; IGI:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IGI:UniProtKB.
DR GO; GO:2001222; P:regulation of neuron migration; IMP:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; IMP:UniProtKB.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 3.30.70.850; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16470; S8_pro-domain; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cell projection;
KW Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Metal-binding; Protease; Reference proteome;
KW Serine protease; Signal; Transmembrane; Transmembrane helix; Zymogen.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..139
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT /id="PRO_0000430490"
FT CHAIN 140..692
FT /note="Furin-like protease kpc-1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT /id="PRO_0000430491"
FT TOPO_DOM 140..670
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 671..692
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 182..503
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 512..646
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT REGION 152..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 570..572
FT /note="Cell attachment site"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00293"
FT COMPBIAS 152..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 262
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 436
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 259..260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 321..326
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 360..363
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 369
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 374
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT BINDING 436
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09958"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 279..428
FT /evidence="ECO:0000250|UniProtKB:P23188"
FT DISULFID 371..401
FT /evidence="ECO:0000250|UniProtKB:P23188"
FT DISULFID 518..544
FT /evidence="ECO:0000250|UniProtKB:P23188"
FT MUTAGEN 136
FT /note="R->A: In wy1060; loss of propeptide cleavage,
FT trapped secondary dendrite branches and loss of tertiary
FT and quaternary dendrite branches; when associated with A-
FT 143."
FT /evidence="ECO:0000269|PubMed:26974341"
FT MUTAGEN 143
FT /note="R->A: In wy1060; loss of propeptide cleavage,
FT trapped secondary dendrite branches and loss of tertiary
FT and quaternary dendrite branches; when associated with A-
FT 136."
FT /evidence="ECO:0000269|PubMed:26974341"
FT MUTAGEN 263
FT /note="G->R: In gk(779937); increased secondary dendritic
FT branches in PVD neurons."
FT /evidence="ECO:0000269|PubMed:25232734"
FT MUTAGEN 265
FT /note="R->Q: In gk(333538); normal secondary dendritic
FT branches in PVD neurons."
FT /evidence="ECO:0000269|PubMed:25232734"
FT MUTAGEN 265
FT /note="R->W: In dz185; increased secondary dendritic
FT branches in PVD neurons."
FT /evidence="ECO:0000269|PubMed:25232734"
FT MUTAGEN 440
FT /note="P->L: In my24; highly disorganized and truncated
FT dauer-specific branching of the IL2Q neuron and
FT disorganized and truncated branching of the PVD and FLP
FT neurons in adults."
FT /evidence="ECO:0000269|PubMed:23932402"
FT MUTAGEN 440
FT /note="P->S: In xr58; partial trapping of secondary
FT dendrite branches next to primary dendrite branches. Forms
FT tertiary and quaternary branches but with substantial
FT overlap between tertiary dendrite branches. Increased dma-1
FT protein levels in PVD neuron dendrites."
FT /evidence="ECO:0000269|PubMed:26974341"
FT MUTAGEN 579
FT /note="S->T: In ns623; uncoordinated movements in a chin-1
FT ns399 mutant background. Impaired nerve ring assembly due
FT to follower axons of neurons including the amphid-
FT commissure neuron (AFD), and the non-commissural
FT interneurons AIY and PVQ, failing to extend dorsally and
FT enter the nerve ring. SubL pioneer axons enter the nerve
FT ring, but exhibit fasciculation defects."
FT /evidence="ECO:0000269|PubMed:28846083"
FT CONFLICT 205
FT /note="A -> V (in Ref. 1; AAB63525)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 77125 MW; B5F17DDF22BA3311 CRC64;
MSNISWYRHC SVRLQLVTLA LFLLLGSASL GSAHIDEEFE DDVTTTISSI ASPMRRTYTN
EWAVRIAGGK VEEANRLANK YGYTNLGPII PGDEYYLFRD DRKKSRSSRK TRSLSANQLQ
HEEDVMWMEQ QVAKRRVKRG YRRIRRHTDD NDIFEEDDDG TQISKSRNRK HPDPNDPLWT
DMWYLNRGEH HSDSTTRMDH NVKEAWDLGY TGKGVVVTIL DDGLERTHPD ISPNYDERAS
YDVNDRDNDP MPRYEFSDEN RHGTRCAGEV AAIFNNSLCI VGIAYNANIG GIRMLDGDVT
DAVEAASVGH NADYIDIYSA SWGPDDDGRT VDGPAKLTRS AFEKGITMGR KGKGSIFVWA
SGNGGKDADS CNCDGYTNSI YTLSISSATE NGNIPWYSEA CSSTLATTYS SGATGEKMIL
TTDLHHACTN MHTGTSASAP LAAGIVALAL EANPNLTWRD LQHIVIRTAK PINLRAGDWT
TNGVGRNVSH SFGYGLMDAG AMVKLAKIWK KVDEQHRCRQ FYPSRYKNIP NGNRLQLQLY
SDGCYGGADE NKVSYVEHVQ AIVTLKAPKR GDLQIYLTSP SGTKSTLLTK RARDTSRSGF
TDWAFMTTHN WGEQAAGLWI LEIDNDGWDD AELVKWELVL YGTDRETGDF GGQHASPLAV
RSVQMEATSS GTQYSIFHVI TLVILTFSQI LY
