RIG3_CAEEL
ID RIG3_CAEEL Reviewed; 487 AA.
AC Q18806;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Neuronal immunoglobulin domain-containing protein rig-3 {ECO:0000305};
DE Flags: Precursor;
GN Name=rig-3 {ECO:0000312|WormBase:C53B7.1};
GN ORFNames=C53B7.1 {ECO:0000312|WormBase:C53B7.1};
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|Proteomes:UP000001940}
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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP GPI-ANCHOR AT ASP-466, AND MUTAGENESIS OF 465-MET--ILE-487.
RX PubMed=21745641; DOI=10.1016/j.neuron.2011.05.034;
RA Babu K., Hu Z., Chien S.C., Garriga G., Kaplan J.M.;
RT "The immunoglobulin super family protein RIG-3 prevents synaptic
RT potentiation and regulates Wnt signaling.";
RL Neuron 71:103-116(2011).
CC -!- FUNCTION: Cell surface protein which plays a role in the plasticity of
CC cholinergic synapses at neuromuscular junctions and in the polarity of
CC the mechanosensory neuron ALM, possibly by antagonizing Wnt signaling.
CC {ECO:0000269|PubMed:21745641}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:21745641}. Synapse {ECO:0000269|PubMed:21745641}.
CC Cell membrane {ECO:0000269|PubMed:21745641}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:21745641}. Note=Membrane association is important
CC for synaptic function. {ECO:0000269|PubMed:21745641}.
CC -!- TISSUE SPECIFICITY: Expressed in the cholinergic motor neurons AS, VA
CC and DA in the ventral nerve cord and in the mechanosensory ALM neurons
CC in the midbody. {ECO:0000269|PubMed:21745641}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in
CC hypersensitivity to the acetylcholinesterase inhibitor aldicarb,
CC indicating increased cholinergic transmission in mutant animals.
CC {ECO:0000269|PubMed:21745641}.
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DR EMBL; BX284606; CCD67885.1; -; Genomic_DNA.
DR PIR; T28804; T28804.
DR RefSeq; NP_509155.1; NM_076754.4.
DR AlphaFoldDB; Q18806; -.
DR STRING; 6239.C53B7.1; -.
DR EPD; Q18806; -.
DR PaxDb; Q18806; -.
DR PeptideAtlas; Q18806; -.
DR EnsemblMetazoa; C53B7.1.1; C53B7.1.1; WBGene00004370.
DR GeneID; 180958; -.
DR KEGG; cel:CELE_C53B7.1; -.
DR UCSC; C53B7.1.2; c. elegans.
DR CTD; 180958; -.
DR WormBase; C53B7.1; CE06971; WBGene00004370; rig-3.
DR eggNOG; KOG3510; Eukaryota.
DR HOGENOM; CLU_561681_0_0_1; -.
DR InParanoid; Q18806; -.
DR OMA; FRISCIC; -.
DR OrthoDB; 588228at2759; -.
DR PhylomeDB; Q18806; -.
DR Reactome; R-CEL-1474228; Degradation of the extracellular matrix.
DR Reactome; R-CEL-210991; Basigin interactions.
DR Reactome; R-CEL-216083; Integrin cell surface interactions.
DR Reactome; R-CEL-376172; DSCAM interactions.
DR Reactome; R-CEL-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR Reactome; R-CEL-433692; Proton-coupled monocarboxylate transport.
DR Reactome; R-CEL-70268; Pyruvate metabolism.
DR Reactome; R-CEL-9749641; Aspirin ADME.
DR PRO; PR:Q18806; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004370; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR043204; Basigin-like.
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; IPR013151; Immunoglobulin.
DR PANTHER; PTHR10075; PTHR10075; 2.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Signal; Synapse.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..466
FT /note="Neuronal immunoglobulin domain-containing protein
FT rig-3"
FT /evidence="ECO:0000255"
FT /id="PRO_5004186920"
FT PROPEP 467..487
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:21745641"
FT /id="PRO_0000440240"
FT DOMAIN 34..139
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 247..354
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT LIPID 466
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000305|PubMed:21745641"
FT DISULFID 61..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 271..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 465..487
FT /note="Missing: Reduced axonal localization and increased
FT coelomocyte expression, indicating shedding into the body
FT cavity."
FT /evidence="ECO:0000269|PubMed:21745641"
SQ SEQUENCE 487 AA; 54615 MW; C6B8F2DF0705664F CRC64;
MGRLLAKMLF PLAMCLFVSA VSASDSPSSN EANPIVISSE AMDYDTNTIT VREGKKLMVS
CVFESDEQIH KSDLLWKQAN GNNIDGESNP SLFSVILNEK GSKHRKTSLH FSSVHTRDTG
LYTCTGRTAG GENFEKTIKL VVLPAIEWND KDTVKGALLG EPITIDCGVK GPSGKEPMIQ
MTNGNGEPLD EEIWTIAGNE ATIDSLKKEH AELTVSCITI EMHQETSKEE FPVVDRKDVN
IEVYTLPEFE TEESVQYTVI DNHVRDAIIY CNVTHSFPPV RHYTFYHGDE EIKMSDKFNI
FVNVGVSQGA HLKIHNVNEN DLGTYKCEAN NIKAKSYHTI HLREANAPAE PKVTLIEDKR
HSIIWKVESI DRDPDLPMTA VEIRHLRAGT AEASGVSDED ISDAYWKSHS IFMQRNIKDD
GIYEINGLRH GHEYVWRFRQ INEAGFGDSV VLRAKTLDDH DLEMMDSASD SKFPLALATL
FFVCLFI
