OIG4_CAEEL
ID OIG4_CAEEL Reviewed; 155 AA.
AC Q5WRU0;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Immunoglobulin domain-containing protein oig-4 {ECO:0000305};
DE Flags: Precursor;
GN Name=oig-4 {ECO:0000312|WormBase:R07G3.9};
GN ORFNames=R07G3.9 {ECO:0000312|WormBase:R07G3.9};
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 {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 [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH UNC-29 AND LEV-10, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-84.
RX PubMed=21252855; DOI=10.1038/emboj.2010.355;
RA Rapti G., Richmond J., Bessereau J.L.;
RT "A single immunoglobulin-domain protein required for clustering
RT acetylcholine receptors in C. elegans.";
RL EMBO J. 30:706-718(2011).
CC -!- FUNCTION: Required for the localization of acetylcholine receptors at
CC neuromuscular junctions and for subsequently controlling the response
CC evoked by receptor stimulation. {ECO:0000269|PubMed:21252855}.
CC -!- SUBUNIT: Interacts with the non-alpha subunit of nicotinic
CC acetylcholine receptor unc-29 and lev-10 to stabilize the complex
CC formed between unc-29 and lev-10. {ECO:0000269|PubMed:21252855}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:21252855}. Secreted
CC {ECO:0000269|PubMed:21252855}. Note=Secreted by body wall cells. Co-
CC localizes with and requires acetylcholine receptors for localization at
CC neuromuscular junctions. {ECO:0000269|PubMed:21252855}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscle cells, the pharyngeal
CC muscle cell pm6 and in four head neurons.
CC {ECO:0000269|PubMed:21252855}.
CC -!- DISRUPTION PHENOTYPE: Disrupted localization of levamisole-sensitive
CC nicotinic acetylcholine receptor subunits in 80% of mutants, and this
CC is mostly in conjunction with the disrupted localization of the
CC associated transmembrane protein lev-10 and secreted protein lev-9.
CC This results in increased sensitivity to the acetylcholine agonist
CC levamisole. {ECO:0000269|PubMed:21252855}.
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DR EMBL; BX284602; CCD70521.1; -; Genomic_DNA.
DR RefSeq; NP_001022278.1; NM_001027107.4.
DR AlphaFoldDB; Q5WRU0; -.
DR SMR; Q5WRU0; -.
DR IntAct; Q5WRU0; 2.
DR MINT; Q5WRU0; -.
DR STRING; 6239.R07G3.9; -.
DR PaxDb; Q5WRU0; -.
DR EnsemblMetazoa; R07G3.9.1; R07G3.9.1; WBGene00043050.
DR GeneID; 259448; -.
DR KEGG; cel:CELE_R07G3.9; -.
DR UCSC; R07G3.9; c. elegans.
DR CTD; 259448; -.
DR WormBase; R07G3.9; CE37545; WBGene00043050; oig-4.
DR eggNOG; ENOG502RYK7; Eukaryota.
DR GeneTree; ENSGT00970000196744; -.
DR HOGENOM; CLU_120649_0_0_1; -.
DR InParanoid; Q5WRU0; -.
DR OMA; ICKARGD; -.
DR OrthoDB; 1418131at2759; -.
DR PhylomeDB; Q5WRU0; -.
DR PRO; PR:Q5WRU0; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00043050; Expressed in larva and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:WormBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:WormBase.
DR Gene3D; 2.60.40.10; -; 1.
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 SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Reference proteome;
KW Secreted; Signal; Synapse.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..155
FT /note="Immunoglobulin domain-containing protein oig-4"
FT /evidence="ECO:0000305"
FT /id="PRO_5004263494"
FT DOMAIN 73..154
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 80..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 84
FT /note="G->R: In kr39; the mutant protein is intracellularly
FT retained in body wall muscle cells and not localized to
FT neuromuscular junctions."
FT /evidence="ECO:0000269|PubMed:21252855"
SQ SEQUENCE 155 AA; 17556 MW; 01EE06255415CA0A CRC64;
MSFRLWGRCI FFFCFLLEAI DSRGGRRGGK GKGKSNLQFA QVAEFSLVQT VLSDNRSAQI
ITGSHFSQTY RLGYKLLIIC KARGDPRPTI KWYKEGAEIQ PKASIHYYEK PIENDTIWSK
LEVDPATMGD QGVYACVANN PHGVMAKNFK AEYTY
