INX3_CAEEL
ID INX3_CAEEL Reviewed; 420 AA.
AC Q19746; Q17393;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Innexin-3;
DE AltName: Full=Protein opu-3;
GN Name=inx-3 {ECO:0000312|WormBase:F22F4.2};
GN Synonyms=opu-3 {ECO:0000312|WormBase:F22F4.2};
GN ORFNames=F22F4.2 {ECO:0000312|WormBase:F22F4.2};
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].
RX PubMed=8707836; DOI=10.1083/jcb.134.2.537;
RA Starich T.A., Lee R.Y., Panzarella C., Avery L., Shaw J.E.;
RT "eat-5 and unc-7 represent a multigene family in Caenorhabditis elegans
RT involved in cell-cell coupling.";
RL J. Cell Biol. 134:537-548(1996).
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 CHARACTERIZATION.
RX PubMed=10381394; DOI=10.1242/jcs.112.14.2391;
RA Landesman Y., White T.W., Starich T.A., Shaw J.E., Goodenough D.A.,
RA Paul D.L.;
RT "Innexin-3 forms connexin-like intercellular channels.";
RL J. Cell Sci. 112:2391-2396(1999).
RN [4]
RP FUNCTION, INTERACTION WITH F-ACTIN, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=33238150; DOI=10.1016/j.devcel.2020.10.020;
RA Meng L., Yan D.;
RT "NLR-1/CASPR Anchors F-Actin to Promote Gap Junction Formation.";
RL Dev. Cell 55:574-587(2020).
CC -!- FUNCTION: Structural component of gap junctions (PubMed:10381394,
CC PubMed:33238150). Plays a role in maintaining gap junction activity to
CC promote phayngeal muscle contraction (PubMed:33238150).
CC {ECO:0000269|PubMed:10381394, ECO:0000269|PubMed:33238150}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000269|PubMed:33238150}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC junction {ECO:0000269|PubMed:33238150}. Note=Partially co-localizes
CC with F-actin at gap junctions between EA and EP endodermal precursor
CC cells in embryos. {ECO:0000269|PubMed:33238150}.
CC -!- TISSUE SPECIFICITY: Evenly distributed along the adjoining membranes of
CC the two pm5 pharyngeal muscle cells. {ECO:0000269|PubMed:33238150}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis (PubMed:33238150).
CC Expressed in EA and EP endodermal precursor cells at the 16-24 cell
CC stage of embryogenesis (PubMed:33238150).
CC {ECO:0000269|PubMed:33238150}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown impairs gap junction
CC function in pharyngeal muscles which disrupts the synchronized muscle
CC contraction between the pharyngeal metacorpus and terminal bulbs and
CC thereby decreases the pharyngeal pumping rate.
CC {ECO:0000269|PubMed:33238150}.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
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DR EMBL; U59211; AAB09670.1; -; mRNA.
DR EMBL; BX284606; CCD63822.1; -; Genomic_DNA.
DR PIR; T16141; T16141.
DR RefSeq; NP_509002.2; NM_076601.6.
DR AlphaFoldDB; Q19746; -.
DR SMR; Q19746; -.
DR BioGRID; 45798; 1.
DR IntAct; Q19746; 1.
DR MINT; Q19746; -.
DR STRING; 6239.F22F4.2; -.
DR TCDB; 1.A.25.1.1; the gap junction-forming innexin (innexin) family.
DR EPD; Q19746; -.
DR PaxDb; Q19746; -.
DR PeptideAtlas; Q19746; -.
DR EnsemblMetazoa; F22F4.2.1; F22F4.2.1; WBGene00002125.
DR GeneID; 180866; -.
DR KEGG; cel:CELE_F22F4.2; -.
DR UCSC; F22F4.2; c. elegans.
DR CTD; 180866; -.
DR WormBase; F22F4.2; CE33055; WBGene00002125; inx-3.
DR eggNOG; KOG3883; Eukaryota.
DR HOGENOM; CLU_035763_0_1_1; -.
DR InParanoid; Q19746; -.
DR OMA; GHHEHLY; -.
DR OrthoDB; 738314at2759; -.
DR PhylomeDB; Q19746; -.
DR PRO; PR:Q19746; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002125; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005921; C:gap junction; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005243; F:gap junction channel activity; IMP:UniProtKB.
DR GO; GO:0055077; F:gap junction hemi-channel activity; ISS:UniProtKB.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:WormBase.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:1903746; P:positive regulation of pharyngeal pumping; IMP:UniProtKB.
DR InterPro; IPR000990; Innexin.
DR PANTHER; PTHR11893; PTHR11893; 1.
DR Pfam; PF00876; Innexin; 1.
DR PRINTS; PR01262; INNEXIN.
DR PROSITE; PS51013; PANNEXIN; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Gap junction; Ion channel; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..420
FT /note="Innexin-3"
FT /id="PRO_0000208506"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT REGION 378..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 48917 MW; 8B8B6E65924966B1 CRC64;
MLGVPFIDRW LSETFKPKTF DDAVDRLSYV TTATLLAFFS IMVSCKQYVG SAIQCWMPME
FKGGWEQYAE DYCFIQNTFF IPERSEIPGD VEDRQKAEIG YYQWVPIVLA IQAFMFYLPS
WIWSSLYKQC GLDFPSVISE AEALRSQDSE TRTKGVNKLV DFIGDILDTR SKNEYGRFYC
YRFGKGLGSM TSMLYICIKL MYLANVFVQF IILNKFLGNE TFLWGFHTFA DLYAGREWQD
SGVFPRVTLC DFSVRKLANV HRYTVQCVLM INMFNEKIYL FIWFWFVFVL ITTFINTLCT
IYRLSFDSSR HNYIRSLLSG PVNNFKDEKA MIASFANNGL KQDGVLLMRF IDDHAGAMVT
KEICEELFKK HGENLQHNRD FHHGHSTKST SPGLEEGHHE HLYTPEKMKL MAPDYPIKHA
