UNC9_CAEEL
ID UNC9_CAEEL Reviewed; 386 AA.
AC O01393; Q9NAN6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Innexin unc-9;
DE AltName: Full=Uncoordinated protein 9;
GN Name=unc-9 {ECO:0000312|WormBase:R12H7.1a};
GN ORFNames=R12H7.1 {ECO:0000312|WormBase:R12H7.1a};
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=Bristol N2;
RX PubMed=9375655; DOI=10.1046/j.1471-4159.1997.69062251.x;
RA Barnes T.M., Hekimi S.;
RT "The C. elegans avermectin resistance and anesthetic response gene unc-9
RT encodes a member of a protein family implicated in electrical coupling of
RT excitable cells.";
RL J. Neurochem. 69:2251-2260(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]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27015090; DOI=10.1371/journal.pgen.1005948;
RA Meng L., Chen C.H., Yan D.;
RT "Regulation of Gap Junction Dynamics by UNC-44/ankyrin and UNC-33/CRMP
RT through VAB-8 in C. elegans Neurons.";
RL PLoS Genet. 12:E1005948-E1005948(2016).
RN [4]
RP FUNCTION, INTERACTION WITH F-ACTIN, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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:27015090,
CC PubMed:33238150). Plays a role in maintaining gap junction activity to
CC promote locomotion (PubMed:33238150). {ECO:0000269|PubMed:27015090,
CC ECO:0000269|PubMed:33238150}.
CC -!- SUBUNIT: Heterooligomer of unc-7 and unc-9. Interacts with F-actin
CC (PubMed:33238150). {ECO:0000269|PubMed:33238150, ECO:0000305}.
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:27015090, ECO:0000269|PubMed:33238150}.
CC Note=Co-localizes with unc-1 at the gap junctions formed between PLM
CC and other neurons. {ECO:0000269|PubMed:27015090}.
CC -!- TISSUE SPECIFICITY: Expressed in PLM neurons (at protein level).
CC Expressed in the nerve ring (PubMed:33238150).
CC {ECO:0000269|PubMed:27015090, ECO:0000269|PubMed:33238150}.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
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DR EMBL; U93195; AAB51534.1; -; mRNA.
DR EMBL; BX284606; CAB61030.2; -; Genomic_DNA.
DR RefSeq; NP_741917.1; NM_171790.3.
DR AlphaFoldDB; O01393; -.
DR SMR; O01393; -.
DR BioGRID; 46346; 4.
DR STRING; 6239.R12H7.1; -.
DR EPD; O01393; -.
DR PaxDb; O01393; -.
DR PeptideAtlas; O01393; -.
DR EnsemblMetazoa; R12H7.1a.1; R12H7.1a.1; WBGene00006749.
DR EnsemblMetazoa; R12H7.1a.2; R12H7.1a.2; WBGene00006749.
DR GeneID; 181443; -.
DR KEGG; cel:CELE_R12H7.1; -.
DR UCSC; R12H7.1; c. elegans.
DR CTD; 181443; -.
DR WormBase; R12H7.1a; CE28246; WBGene00006749; unc-9.
DR eggNOG; ENOG502QSWG; Eukaryota.
DR HOGENOM; CLU_035763_0_1_1; -.
DR InParanoid; O01393; -.
DR OMA; NFWLMDV; -.
DR OrthoDB; 738314at2759; -.
DR PhylomeDB; O01393; -.
DR PRO; PR:O01393; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006749; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; O01393; baseline and differential.
DR GO; GO:0005911; C:cell-cell junction; 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; IDA:WormBase.
DR GO; GO:0055077; F:gap junction hemi-channel activity; ISS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:WormBase.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR InterPro; IPR000990; Innexin.
DR PANTHER; PTHR11893; PTHR11893; 2.
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..386
FT /note="Innexin unc-9"
FT /id="PRO_0000208518"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
SQ SEQUENCE 386 AA; 45192 MW; D7126726B74B7CAB CRC64;
MSMLLYYFAS AVKSIQFHVD DDIIDKLNYY YTTAIITVFA ILVSAKQYVG FPIQCWVPAT
FTEPMEQYTE NYCWVQNTYF LPLHDYIPHN YAERENRQIG YYQWVPFVLA LEALLFYVPT
IVWRLLSWQS GIHVQSLVQM ACDSRLLDLE SRNRALQTIA TNVEEALHVK HQVMSGNRLK
LLNLIICTRS SGAAVTFLYI SVKILYTVNI VGQIFLLNTF LGNRSKWYGL QVLNDLMNGR
EWEESGHFPR VTLCDFEVKV LGNVHRHTVQ CVLMINMFNE KIFLFLWFWY FLLAGATLCS
LFYWIYISVV PSRQLNFVGK YLTGIEGYKM VDSQSLRRFV FHFLRQDGVF LLRMVATHAG
ELPCYELAKT LWNNYCDNKE GKMHDV
