INX2_CAEEL
ID INX2_CAEEL Reviewed; 419 AA.
AC Q9U3K5; Q9BMT8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Innexin-2;
DE AltName: Full=Protein opu-2;
GN Name=inx-2; Synonyms=opu-2; ORFNames=F08G12.10;
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 [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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Bristol N2;
RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA Thierry-Mieg D., Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Structural component of the gap junctions.
CC {ECO:0000250|UniProtKB:O61715}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC junction.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z66561; CAB54206.2; -; Genomic_DNA.
DR EMBL; AF304127; AAG50240.1; -; mRNA.
DR PIR; T20594; T20594.
DR RefSeq; NP_509885.1; NM_077484.3.
DR AlphaFoldDB; Q9U3K5; -.
DR SMR; Q9U3K5; -.
DR BioGRID; 46228; 2.
DR STRING; 6239.F08G12.10; -.
DR EPD; Q9U3K5; -.
DR PaxDb; Q9U3K5; -.
DR PeptideAtlas; Q9U3K5; -.
DR EnsemblMetazoa; F08G12.10.1; F08G12.10.1; WBGene00002124.
DR GeneID; 181318; -.
DR KEGG; cel:CELE_F08G12.10; -.
DR UCSC; F08G12.10; c. elegans.
DR CTD; 181318; -.
DR WormBase; F08G12.10; CE26709; WBGene00002124; inx-2.
DR eggNOG; ENOG502S565; Eukaryota.
DR HOGENOM; CLU_035763_0_1_1; -.
DR InParanoid; Q9U3K5; -.
DR OMA; HINYYRW; -.
DR OrthoDB; 738314at2759; -.
DR PhylomeDB; Q9U3K5; -.
DR PRO; PR:Q9U3K5; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002124; Expressed in embryo and 4 other tissues.
DR GO; GO:0005921; C:gap junction; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005243; F:gap junction channel activity; ISS:UniProtKB.
DR GO; GO:0055077; F:gap junction hemi-channel activity; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR000990; Innexin.
DR PANTHER; PTHR11893; PTHR11893; 1.
DR Pfam; PF00876; Innexin; 1.
DR PRINTS; PR01262; INNEXIN.
DR PROSITE; PS51013; PANNEXIN; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Gap junction; Ion channel; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..419
FT /note="Innexin-2"
FT /id="PRO_0000208505"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
SQ SEQUENCE 419 AA; 48882 MW; F9D8A031257C805B CRC64;
MLGFFGPLYE QLVGMLRKQQ GQLAFDTIDR VNAWFTPFVL VAMTLAISCK QYFGQPIKCW
TPREFSGSWD GYVHDFCFIE NTYFVPNGTE VTDEARGGRH INYYRWVPLV LLFQAAMFVL
PYHLWNLFHK RTTINLKGSL RFFEGALKKL EPAQACESFA GEIWNRLSDI RNSSNKLYGF
QATINYFLLK LGFIVNCILQ MVLLKHFLDV DDYFWGFFHL WNVEFKGTAE KEDSIFPRIV
LCDFKVRNLG QQHQHTVSCI MILNMIIEKL YICFYFWLIF VFVVTTAGMI HFAFQILFRR
HSLIPTNLNN KNKMNPTRSH EFIKDYLNFD GCLLLTYVDA QFGAFRTSQV IDGLVHRFTN
ELDSDSSAVT SLNEDHPERY VAFNTDTIPM DRYARKHHSL IEEVDGPSAP PANEEKKEI