ID G0M6M8_CAEBE Unreviewed; 420 AA.
AC G0M6M8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN Name=Cbn-inx-2 {ECO:0000313|EMBL:EGT29910.1};
GN Synonyms=inx {ECO:0000256|RuleBase:RU010713};
GN ORFNames=CAEBREN_20353 {ECO:0000313|EMBL:EGT29910.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Structural component of the gap junctions.
CC {ECO:0000256|RuleBase:RU010713}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU010713};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU010713}. Cell
CC junction, gap junction {ECO:0000256|RuleBase:RU010713}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00351, ECO:0000256|RuleBase:RU010713}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00351,
CC ECO:0000256|RuleBase:RU010713}.
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DR EMBL; GL379786; EGT29910.1; -; Genomic_DNA.
DR AlphaFoldDB; G0M6M8; -.
DR STRING; 135651.G0M6M8; -.
DR EnsemblMetazoa; CBN20353.1; CBN20353.1; WBGene00159078.
DR eggNOG; ENOG502S565; Eukaryota.
DR HOGENOM; CLU_035763_0_1_1; -.
DR InParanoid; G0M6M8; -.
DR OMA; HINYYRW; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR InterPro; IPR000990; Innexin.
DR PANTHER; PTHR11893; INNEXIN; 1.
DR PANTHER; PTHR11893:SF28; INNEXIN-2; 1.
DR Pfam; PF00876; Innexin; 1.
DR PRINTS; PR01262; INNEXIN.
DR PROSITE; PS51013; PANNEXIN; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|RuleBase:RU010713};
KW Gap junction {ECO:0000256|ARBA:ARBA00022868, ECO:0000256|PROSITE-
KW ProRule:PRU00351}; Ion channel {ECO:0000256|RuleBase:RU010713};
KW Ion transport {ECO:0000256|RuleBase:RU010713};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU00351}; Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU00351};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU00351}; Transport {ECO:0000256|RuleBase:RU010713}.
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
SQ SEQUENCE 420 AA; 49173 MW; B0BED8335CE57280 CRC64;
MLGFFGPIYD HLAGMLRKQQ GQLAYDTIDR INAWFTPFVL VAMTLAISCK QYFGQPIKCW
TPREFSGSWD GYVHDFCFIE NTYFVPNGTE VTDQARGDRH INYYRWVPLV LLLQAAMFIL
PYSIWNMFHK KTNINLKGSL RFFEDAMKKQ EPAQACESFA REVWGKLIES RKSTGKFYGC
QATINYFLLK LGFIVNCILQ MVLLKNFLDV DDYFWGFFHL WNVEFKGTAE KDDSIFPRVV
LCDFKVRNLG QQHQHTVSCI MILNMIIEKL YICFYFWLIF VFILTTVGML NFGFQMLFRR
HSLIPTNLNN KPSMNPTRSH RFIRKYLNFD GILLLTFIDS QFGAYRANQV IDGLIERFVA
EQQPDSSTVT SLNEDHPERY VTFNHDTIPM DRLNRKVHSL IEEVDGPHPS APVIEEKKTM
//