ID A0A1I7T0S1_9PELO Unreviewed; 423 AA.
AC A0A1I7T0S1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN Name=inx {ECO:0000256|RuleBase:RU010713};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold450.g1298.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold450.g1298.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 AlphaFoldDB; A0A1I7T0S1; -.
DR WBParaSite; Csp11.Scaffold450.g1298.t1; Csp11.Scaffold450.g1298.t1; Csp11.Scaffold450.g1298.
DR eggNOG; ENOG502S565; Eukaryota.
DR Proteomes; UP000095282; Unplaced.
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};
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 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 274..298
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT REGION 392..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 49391 MW; DFFE42766E0006DA CRC64;
MLGFFGPIYE HLAGMLRKQQ GQLAYDTIDR VNAWFTPFVL VAMTLAISCK QYFGQPLKCW
TPREFSGSWD GYVHDFCFIE NTYFVPNGTE VTDQVRGDRH INYYRWVPLV LLLQAAMFII
PYNIWNIFHK KTNINLKGCL RFFEGAMKKQ EAGQACEAFS REIWGKLIEA RKSTNKFYGC
QATINFFLLK LGFLINCILQ MVLLKHFLDV DDYFWGFFHL WNVEFKGTAE KEDSIFPRVV
LCDFKVRNFG QQQQHTVSCI MILNMIIEKL YICFYFWLIF VFVLTAAGMM NFGFQLLFRR
HSLIPTNLNN KRSMNPTRSH RFIRKYLNFD GVLLLTFVDA QFGAYRTSQV IDGLIERFVA
EQQPDSSTVT SLNEESPERY VTFNADTIPM DRMKRKTHTL LDEVDSSSAR PSAPSAVEEK
KEM
//
