ID   A0A2G5VHE6_9PELO        Unreviewed;       425 AA.
AC   A0A2G5VHE6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN   Name=Cni-eat-5 {ECO:0000313|EMBL:PIC51157.1};
GN   Synonyms=Cnig_chr_I.g1783 {ECO:0000313|EMBL:PIC51157.1}, inx
GN   {ECO:0000256|RuleBase:RU010713};
GN   ORFNames=B9Z55_001783 {ECO:0000313|EMBL:PIC51157.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC51157.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIC51157.1}.
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DR   EMBL; PDUG01000001; PIC51157.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5VHE6; -.
DR   STRING; 1611254.A0A2G5VHE6; -.
DR   Proteomes; UP000230233; Chromosome i.
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:SF21; INNEXIN EAT-5; 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:UP000230233};
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        24..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        100..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        189..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        277..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
SQ   SEQUENCE   425 AA;  50326 MW;  7CBE51F5F090C770 CRC64;
     MNMLGSMFST VKPRLDDLGT DRLNYYYSTL IIMGMSLTIT ARQYVGSPLQ CWVPAQFTKA
     WEQYAEDYCF VYNTYWVKPN DKVPTTIEER VSQQLIYYQW APFIMAIEAA FFYLPVIFWS
     MLSTKSGINI IKLVETAQKA EGAESEDRKK QIDIICRHIS NNLRKRRNEE ETTKMAKIQR
     IFGMQHGKFI TNVYLVTKFI YMLNSFLQFY STNKFLGQND PYWGMRILDD ILHGTDWEHS
     GNFPRIAMCD FQVRVLGNLQ RHSIQCVLTL NMFNEKIFLF LYIWFLLVFF VTLFDSIFLI
     YNMFSSHKIV EFLQQFLDNQ EADENEEKKP DDEKKKVYRK EQHAILLSEF CLHKFTPDII
     ILLKMINNHT GDIVCTEIVG RMWNEFLKRD AKLVLQRFVD NDHNMETKSS SLKSVQLFEE
     HKGLI
//