ID A0A3B0J8G3_DROGU Unreviewed; 457 AA.
AC A0A3B0J8G3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN Name=inx {ECO:0000256|RuleBase:RU010713};
GN ORFNames=DGUA_6G011134 {ECO:0000313|EMBL:SPP78487.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP78487.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) 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}.
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DR EMBL; OUUW01000003; SPP78487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0J8G3; -.
DR OMA; NFWLMDV; -.
DR OrthoDB; 2873211at2759; -.
DR Proteomes; UP000268350; 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:SF43; INNEXIN INX4-RELATED; 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 23..43
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 131..153
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 200..221
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 291..315
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT REGION 398..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 51831 MW; 783AC1B86649A938 CRC64;
MYAAVKPLSQ YLRQKTVRIY DPIFILHSKY TIVILLACTI LLSAKQYFGE PILCISTNKH
TEYIQSYCWT MGTYILPTES NTSTGLPGAA FNRSGLQGLV ARDQQFARLI SIAEGVGPEK
RGVTKRLYLR YYQWVFMILL FQSLLFHMPS YLWKVWEGHR MAQLSCEVGG AIIVEDTYRT
RLHMLTKYFR SKFSAIHCCY AIKYTFCEML NLLISILNFW LMDVVFNGFW QKYIHALAAI
PVYDWQLWNM MTSRVFPKVA KCEMFVYGPS GTPNVLDILC VLPLNILNEK IFAVLYVWFL
FIAMLSALNM LYRLLLVCCA RLRLQLLCTH LRGMPKTHVR EVLTTAGYGD WFVLMGVSVN
VNPKLFRELV EQLYTELMEE RAAAAAAAAA AKRESPAASH QVPGAAAPQS PQPTPSAPHA
EAVASVRTLT LMAPTLNLMG SNNEIVSIDR CCDESQA
//
