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Database: UniProt
Entry: A0A0R3S688_9BILA
LinkDB: A0A0R3S688_9BILA
Original site: A0A0R3S688_9BILA 
ID   A0A0R3S688_9BILA        Unreviewed;       332 AA.
AC   A0A0R3S688;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN   Name=inx {ECO:0000256|RuleBase:RU010713};
OS   Elaeophora elaphi.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX   NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0001031001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EEL_0001031001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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; A0A0R3S688; -.
DR   WBParaSite; EEL_0001031001-mRNA-1; EEL_0001031001-mRNA-1; EEL_0001031001.
DR   Proteomes; UP000050640; 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:SF45; INNEXIN; 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        100..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
SQ   SEQUENCE   332 AA;  39440 MW;  582B084D94741E4D CRC64;
     MLFLDAFLKG LKPQFDDDAV DRLNYYYTPL LLVIFALTLS AKQYVGQPIQ CWIPAQFTGA
     WEQYSENYCF IQNTYFLPLN HYIPRDLHER EEREIGYYQW VPFVLGLQGI LFYLPCLIWR
     LLNWQSGIFL KGIVLMSQDV NNMQSDKRKD SVTVVATHIY DSLKTQRNLI RNNPIAFLLR
     KGAYLTLLYM LVKFIYLLQA ITQFVILNNF LGTDYTFWGF EILRDLVNGH EWQESGHFPR
     VTMCDFDVRV LGNKHRHTVQ CVLMINMFNE KVYLFLWWWI LLVIISTIAS LIYWYCMSFI
     ESQQYSFIAQ YLRVYGLLDG QGNLLHVIFY IS
//
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