ID A0A0R3QS77_9BILA Unreviewed; 445 AA.
AC A0A0R3QS77;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN Name=inx {ECO:0000256|RuleBase:RU010713};
GN ORFNames=BTMF_LOCUS8613 {ECO:0000313|EMBL:VDO28809.1};
OS Brugia timori.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001057901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BTMF_0001057901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO28809.1, ECO:0000313|Proteomes:UP000280834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-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}.
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; UZAG01016506; VDO28809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3QS77; -.
DR STRING; 42155.A0A0R3QS77; -.
DR WBParaSite; BTMF_0001057901-mRNA-1; BTMF_0001057901-mRNA-1; BTMF_0001057901.
DR Proteomes; UP000050602; Unplaced.
DR Proteomes; UP000280834; 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:SF9; INNEXIN-7; 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:UP000280834};
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 88..109
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 184..209
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT REGION 416..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 51586 MW; 7EE596B82B713E58 CRC64;
MPFFLLFQAA CFKAPTLIWK YFAGQSGMKL GQILRLASDP ANSSLEVKKG NIETLCMHLQ
GALRFHERVK KKKLVPHKIC RFLNIKYANY YVTTVYILAK LAFLTNAVFQ ISLMTRYLLP
ELENNYGLES WMNIIWPKNV SPSWHHSGIF PLVTLCDFEV REMGNIQTHT VQCVLVVNLF
TEKIFILLWA WFMILATFTS LSVLNWIYLL TENCSKEHFI LNHLEMSGTP FNKNDPRNKK
HVDRFLHEYL GIDGIFVLRM VANHADVVFA TELVASLWRS HYVFEERRKN LLQMDKVWPQ
HQQRLELALL EEAEIARKIS SDALNALQRK RSVFFDSPYF VKRSSLTGIT IPKVLSRNML
GSSCAPSRNN SRDSIIPFSP RLGNHPRGSI FSTDSQCKPR RRHSLEETDI GCRVKKFADS
SDEEEQEKEK GPKSFMSRKS TIKIW
//