GenomeNet

Database: UniProt
Entry: A0A0R3QS77_9BILA
LinkDB: A0A0R3QS77_9BILA
Original site: A0A0R3QS77_9BILA 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system