ID A0A0K0D1T8_ANGCA Unreviewed; 207 AA.
AC A0A0K0D1T8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN Name=inx {ECO:0000256|RuleBase:RU010713};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000403301-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0000403301-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; A0A0K0D1T8; -.
DR WBParaSite; ACAC_0000403301-mRNA-1; ACAC_0000403301-mRNA-1; ACAC_0000403301.
DR Proteomes; UP000035642; 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:SF10; INNEXIN-6; 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:UP000035642};
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 39..59
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
FT TRANSMEM 126..150
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT ECO:0000256|RuleBase:RU010713"
SQ SEQUENCE 207 AA; 23716 MW; F33DA842FD60B75F CRC64;
MENPGEPIPE RIAAFEARAS AYVWDGLRLA RNKGSQDMAL YYTISTAIQS LNAWIQWFWL
NSLLQSPLYT LWGPSLVHDL IRGDDWQVTG HFPRITHCDF NRRRPASVQL DTVLCVLTLN
IYYEKLFIFL WFWLLFVAIV STSNSIYWIG SICVSTKARR VITDYLATDP STQTGGLSTE
QFFRLLGKDG LFVLQQMSLN LGDIPAR
//