ID   A0A077Z3E1_TRITR        Unreviewed;       497 AA.
AC   A0A077Z3E1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN   Name=inx {ECO:0000256|RuleBase:RU010713};
GN   ORFNames=TTRE_0000263901 {ECO:0000313|EMBL:CDW54369.1};
OS   Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW54369.1};
RN   [1] {ECO:0000313|EMBL:CDW54369.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Aslett M.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDW54369.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA   Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA   Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT   "The whipworm genome and dual-species transcriptomics of an intimate host-
RT   pathogen interaction.";
RL   Submitted (MAR-2014) 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; HG805893; CDW54369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077Z3E1; -.
DR   STRING; 36087.A0A077Z3E1; -.
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:SF14; INNEXIN-10; 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        27..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        104..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        199..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        296..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   REGION          422..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   497 AA;  58729 MW;  E67E811CF6B9CADA CRC64;
     MSYLYSALGS VHLFTTKGTD DDITDQLHYR WTCTLLIILS IIVSFKQFGG RPIECMVPEM
     FSSAWEQYAE SYCWAQDTYF IPFGDDIPQE IALREGRRIS YYQWVPFFLL ITAFSFQLPY
     FAWRFMSHRS GIRIRNIIEQ VRDPKNLMPD SRRFTLRLLT VHMENALKFQ RRLYRKKVLP
     HRILRFLNLP YSSFYVTSIY LLVKVLYLIN VIGQFFIMNY FLETDNNQGS LYGWEMFRNI
     LNGTQWDTSG FLPRVTLCDF EVSPLERAHP AVRVMGNVQR YSVQCVLVIN LFNEKIFVFL
     WFWYHLLTLV TVCSVLYWLT LMVCPWFSRW FIVRQLELAD LPFDAKNSHK DVVRFIDDYL
     RTDGVFVLRL LSMHTGVIFT CDLVGSLWKS FFGVENRMEE LGSHRWPSIA EINWLYEKQQ
     MESSKKGSRK PSFDSESDGE DEIGEIRQRP PPAYRRRSTI VRSRRSSEQA NPLIGRKEEN
     KEDSSPAKPA DTKESNL
//