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Database: UniProt
Entry: A0A158R7D1_TAEAS
LinkDB: A0A158R7D1_TAEAS
Original site: A0A158R7D1_TAEAS 
ID   A0A158R7D1_TAEAS        Unreviewed;       614 AA.
AC   A0A158R7D1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Innexin {ECO:0000256|RuleBase:RU010713};
GN   Name=inx {ECO:0000256|RuleBase:RU010713};
GN   ORFNames=TASK_LOCUS3630 {ECO:0000313|EMBL:VDK32103.1};
OS   Taenia asiatica (Asian tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000362901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TASK_0000362901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK32103.1, ECO:0000313|Proteomes:UP000282613}
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; UYRS01018306; VDK32103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158R7D1; -.
DR   STRING; 60517.A0A158R7D1; -.
DR   WBParaSite; TASK_0000362901-mRNA-1; TASK_0000362901-mRNA-1; TASK_0000362901.
DR   Proteomes; UP000046400; Unplaced.
DR   Proteomes; UP000282613; 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:SF36; 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}; Reference proteome {ECO:0000313|Proteomes:UP000282613};
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        109..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   REGION          185..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   614 AA;  70806 MW;  9BBBEE9EB608E6F7 CRC64;
     MDTRIIDGIT NSSASIGEDR SCPDDDFVDR VNHTYTMNLL MFFTAIVLSR QLVGKPISCW
     IPNDFTGAQG EYAETVCWVT STYFIPPAQA TVPIEEDIRY EKKIYYYQWV PFILMIQAAL
     FVLPCIVWRL FNTQSRINLR TVMEVSSDLK NLNDSLDQRR DLINCLVRYL EDALAIRHFR
     RQRRGKKTRA TDQQHYGKGW SQLNTAGSKA DERRGTSGRR FSTPVVPLTF SKQVRVPGPR
     PCMPTSSAYL SGLYLAVKIL YLANSTTQLV LTGKYLNGEA FIFGIETLRD LMNTRFWDQT
     GSFPRVALCD FELRRMGSNQ HRYTIQCVLR INIFNEKIYI FLWFWFFLIS LLNLLSFLRW
     CYKLLLSSVR VLFIRNLICI YFNIAAAKSQ LPSKILLDNK DKEKQQCQFS IADVFKTRDE
     LQASRVFSED ILGQDGVLLL RFINMNVGPS SAAELAGVIW IKYRKTAAFV NGTTSSGVED
     FVLANMAAGE IERPPAIPPK RRRPPAQWKK KKPTIMPLSA FIYRSRHAED NDSDKSTDSS
     RPTIEMLQEH RRYKPMIRKR GNYLSDDDDE NGQMSVVHEN YGPEEFLDSH DVPEPEVGQE
     LEELASEYRS FDDY
//
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