ID   A0A3B3TF91_9TELE        Unreviewed;       655 AA.
AC   A0A3B3TF91;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Pannexin {ECO:0000256|RuleBase:RU010713};
GN   Name=PANX {ECO:0000256|RuleBase:RU010713};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000040966.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000040966.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Structural component of the gap junctions and the
CC       hemichannels. {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   ---------------------------------------------------------------------------
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   STRING; 1676925.ENSPKIP00000040960; -.
DR   Ensembl; ENSPKIT00000021988.1; ENSPKIP00000040960.1; ENSPKIG00000017709.1.
DR   Ensembl; ENSPKIT00000021994.1; ENSPKIP00000040966.1; ENSPKIG00000017709.1.
DR   GeneTree; ENSGT00940000153972; -.
DR   OrthoDB; 5346856at2759; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   GO; GO:0006812; P:monoatomic cation transport; IEA:InterPro.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0032732; P:positive regulation of interleukin-1 production; IEA:InterPro.
DR   InterPro; IPR000990; Innexin.
DR   InterPro; IPR039099; Pannexin.
DR   PANTHER; PTHR15759; PANNEXIN; 1.
DR   PANTHER; PTHR15759:SF7; PANNEXIN-2; 1.
DR   Pfam; PF00876; Innexin; 1.
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}; Glycoprotein {ECO:0000256|PIRSR:PIRSR600990-52};
KW   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        54..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        124..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        227..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   REGION          555..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..645
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600990-52"
SQ   SEQUENCE   655 AA;  73470 MW;  A73BAB5AF5DAE6BD CRC64;
     MQNIFEQNLD MATALLAGEK LKELILPGST QDEKGGALAG LMVQLKLELP FDRVVTIGTV
     IIPILLVTLV FTRNFAEESI YCYTPSNFTR DQALYARGYC WTELRDAIPG VETTVRPSLF
     EHKFLPYALL AFAGIMYIPA LGWEFLGSTR LTSELNFLLQ EIDNCYHRAA EGRAPKIEKQ
     IQSKGPGITE RERREIIENA EKEKSPEQNL FEKYLERRGQ SNFLAKLYLA RHLAIICLSS
     IPITYLSTYY ARQRQNEFTC ALGEPPDSSS TSDLRVSVNC KLPSVQLQRI MAAVDIGLLC
     FMNLIILVNL LHLFVVRKSN FVFDKLHKVG IKTRRRWQKS PFCDINILAM FCDENRDHIK
     SLNRLDFITN ESDLMYDNVV RQLLAALAQS NHDATPTVRD SGVQTIDPNL DPSVLGIGEL
     GGEPLVIKRP RKKIKWIPTS NPLPQSFKEP LALTRLENST KADKPKPLRR KTVADTFIAP
     LMDTKSTQYP LTSKTGDLSG VGMEKKHKGN FSLDVQPYML TIRKPKAEVA HAEPTPPDSS
     LDTVFLEGTH TIVHVPSSIT DNKESVSEPN PSSFSGVTLS TSSFLNGTTS SLPMTLPPAS
     QEDAENQGRP FNRNPSHPLL NIHRTLYEEE EPSEQARRDR LTERPAGELI TAGEC
//