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Database: UniProt
Entry: A0A3B4E828_PYGNA
LinkDB: A0A3B4E828_PYGNA
Original site: A0A3B4E828_PYGNA 
ID   A0A3B4E828_PYGNA        Unreviewed;       420 AA.
AC   A0A3B4E828;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Pannexin {ECO:0000256|RuleBase:RU010713};
GN   Name=PANX {ECO:0000256|RuleBase:RU010713};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000031838.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000031838.1}
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   -!- PTM: S-nitrosylation inhibits channel currents and ATP release.
CC       {ECO:0000256|PIRSR:PIRSR600990-50}.
CC   -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00351, ECO:0000256|RuleBase:RU010713}.
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DR   RefSeq; XP_017554753.1; XM_017699264.1.
DR   AlphaFoldDB; A0A3B4E828; -.
DR   STRING; 42514.ENSPNAP00000031838; -.
DR   GlyCosmos; A0A3B4E828; 2 sites, No reported glycans.
DR   Ensembl; ENSPNAT00000021186.1; ENSPNAP00000031838.1; ENSPNAG00000019410.1.
DR   GeneID; 108428339; -.
DR   CTD; 393890; -.
DR   GeneTree; ENSGT00940000153972; -.
DR   OMA; IPDRFQC; -.
DR   OrthoDB; 2996841at2759; -.
DR   Proteomes; UP000261440; 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:SF5; PANNEXIN-1; 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:PIRSR600990-51};
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}; S-nitrosylation {ECO:0000256|PIRSR:PIRSR600990-50};
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        34..56
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        196..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   TRANSMEM        260..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00351,
FT                   ECO:0000256|RuleBase:RU010713"
FT   MOD_RES         41
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600990-50"
FT   MOD_RES         332
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600990-50"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600990-52"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600990-51"
SQ   SEQUENCE   420 AA;  47352 MW;  83A19C4920496949 CRC64;
     MAIAHAATEY VFTDFLLKEP TSEAKYKGIR LDLALDKMVT CIAVGLPLLL ISLAFAQEVS
     VGTQISCFSP TNFSWRQAAY VDSYCWAAVQ RQDTGGLPLS LHKFFPYILL FVAVLVYVPA
     LFWRFTAAPV LSSDLTFIME ELDRSYNRAI KLAKCLHSSP THLDAQSSMP DLTENCFKYP
     LVEQYLKTKR FSHGLLVRYL LCRVVTFLVL VLACVYLCYY IQLSVTDEFH CNIRTGVLIN
     DSSVPSPLQC KLIAVGVFQL LSYINLCVYL LLAPACIYAT VVPMRSSADF LKPYEMLPTL
     GVMKFGTRAC NDLAMYLLFL EENLSELKSY KCLKVLELVK DQGDEHGPDT MLLLQSLGQV
     KMDVLDGRLK MKISHASDTN MSRDQDGERN CLEMKEVSPL LLKDGAKKSE DEKVLRQRVI
//
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