ID   PANX1_PONAB             Reviewed;         426 AA.
AC   Q5REE3;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Pannexin-1;
GN   Name=PANX1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Structural component of the gap junctions and the
CC       hemichannels. May play a role as a Ca(2+)-leak channel to regulate ER
CC       Ca(2+) homeostasis. {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. Forms homomeric or PANX1/PANX2-heteromeric
CC       intercellular channels on coexpression in paired Xenopus oocytes.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC       junction {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}.
CC   -!- PTM: S-nitrosylation inhibits channel currents and ATP release.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00351}.
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DR   EMBL; CR857586; CAH89864.1; -; mRNA.
DR   RefSeq; NP_001124868.1; NM_001131396.1.
DR   AlphaFoldDB; Q5REE3; -.
DR   SMR; Q5REE3; -.
DR   STRING; 9601.ENSPPYP00000004323; -.
DR   GeneID; 100171730; -.
DR   KEGG; pon:100171730; -.
DR   CTD; 24145; -.
DR   eggNOG; ENOG502QT58; Eukaryota.
DR   InParanoid; Q5REE3; -.
DR   OrthoDB; 623546at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0022840; F:leak channel activity; ISS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR   GO; GO:0032732; P:positive regulation of interleukin-1 production; IEA:InterPro.
DR   InterPro; IPR000990; Innexin.
DR   InterPro; IPR039099; Pannexin.
DR   PANTHER; PTHR15759; PTHR15759; 1.
DR   Pfam; PF00876; Innexin; 1.
DR   PROSITE; PS51013; PANNEXIN; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel; Calcium transport; Cell junction; Cell membrane;
KW   Endoplasmic reticulum; Gap junction; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Reference proteome; S-nitrosylation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..426
FT                   /note="Pannexin-1"
FT                   /id="PRO_0000208486"
FT   TOPO_DOM        1..40
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        62..106
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        128..217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        239..266
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        288..426
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         40
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIP4"
FT   MOD_RES         347
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIP4"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   426 AA;  48036 MW;  52F0F5BA0A14696F CRC64;
     MAIAHLATEY VFSDFLLKEP TEPKFKGLRL ELAVDKMVTC IAVGLPLLLI SLAFAQEISI
     GTQISCFSPS SFSWRQAAFV DSYCWAAVQQ KNSLQSESGN LPLWLHKFFP YILLLFAILL
     YLPPLFWRFA AAPHICSDLK FIMEELDKVY NRAIKAAKSA RDLDMRDGAC SVPGVTENLR
     QSLWEVSESH FKYPIVEQYL KTKKNSNNLI IKYISCRLLT LIIILLACIY LGYYFSLSSL
     SGEFVCSIKS GILRNDSTVP DQFQCKLIAV GIFQLLSVIN LVVYVLLAPV VVYTLFVPFR
     QKTDVLKVYE ILPTFDVLHF KSEGYNDLSL YNLFLEENIS EVKSYKCLKV LENIKSSGQG
     IDPMLLLTNL GMIKMDVVDG KTAMSAETRE EHGNQTAELQ AMNIDGETKA NNGEKNARQR
     LLNSSC