PANX1_RAT
ID PANX1_RAT Reviewed; 426 AA.
AC P60570;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Pannexin-1;
GN Name=Panx1; Synonyms=Px1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBUNIT.
RC STRAIN=Wistar; TISSUE=Hippocampus;
RX PubMed=14597722; DOI=10.1073/pnas.2233464100;
RA Bruzzone R., Hormuzdi S.G., Barbe M., Herb A., Monyer H.;
RT "Pannexins, a family of gap junction proteins expressed in brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13644-13649(2003).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer (By similarity). Forms homomeric or PANX1/PANX2-
CC heteromeric intercellular channels on coexpression in paired Xenopus
CC oocytes. {ECO:0000250, ECO:0000269|PubMed:14597722}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; 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 -!- TISSUE SPECIFICITY: Expressed in the eye, thyroid, prostate, kidney and
CC liver. Abundantly expressed in the CNS, including hippocampus,
CC olfactory bulb, cortex, cerebellum and white matter.
CC {ECO:0000269|PubMed:14597722}.
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; AJ557015; CAD89522.1; -; mRNA.
DR RefSeq; NP_955429.1; NM_199397.2.
DR AlphaFoldDB; P60570; -.
DR SMR; P60570; -.
DR STRING; 10116.ENSRNOP00000013577; -.
DR GlyGen; P60570; 1 site.
DR iPTMnet; P60570; -.
DR PhosphoSitePlus; P60570; -.
DR PaxDb; P60570; -.
DR PRIDE; P60570; -.
DR Ensembl; ENSRNOT00000013577; ENSRNOP00000013577; ENSRNOG00000010060.
DR GeneID; 315435; -.
DR KEGG; rno:315435; -.
DR UCSC; RGD:735204; rat.
DR CTD; 24145; -.
DR RGD; 735204; Panx1.
DR eggNOG; ENOG502QT58; Eukaryota.
DR GeneTree; ENSGT00940000153972; -.
DR HOGENOM; CLU_050054_1_0_1; -.
DR InParanoid; P60570; -.
DR OMA; IPDRFQC; -.
DR OrthoDB; 623546at2759; -.
DR PhylomeDB; P60570; -.
DR TreeFam; TF333142; -.
DR Reactome; R-RNO-112303; Electric Transmission Across Gap Junctions.
DR Reactome; R-RNO-844456; The NLRP3 inflammasome.
DR PRO; PR:P60570; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000010060; Expressed in jejunum and 17 other tissues.
DR ExpressionAtlas; P60570; baseline and differential.
DR Genevisible; P60570; RN.
DR GO; GO:0032059; C:bleb; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR GO; GO:0015267; F:channel activity; ISO:RGD.
DR GO; GO:0005243; F:gap junction channel activity; IMP:RGD.
DR GO; GO:0022840; F:leak channel activity; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IMP:RGD.
DR GO; GO:0097110; F:scaffold protein binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0022829; F:wide pore channel activity; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0006812; P:cation transport; ISO:RGD.
DR GO; GO:0007267; P:cell-cell signaling; IMP:RGD.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
DR GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; ISO:RGD.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:RGD.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IEA:Ensembl.
DR GO; GO:0033198; P:response to ATP; ISO:RGD.
DR GO; GO:0002931; P:response to ischemia; ISO:RGD.
DR GO; GO:0055085; P:transmembrane transport; ISO:RGD.
DR InterPro; IPR000990; Innexin.
DR InterPro; IPR039099; Pannexin.
DR PANTHER; PTHR15759; PTHR15759; 1.
DR Pfam; PF00876; Innexin; 1.
DR PROSITE; PS51013; PANNEXIN; 1.
PE 1: Evidence at protein 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_0000208487"
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..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 238..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 299..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 407..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIP4"
FT MOD_RES 346
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIP4"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 426 AA; 48073 MW; 1C2AF8FF058323B4 CRC64;
MAIAHLATEY VFSDFLLKEP TEPKFKGLRL ELAVDKMVTC IAVGLPLLLI SLAFAQEISI
GTQISCFSPS SFSWRQAAFV DSYCWAAVQQ KNSLQSESGN LPLWLHKFFP YILLLFAILL
YLPALFWRFA AAPHLCSDLK FIMEELDKVY NRAIKAAKSA RDLDLRDGPG PPGVTENVGQ
SLWEISESHF KYPIVEQYLK TKKNSSHLIM KYISCRLVTF AVVLLACIYL SYYFSLSSLS
DEFLCSIKSG VLRNDSTIPD SFQCKLIAVG IFQLLSLINL LVYALLVPVV IYTLFVPFRQ
KTDVLKVYEI LPTFDVLHFK SEGYNDLSLY NLFLEENISE LKSYKCLKVL ENIKSNGQGI
DPMLLLTNLG MIKMDVIDGK VPMSLQTKGE DQGSQRMDFK DLDLSSETAA NNGEKNSRQR
LLNSSC
