Detail Information for IndEnz0002001138
IED ID IndEnz0002001138
Enzyme Type ID protease001138
Protein Name Pannexin-1
Gene Name Panx1 Px1
Organism Rattus norvegicus (Rat)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MAIAHLATEYVFSDFLLKEPTEPKFKGLRLELAVDKMVTCIAVGLPLLLISLAFAQEISIGTQISCFSPSSFSWRQAAFVDSYCWAAVQQKNSLQSESGNLPLWLHKFFPYILLLFAILLYLPALFWRFAAAPHLCSDLKFIMEELDKVYNRAIKAAKSARDLDLRDGPGPPGVTENVGQSLWEISESHFKYPIVEQYLKTKKNSSHLIMKYISCRLVTFAVVLLACIYLSYYFSLSSLSDEFLCSIKSGVLRNDSTIPDSFQCKLIAVGIFQLLSLINLLVYALLVPVVIYTLFVPFRQKTDVLKVYEILPTFDVLHFKSEGYNDLSLYNLFLEENISELKSYKCLKVLENIKSNGQGIDPMLLLTNLGMIKMDVIDGKVPMSLQTKGEDQGSQRMDFKDLDLSSETAANNGEKNSRQRLLNSSC
Enzyme Length 426
Uniprot Accession Number P60570
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Structural component of the gap junctions and the hemichannels. May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Glycosylation (1); Modified residue (2); Region (1); Topological domain (5); Transmembrane (4)
Keywords Calcium;Calcium channel;Calcium transport;Cell junction;Cell membrane;Endoplasmic reticulum;Gap junction;Glycoprotein;Ion channel;Ion transport;Membrane;Reference proteome;S-nitrosylation;Transmembrane;Transmembrane helix;Transport
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}.
Modified Residue MOD_RES 40; /note=S-nitrosocysteine; /evidence=ECO:0000250|UniProtKB:Q9JIP4; MOD_RES 346; /note=S-nitrosocysteine; /evidence=ECO:0000250|UniProtKB:Q9JIP4
Post Translational Modification PTM: S-nitrosylation inhibits channel currents and ATP release. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 16616526; 17036048; 17715132; 18649184; 19009624; 19056988; 19416975; 19780818; 20086016; 20200324; 20237259; 20332104; 20516070; 21041301; 21185900; 21267638; 21337450; 21467198; 21659516; 21685263; 21865551; 21907716; 22733659; 22956847; 22972801; 24269631; 24839011; 25170954; 25172944; 25376229; 25605289; 25630792; 25637780; 25925949; 26854804; 29484398; 29895988; 30456914; 30481075; 31138827; 31630543; 31712070; 32386453; 33640607; 33688389; 34205953; 34301850; 34768835;
Motif
Gene Encoded By
Mass 48,073
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda