Panx1
entrez
315435
canonical
uniprot
P60570
canonical
ensembl
ENSRNOG00000010060
resolver
ensembl
ENSRNOG00055006999
resolver
ensembl
ENSRNOG00060005863
resolver
ensp
ENSRNOP00000013577
resolver
ensp
ENSRNOP00000075246
resolver
ensp
ENSRNOP00055009085
resolver
ensp
ENSRNOP00060007322
resolver
enst
ENSRNOT00000013577
resolver
enst
ENSRNOT00000083395
resolver
enst
ENSRNOT00055011550
resolver
enst
ENSRNOT00060009767
resolver
genesymbol
Panx1
resolver
genesymbol_syn
Panx
resolver
genesymbol_syn
Px1
resolver
uniprot
A0A0G2KA39
resolver
uniprot
E0X642
resolver
uniprot
E0X643
resolver
uniprot_entry
A0A0G2KA39_RAT
resolver
uniprot_entry
E0X642_RAT
resolver
uniprot_entry
E0X643_RAT
resolver
uniprot_entry
PANX1_RAT
resolver
amino_acid_sequence
MAIAHLATEYVFSDFLLKEPTEPKFKGLRLELAVDKMVTCIAVGLPLLLISLAFAQEISIGTQISCFSPSSFSWRQAAFVDSYCWAAVQQKNSLQSESGNLPLWLHKFFPYILLLFAILLYLPALFWRFAAAPHLCSDLKFIMEELDKVYNRAIKAAKSARDLDLRDGPGPPGVTENVGQSLWEISESHFKYPIVEQYLKTKKNSSHLIMKYISCRLVTFAVVLLACIYLSYYFSLSSLSDEFLCSIKSGVLRNDSTIPDSFQCKLIAVGIFQLLSLINLLVYALLVPVVIYTLFVPFRQKTDVLKVYEILPTFDVLHFKSEGYNDLSLYNLFLEENISELKSYKCLKVLENIKSNGQGIDPMLLLTNLGMIKMDVIDGKVPMSLQTKGEDQGSQRMDFKDLDLSSETAANNGEKNSRQRLLNSSC
uniprot
proteins
function
FUNCTION: Ion channel involved in a variety of physiological functions such as blood pressure regulation, apoptotic cell clearance and oogenesis (By similarity). Forms anion-selective channels with relatively low conductance and an order of permeabilities: nitrate>iodide>chlroride>>aspartate=glutamate=gluconate (By similarity). Can release ATP upon activation through phosphorylation or cleavage at C-terminus. May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis (By similarity). {ECO:0000250|UniProtKB:Q96RD7, ECO:0000250|UniProtKB:Q9JIP4}.; FUNCTION: [Caspase-activated pannexin-1]: During apoptosis, the C terminal tail is cleaved by caspases, which opens the main pore acting as a large-pore ATP efflux channel with a broad distribution, which allows the regulated release of molecules and ions smaller than 1 kDa, such as nucleotides ATP and UTP, and selective plasma membrane permeability to attract phagocytes that engulf the dying cells. {ECO:0000250|UniProtKB:Q96RD7}.
uniprot
proteins
mass_dalton
48073
uniprot
proteins
post_translational_modification
PTM: S-nitrosylation inhibits channel currents and ATP release. {ECO:0000250}.; PTM: N-glycosylation plays a role in cell surface targeting. Glycosylation at its extracellular surface makes unlikely that two oligomers could dock to form an intercellular channel such as in gap junctions. Exists in three glycosylation states: non-glycosylated (GLY0), high-mannose glycosylated (GLY1), and fully mature glycosylated (GLY2). {ECO:0000250|UniProtKB:Q96RD7}.; PTM: Cleaved by CASP3 and CASP7 during apoptosis. Cleavage opens the channel for the release of metabolites and induces plasma membrane permeability during apoptosis. {ECO:0000250|UniProtKB:Q96RD7}.; PTM: Phosphorylated at Tyr-198 by SRC. Phosphorylation activates ATP release. Constitutively phosphorylated in vascular smooth muscle cells. {ECO:0000250|UniProtKB:Q96RD7}.
uniprot
proteins
protein_family
Pannexin family
uniprot
proteins
pubmed
14597722
uniprot
proteins
sequence_length
426
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96RD7}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96RD7}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}.
uniprot
proteins
transmembrane_region
TRANSMEM 41..61; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"; TRANSMEM 107..127; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"; TRANSMEM 217..237; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"; TRANSMEM 278..298; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00351
uniprot
proteins