PANX1
entrez
24145
canonical
uniprot
Q96RD7
canonical
ensembl
ENSG00000110218
resolver
ensp
ENSP00000227638
resolver
genesymbol
PANX1
resolver
genesymbol_syn
MRS1
resolver
hgnc
HGNC:8599
resolver
uniprot
O75968
resolver
uniprot
Q543A0
resolver
uniprot
Q6UW26
resolver
uniprot
Q96AM9
resolver
uniprot
Q96L77
resolver
uniprot
Q96RS5
resolver
uniprot_entry
PANX1_HUMAN
resolver
uniprot_sec
O75968
resolver
uniprot_sec
Q543A0
resolver
uniprot_sec
Q6UW26
resolver
uniprot_sec
Q96AM9
resolver
uniprot_sec
Q96L77
resolver
uniprot_sec
Q96RS5
resolver
amino_acid_sequence
MAIAQLATEYVFSDFLLKEPTEPKFKGLRLELAVDKMVTCIAVGLPLLLISLAFAQEISIGTQISCFSPSSFSWRQAAFVDSYCWAAVQQKNSLQSESGNLPLWLHKFFPYILLLFAILLYLPPLFWRFAAAPHICSDLKFIMEELDKVYNRAIKAAKSARDLDMRDGACSVPGVTENLGQSLWEVSESHFKYPIVEQYLKTKKNSNNLIIKYISCRLLTLIIILLACIYLGYYFSLSSLSDEFVCSIKSGILRNDSTVPDQFQCKLIAVGIFQLLSVINLVVYVLLAPVVVYTLFVPFRQKTDVLKVYEILPTFDVLHFKSEGYNDLSLYNLFLEENISEVKSYKCLKVLENIKSSGQGIDPMLLLTNLGMIKMDVVDGKTPMSAEMREEQGNQTAELQGMNIDSETKANNGEKNARQRLLDSSC
uniprot
proteins
disease_involvement
DISEASE: Oocyte/zygote/embryo maturation arrest 7 (OZEMA7) [MIM:618550]: An autosomal dominant infertility disorder due to oocyte degeneration and death, which may occur before or after fertilization. {ECO:0000269|PubMed:20829356, ECO:0000269|PubMed:30918116}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Ion channel involved in a variety of physiological functions such as blood pressure regulation, apoptotic cell clearance and oogenesis (PubMed:15304325, PubMed:16908669, PubMed:20829356, PubMed:20944749, PubMed:30918116). 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 (PubMed:32238926). May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis (PubMed:16908669). {ECO:0000250|UniProtKB:Q9JIP4, ECO:0000269|PubMed:15304325, ECO:0000269|PubMed:16908669, ECO:0000269|PubMed:20944749, ECO:0000269|PubMed:32238926}.; 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:0000269|PubMed:20944749, ECO:0000269|PubMed:32238926, ECO:0000269|PubMed:32494015}.
uniprot
proteins
mass_dalton
48050
uniprot
proteins
mutagenesis
MUTAGEN 74; /note="W->A: No effect on voltage-dependence. Altered anion selectivity with equal permeability for iodide and choride."; /evidence="ECO:0000269|PubMed:32494015"; MUTAGEN 75; /note="R->E: Loss of voltage-dependence and anion selectivity. Strong increase in permeability of sodium over chloride."; /evidence="ECO:0000269|PubMed:32494015"; MUTAGEN 164..167; /note="DMRD->AAAA: Not cleaved by CASP3 or CASP7."; /evidence="ECO:0000269|PubMed:20944749"; MUTAGEN 255; /note="N->A: Impaired glycosylation. Forms gap junctions by 2 hemichannels."; /evidence="ECO:0000269|PubMed:32494015"; MUTAGEN 255; /note="N->Q: Impaired glycosylation. Loss of GLY1 and GLY2 forms. No effect on oocyte survival. Located in the cytoplasm. Decreased levels of pro-IL1B upon LPS priming and ATP stimulation. Attenuated pyroptotic cell death induced by LPS and ATP."; /evidence="ECO:0000269|PubMed:17715132, ECO:0000269|PubMed:30918116, ECO:0000269|PubMed:33947837"; MUTAGEN 338; /note="N->Q: Impaired glycosylation; loss of GLY2 form; oocyte death."; /evidence="ECO:0000269|PubMed:30918116"; MUTAGEN 376..379; /note="DVVD->AAAA,EEEE: Not cleaved by CASP3 or CASP7. Reduces channel activation."; /evidence="ECO:0000269|PubMed:20944749"; MUTAGEN 379; /note="D->A: No effect on cell membrane location. Decreased levels of pro-IL1B upon LPS priming and ATP stimulation. Attenuated pyroptotic cell death induced by LPS and ATP."; /evidence="ECO:0000269|PubMed:33947837"; MUTAGEN 394; /note="N->Q: No change in glycosylation pattern."; /evidence="ECO:0000269|PubMed:30918116"; MUTAGEN 424; /note="S->A: No effect on cell membrane location. Promoted pyroptotic cell death induced by LPS and ATP."; /evidence="ECO:0000269|PubMed:33947837
uniprot
proteins
post_translational_modification
PTM: S-nitrosylation inhibits channel currents and ATP release. {ECO:0000250|UniProtKB:Q9JIP4}.; 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 (PubMed:17715132, PubMed:32494015, PubMed:33947837). Exists in three glycosylation states: non-glycosylated (GLY0), high-mannose glycosylated (GLY1), and fully mature glycosylated (GLY2) (PubMed:30918116). {ECO:0000269|PubMed:17715132, ECO:0000269|PubMed:30918116, ECO:0000269|PubMed:32494015, ECO:0000269|PubMed:33947837}.; 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:0000269|PubMed:20944749, ECO:0000269|PubMed:32284561, ECO:0000269|PubMed:32494015}.; PTM: Phosphorylated at Tyr-199 by SRC. Phosphorylation activates ATP release. Constitutively phosphorylated in vascular smooth muscle cells. {ECO:0000269|PubMed:30814251}.
uniprot
proteins
protein_family
Pannexin family
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
15028292
uniprot
proteins
pubmed
15304325
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16303743
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16908669
uniprot
proteins
pubmed
17715132
uniprot
proteins
pubmed
20829356
uniprot
proteins
pubmed
20944749
uniprot
proteins
pubmed
27129271
uniprot
proteins
pubmed
30814251
uniprot
proteins
pubmed
30918116
uniprot
proteins
pubmed
32231289
uniprot
proteins
pubmed
32238926
uniprot
proteins
pubmed
32284561
uniprot
proteins
pubmed
32494015
uniprot
proteins
pubmed
33947837
uniprot
proteins
sequence_length
426
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20944749, ECO:0000269|PubMed:30814251, ECO:0000269|PubMed:30918116}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16908669}; 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 218..238; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"; TRANSMEM 267..287; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00351
uniprot
proteins