Q5REE3

SS
Gene name
PANX1
Protein name
Pannexin-1
Names
Species
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
KEGG Pathway
pon:100171730
EC number
Protein Class

Descriptions

Pannexin-1(Panx1) is structural component of the gap junctions and the hemichannels involved in the ATP release and nucleotide permeation. Cleavage at Asp-379 removes a 46-amino acid C-terminal segment (380-426) that otherwise acts as an autoinhibitory blocker of the conducting pore formed by the Panx1 hexameric complex. Thus, accumulation of active caspase-3 during apoptosis can result in essentially irreversible open-gating of Panx1 channels.

Autoinhibitory domains (AIDs)

380-426 (C-terminal tail) SS

Target domain

28-294 (Pannexin)

Relief mechanism

Cleavage

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q5REE3

Entry ID Method Resolution Chain Position Source
AF-Q5REE3-F1 Predicted AlphaFoldDB

No variants for Q5REE3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5REE3

No associated diseases with Q5REE3

No regional properties for Q5REE3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q5REE3

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane ; Multi-pass membrane protein
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
gap junction A cell-cell junction composed of pannexins or innexins and connexins, two different families of channel-forming proteins.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

3 GO annotations of molecular function

Name Definition
calcium channel activity Enables the facilitated diffusion of a calcium ion (by an energy-independent process) involving passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism.
leak channel activity Enables the transport of a solute across a membrane via a narrow pore channel that is open even in an unstimulated or 'resting' state.
structural molecule activity The action of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell.

2 GO annotations of biological process

Name Definition
calcium ion transport The directed movement of calcium (Ca) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
positive regulation of interleukin-1 production Any process that activates or increases the frequency, rate, or extent of interleukin-1 production.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAIAHLATEY VFSDFLLKEP TEPKFKGLRL ELAVDKMVTC IAVGLPLLLI SLAFAQEISI
70 80 90 100 110 120
GTQISCFSPS SFSWRQAAFV DSYCWAAVQQ KNSLQSESGN LPLWLHKFFP YILLLFAILL
130 140 150 160 170 180
YLPPLFWRFA AAPHICSDLK FIMEELDKVY NRAIKAAKSA RDLDMRDGAC SVPGVTENLR
190 200 210 220 230 240
QSLWEVSESH FKYPIVEQYL KTKKNSNNLI IKYISCRLLT LIIILLACIY LGYYFSLSSL
250 260 270 280 290 300
SGEFVCSIKS GILRNDSTVP DQFQCKLIAV GIFQLLSVIN LVVYVLLAPV VVYTLFVPFR
310 320 330 340 350 360
QKTDVLKVYE ILPTFDVLHF KSEGYNDLSL YNLFLEENIS EVKSYKCLKV LENIKSSGQG
370 380 390 400 410 420
IDPMLLLTNL GMIKMDVVDG KTAMSAETRE EHGNQTAELQ AMNIDGETKA NNGEKNARQR
LLNSSC