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Protein

Pannexin-1

Gene

Panx1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Structural component of the gap junctions and the hemichannels. May play a role as a Ca2+-leak channel to regulate ER Ca2+ homeostasis (By similarity).By similarity

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: MGI
  • calcium channel activity Source: UniProtKB
  • channel activity Source: MGI
  • gap junction hemi-channel activity Source: UniProtKB
  • leak channel activity Source: UniProtKB
  • receptor binding Source: MGI
  • wide pore channel activity Source: GO_Central

GO - Biological processi

  • calcium ion transport Source: UniProtKB
  • cation transport Source: MGI
  • cell-cell signaling Source: GO_Central
  • positive regulation of cytokine secretion Source: MGI
  • positive regulation of interleukin-1 alpha secretion Source: MGI
  • positive regulation of interleukin-1 beta secretion Source: MGI
  • protein hexamerization Source: UniProtKB
  • response to ATP Source: MGI
  • response to ischemia Source: MGI
  • transmembrane transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-MMU-112303. Electric Transmission Across Gap Junctions.
R-MMU-844456. The NLRP3 inflammasome.

Names & Taxonomyi

Protein namesi
Recommended name:
Pannexin-1
Gene namesi
Name:Panx1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1860055. Panx1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 40CytoplasmicSequence analysisAdd BLAST40
Transmembranei41 – 61HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini62 – 106ExtracellularSequence analysisAdd BLAST45
Transmembranei107 – 127HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini128 – 216CytoplasmicSequence analysisAdd BLAST89
Transmembranei217 – 237HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini238 – 277ExtracellularSequence analysisAdd BLAST40
Transmembranei278 – 298HelicalPROSITE-ProRule annotationAdd BLAST21
Topological domaini299 – 426CytoplasmicSequence analysisAdd BLAST128

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Endoplasmic reticulum, Gap junction, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40C → A: Abolishes S-nitrosylation; when associated with Ala-346. 1 Publication1
Mutagenesisi254N → Q: Impairs glycosylation. 1 Publication1
Mutagenesisi346C → A: Abolishes S-nitrosylation; when associated with Ala-40. 1 Publication1
Mutagenesisi426C → A: No effect on S-nitrosylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002084851 – 426Pannexin-1Add BLAST426

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40S-nitrosocysteine1 Publication1
Glycosylationi254N-linked (GlcNAc...)1 Publication1
Modified residuei346S-nitrosocysteine1 Publication1

Post-translational modificationi

N-glycosylation may play a role in cell surface targeting.1 Publication
S-nitrosylation inhibits channel currents and ATP release.1 Publication

Keywords - PTMi

Glycoprotein, S-nitrosylation

Proteomic databases

EPDiQ9JIP4.
MaxQBiQ9JIP4.
PaxDbiQ9JIP4.
PRIDEiQ9JIP4.

PTM databases

iPTMnetiQ9JIP4.
PhosphoSitePlusiQ9JIP4.

Expressioni

Tissue specificityi

Widely expressed, including in cartilage, skin, spleen and brain.

Gene expression databases

BgeeiENSMUSG00000031934.
CleanExiMM_PANX1.
ExpressionAtlasiQ9JIP4. baseline and differential.
GenevisibleiQ9JIP4. MM.

Interactioni

Subunit structurei

Homohexamer. Forms homomeric or PANX1/PANX2-heteromeric intercellular channels on coexpression in paired Xenopus oocytes.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Kcnab3P973822EBI-6272917,EBI-7261133

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: MGI
  • receptor binding Source: MGI

Protein-protein interaction databases

IntActiQ9JIP4. 4 interactors.
STRINGi10090.ENSMUSP00000126405.

Structurei

3D structure databases

ProteinModelPortaliQ9JIP4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pannexin family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II5X. Eukaryota.
ENOG410YA5H. LUCA.
GeneTreeiENSGT00390000009703.
HOGENOMiHOG000063721.
HOVERGENiHBG053497.
InParanoidiQ9JIP4.
KOiK03443.
OMAiVPFRQKT.
OrthoDBiEOG091G086D.
PhylomeDBiQ9JIP4.
TreeFamiTF333142.

Family and domain databases

InterProiIPR000990. Innexin.
[Graphical view]
PfamiPF00876. Innexin. 1 hit.
[Graphical view]
PROSITEiPS51013. PANNEXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JIP4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIAHLATEY VFSDFLLKEP TEPKFKGLRL ELAVDKMVTC IAVGLPLLLI
60 70 80 90 100
SLAFAQEISI GTQISCFSPS SFSWRQAAFV DSYCWAAVQQ KSSLQSESGN
110 120 130 140 150
LPLWLHKFFP YILLLFAILL YLPALFWRFS AAPHLCSDLK FIMEELDKVY
160 170 180 190 200
NRAIKAAKSA RDLDLRDGPG PPGVTENVGQ SLWEISESHF KYPIVEQYLK
210 220 230 240 250
TKKNSSHLIM KYISCRLVTF VVILLACIYL SYYFSLSSLS DEFLCSIKSG
260 270 280 290 300
VLKNDSTIPD RFQCKLIAVG IFQLLSLINL IVYALLIPVV VYTFFIPFRQ
310 320 330 340 350
KTDILKVYEI LPTFDVLHFK SEGYNDLSLY NLFLEENISE LKSYKCLKVL
360 370 380 390 400
ENIKSNGQGI DPMLLLTNLG MIKMDIIDGK IPTSLQTKGE DQGSQRVEFK
410 420
DLDLSSEAAA NNGEKNSRQR LLNPSC
Length:426
Mass (Da):48,167
Last modified:July 27, 2011 - v3
Checksum:i86AF6167C5D39565
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti296I → T in AAF75838 (PubMed:10898987).Curated1
Sequence conflicti409A → R in AAF75838 (PubMed:10898987).Curated1
Sequence conflicti422 – 426LNPSC → CESVLLMVSFLNFKPVTSVA DAPLLDL in AAF75838 (PubMed:10898987).Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF207817 mRNA. Translation: AAF75838.1.
AK014033 mRNA. Translation: BAB29125.1.
AK053871 mRNA. Translation: BAC35567.1.
AK089764 mRNA. Translation: BAC40956.1.
CH466522 Genomic DNA. Translation: EDL25014.1.
BC049074 mRNA. Translation: AAH49074.1.
CCDSiCCDS22832.1.
RefSeqiNP_062355.2. NM_019482.2.
UniGeneiMm.142253.

Genome annotation databases

EnsembliENSMUST00000164273; ENSMUSP00000126405; ENSMUSG00000031934.
GeneIDi55991.
KEGGimmu:55991.
UCSCiuc009ofi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF207817 mRNA. Translation: AAF75838.1.
AK014033 mRNA. Translation: BAB29125.1.
AK053871 mRNA. Translation: BAC35567.1.
AK089764 mRNA. Translation: BAC40956.1.
CH466522 Genomic DNA. Translation: EDL25014.1.
BC049074 mRNA. Translation: AAH49074.1.
CCDSiCCDS22832.1.
RefSeqiNP_062355.2. NM_019482.2.
UniGeneiMm.142253.

3D structure databases

ProteinModelPortaliQ9JIP4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JIP4. 4 interactors.
STRINGi10090.ENSMUSP00000126405.

PTM databases

iPTMnetiQ9JIP4.
PhosphoSitePlusiQ9JIP4.

Proteomic databases

EPDiQ9JIP4.
MaxQBiQ9JIP4.
PaxDbiQ9JIP4.
PRIDEiQ9JIP4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000164273; ENSMUSP00000126405; ENSMUSG00000031934.
GeneIDi55991.
KEGGimmu:55991.
UCSCiuc009ofi.1. mouse.

Organism-specific databases

CTDi24145.
MGIiMGI:1860055. Panx1.

Phylogenomic databases

eggNOGiENOG410II5X. Eukaryota.
ENOG410YA5H. LUCA.
GeneTreeiENSGT00390000009703.
HOGENOMiHOG000063721.
HOVERGENiHBG053497.
InParanoidiQ9JIP4.
KOiK03443.
OMAiVPFRQKT.
OrthoDBiEOG091G086D.
PhylomeDBiQ9JIP4.
TreeFamiTF333142.

Enzyme and pathway databases

ReactomeiR-MMU-112303. Electric Transmission Across Gap Junctions.
R-MMU-844456. The NLRP3 inflammasome.

Miscellaneous databases

ChiTaRSiPanx1. mouse.
PROiQ9JIP4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031934.
CleanExiMM_PANX1.
ExpressionAtlasiQ9JIP4. baseline and differential.
GenevisibleiQ9JIP4. MM.

Family and domain databases

InterProiIPR000990. Innexin.
[Graphical view]
PfamiPF00876. Innexin. 1 hit.
[Graphical view]
PROSITEiPS51013. PANNEXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPANX1_MOUSE
AccessioniPrimary (citable) accession number: Q9JIP4
Secondary accession number(s): Q5RL18, Q9CXS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.