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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

GO - Biological processi

  • calcium ion transport Source: UniProtKB
  • cation transport Source: MGI
  • cell-cell signaling Source: Ensembl
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4040CytoplasmicSequence analysisAdd
BLAST
Transmembranei41 – 6121HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini62 – 10645ExtracellularSequence analysisAdd
BLAST
Transmembranei107 – 12721HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini128 – 21689CytoplasmicSequence analysisAdd
BLAST
Transmembranei217 – 23721HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini238 – 27740ExtracellularSequence analysisAdd
BLAST
Transmembranei278 – 29821HelicalPROSITE-ProRule annotationAdd
BLAST
Topological domaini299 – 426128CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401C → A: Abolishes S-nitrosylation; when associated with Ala-346. 1 Publication
Mutagenesisi254 – 2541N → Q: Impairs glycosylation. 1 Publication
Mutagenesisi346 – 3461C → A: Abolishes S-nitrosylation; when associated with Ala-40. 1 Publication
Mutagenesisi426 – 4261C → A: No effect on S-nitrosylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Pannexin-1PRO_0000208485Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401S-nitrosocysteine1 Publication
Glycosylationi254 – 2541N-linked (GlcNAc...)1 Publication
Modified residuei346 – 3461S-nitrosocysteine1 Publication

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

PhosphoSiteiQ9JIP4.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9JIP4.
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 interactions.
STRINGi10090.ENSMUSP00000126405.

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.
OrthoDBiEOG74N5G9.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti296 – 2961I → T in AAF75838 (PubMed:10898987).Curated
Sequence conflicti409 – 4091A → R in AAF75838 (PubMed:10898987).Curated
Sequence conflicti422 – 4265LNPSC → CESVLLMVSFLNFKPVTSVA DAPLLDL in AAF75838 (PubMed:10898987).Curated

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

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JIP4. 4 interactions.
STRINGi10090.ENSMUSP00000126405.

PTM databases

PhosphoSiteiQ9JIP4.

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.
OrthoDBiEOG74N5G9.
PhylomeDBiQ9JIP4.
TreeFamiTF333142.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiPanx1. mouse.
NextBioi311718.
PROiQ9JIP4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JIP4.
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...

Publicationsi

« Hide 'large scale' publications
  1. "A ubiquitous family of putative gap junction molecules."
    Panchin Y., Kelmanson I., Matz M., Lukyanov K., Usman N., Lukyanov S.
    Curr. Biol. 10:R473-R474(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryonic head, Eye and Spleen.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins."
    Penuela S., Bhalla R., Gong X.Q., Cowan K.N., Celetti S.J., Cowan B.J., Bai D., Shao Q., Laird D.W.
    J. Cell Sci. 120:3772-3783(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-254, MUTAGENESIS OF ASN-254.
  6. Cited for: S-NITROSYLATION AT CYS-40 AND CYS-346, MUTAGENESIS OF CYS-40; CYS-346 AND CYS-426.

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: May 11, 2016
This is version 112 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.