PANX1_MOUSE
ID PANX1_MOUSE Reviewed; 426 AA.
AC Q9JIP4; Q5RL18; Q9CXS7;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Pannexin-1;
GN Name=Panx1 {ECO:0000312|MGI:MGI:1860055};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10898987; DOI=10.1016/s0960-9822(00)00576-5;
RA Panchin Y., Kelmanson I., Matz M., Lukyanov K., Usman N., Lukyanov S.;
RT "A ubiquitous family of putative gap junction molecules.";
RL Curr. Biol. 10:R473-R474(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic head, Eye, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP GLYCOSYLATION AT ASN-254, AND MUTAGENESIS OF ASN-254.
RX PubMed=17925379; DOI=10.1242/jcs.009514;
RA Penuela S., Bhalla R., Gong X.Q., Cowan K.N., Celetti S.J., Cowan B.J.,
RA Bai D., Shao Q., Laird D.W.;
RT "Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct
RT characteristics from the connexin family of gap junction proteins.";
RL J. Cell Sci. 120:3772-3783(2007).
RN [6]
RP S-NITROSYLATION AT CYS-40 AND CYS-346, AND MUTAGENESIS OF CYS-40; CYS-346
RP AND CYS-426.
RX PubMed=23033481; DOI=10.1074/jbc.m112.397976;
RA Lohman A.W., Weaver J.L., Billaud M., Sandilos J.K., Griffiths R.,
RA Straub A.C., Penuela S., Leitinger N., Laird D.W., Bayliss D.A.,
RA Isakson B.E.;
RT "S-nitrosylation inhibits pannexin 1 channel function.";
RL J. Biol. Chem. 287:39602-39612(2012).
CC -!- FUNCTION: Structural component of the gap junctions and the
CC hemichannels. May play a role as a Ca(2+)-leak channel to regulate ER
CC Ca(2+) homeostasis (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Structural component of the gap junctions and the
CC hemichannels involved in the ATP release and nucleotide permeation. May
CC play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis.
CC Plays a critical role in oogenesis. {ECO:0000250|UniProtKB:Q96RD7}.
CC -!- SUBUNIT: Homohexamer. Forms homomeric or PANX1/PANX2-heteromeric
CC intercellular channels on coexpression in paired Xenopus oocytes.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9JIP4; P97382: Kcnab3; NbExp=2; IntAct=EBI-6272917, EBI-7261133;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96RD7};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}.
CC Cell junction, gap junction {ECO:0000250|UniProtKB:Q96RD7}. Endoplasmic
CC reticulum membrane {ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00351}.
CC -!- TISSUE SPECIFICITY: Widely expressed, including in cartilage, skin,
CC spleen and brain.
CC -!- PTM: S-nitrosylation inhibits channel currents and ATP release.
CC {ECO:0000269|PubMed:23033481}.
CC -!- PTM: N-glycosylation may play a role in cell surface targeting
CC (PubMed:17925379). Exists in three glycosylation states: non-
CC glycosylated (GLY0), high-mannose glycosylated (GLY1), and fully mature
CC glycosylated (GLY2) (By similarity). {ECO:0000250|UniProtKB:Q96RD7,
CC ECO:0000269|PubMed:17925379}.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF207817; AAF75838.1; -; mRNA.
DR EMBL; AK014033; BAB29125.1; -; mRNA.
DR EMBL; AK053871; BAC35567.1; -; mRNA.
DR EMBL; AK089764; BAC40956.1; -; mRNA.
DR EMBL; CH466522; EDL25014.1; -; Genomic_DNA.
DR EMBL; BC049074; AAH49074.1; -; mRNA.
DR CCDS; CCDS22832.1; -.
DR RefSeq; NP_062355.2; NM_019482.2.
DR AlphaFoldDB; Q9JIP4; -.
DR SMR; Q9JIP4; -.
DR IntAct; Q9JIP4; 4.
DR MINT; Q9JIP4; -.
DR STRING; 10090.ENSMUSP00000126405; -.
DR GlyGen; Q9JIP4; 1 site.
DR iPTMnet; Q9JIP4; -.
DR PhosphoSitePlus; Q9JIP4; -.
DR EPD; Q9JIP4; -.
DR MaxQB; Q9JIP4; -.
DR PaxDb; Q9JIP4; -.
DR PRIDE; Q9JIP4; -.
DR ProteomicsDB; 294158; -.
DR ABCD; Q9JIP4; 9 sequenced antibodies.
DR Antibodypedia; 1920; 263 antibodies from 38 providers.
DR DNASU; 55991; -.
DR Ensembl; ENSMUST00000164273; ENSMUSP00000126405; ENSMUSG00000031934.
DR GeneID; 55991; -.
DR KEGG; mmu:55991; -.
DR UCSC; uc009ofi.1; mouse.
DR CTD; 24145; -.
DR MGI; MGI:1860055; Panx1.
DR VEuPathDB; HostDB:ENSMUSG00000031934; -.
DR eggNOG; ENOG502QT58; Eukaryota.
DR GeneTree; ENSGT00940000153972; -.
DR HOGENOM; CLU_050054_1_0_1; -.
DR InParanoid; Q9JIP4; -.
DR OMA; IPDRFQC; -.
DR OrthoDB; 623546at2759; -.
DR PhylomeDB; Q9JIP4; -.
DR TreeFam; TF333142; -.
DR Reactome; R-MMU-112303; Electric Transmission Across Gap Junctions.
DR Reactome; R-MMU-844456; The NLRP3 inflammasome.
DR BioGRID-ORCS; 55991; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Panx1; mouse.
DR PRO; PR:Q9JIP4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JIP4; protein.
DR Bgee; ENSMUSG00000031934; Expressed in floor plate of midbrain and 222 other tissues.
DR ExpressionAtlas; Q9JIP4; baseline and differential.
DR Genevisible; Q9JIP4; MM.
DR GO; GO:0032059; C:bleb; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IPI:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR GO; GO:0005243; F:gap junction channel activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0022840; F:leak channel activity; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0022829; F:wide pore channel activity; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0006812; P:cation transport; ISO:MGI.
DR GO; GO:0007267; P:cell-cell signaling; ISO:MGI.
DR GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; IMP:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:MGI.
DR GO; GO:0033198; P:response to ATP; IMP:MGI.
DR GO; GO:0002931; P:response to ischemia; IGI:MGI.
DR InterPro; IPR000990; Innexin.
DR InterPro; IPR039099; Pannexin.
DR PANTHER; PTHR15759; PTHR15759; 1.
DR Pfam; PF00876; Innexin; 1.
DR PROSITE; PS51013; PANNEXIN; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Cell junction; Cell membrane;
KW Endoplasmic reticulum; Gap junction; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Reference proteome; S-nitrosylation;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..426
FT /note="Pannexin-1"
FT /id="PRO_0000208485"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 62..106
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 128..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 238..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 299..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 40
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:23033481"
FT MOD_RES 346
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:23033481"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17925379"
FT MUTAGEN 40
FT /note="C->A: Abolishes S-nitrosylation; when associated
FT with Ala-346."
FT /evidence="ECO:0000269|PubMed:23033481"
FT MUTAGEN 254
FT /note="N->Q: Impairs glycosylation."
FT /evidence="ECO:0000269|PubMed:17925379"
FT MUTAGEN 346
FT /note="C->A: Abolishes S-nitrosylation; when associated
FT with Ala-40."
FT /evidence="ECO:0000269|PubMed:23033481"
FT MUTAGEN 426
FT /note="C->A: No effect on S-nitrosylation."
FT /evidence="ECO:0000269|PubMed:23033481"
FT CONFLICT 296
FT /note="I -> T (in Ref. 1; AAF75838)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="A -> R (in Ref. 1; AAF75838)"
FT /evidence="ECO:0000305"
FT CONFLICT 422..426
FT /note="LNPSC -> CESVLLMVSFLNFKPVTSVADAPLLDL (in Ref. 1;
FT AAF75838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 48167 MW; 86AF6167C5D39565 CRC64;
MAIAHLATEY VFSDFLLKEP TEPKFKGLRL ELAVDKMVTC IAVGLPLLLI SLAFAQEISI
GTQISCFSPS SFSWRQAAFV DSYCWAAVQQ KSSLQSESGN LPLWLHKFFP YILLLFAILL
YLPALFWRFS AAPHLCSDLK FIMEELDKVY NRAIKAAKSA RDLDLRDGPG PPGVTENVGQ
SLWEISESHF KYPIVEQYLK TKKNSSHLIM KYISCRLVTF VVILLACIYL SYYFSLSSLS
DEFLCSIKSG VLKNDSTIPD RFQCKLIAVG IFQLLSLINL IVYALLIPVV VYTFFIPFRQ
KTDILKVYEI LPTFDVLHFK SEGYNDLSLY NLFLEENISE LKSYKCLKVL ENIKSNGQGI
DPMLLLTNLG MIKMDIIDGK IPTSLQTKGE DQGSQRVEFK DLDLSSEAAA NNGEKNSRQR
LLNPSC
