PANX2_MOUSE
ID PANX2_MOUSE Reviewed; 677 AA.
AC Q6IMP4; B1PL20; Q4JGM2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Pannexin-2;
GN Name=Panx2;
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] (ISOFORM 2).
RA Skoblov M., Baranova A.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-677 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Dvoriantchikova G., Ivanov D., Pestova A., Shestopalov V.;
RT "Molecular characterization of pannexins in the lens.";
RL Mol. Vis. 12:1417-1426(2006).
RN [4]
RP IDENTIFICATION.
RX PubMed=15028292; DOI=10.1016/j.ygeno.2003.09.025;
RA Baranova A., Ivanov D., Petrash N., Pestova A., Skoblov M., Kelmanson I.,
RA Shagin D., Nazarenko S., Geraymovych E., Litvin O., Tiunova A., Born T.L.,
RA Usman N., Staroverov D., Lukyanov S., Panchin Y.;
RT "The mammalian pannexin family is homologous to the invertebrate innexin
RT gap junction proteins.";
RL Genomics 83:706-716(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593 AND SER-604, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Structural component of the gap junctions and the
CC hemichannels.
CC -!- SUBUNIT: Forms PANX1/PANX2-heteromeric intercellular channels on
CC coexpression in paired Xenopus oocytes. Does not form homomeric
CC channels (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC junction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6IMP4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IMP4-2; Sequence=VSP_039093, VSP_039094;
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
CC -!- SEQUENCE CAUTION:
CC Sequence=DAA00307.1; Type=Frameshift; Evidence={ECO:0000305};
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; EU446266; ACA30452.1; -; mRNA.
DR EMBL; AC113069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ093579; AAY98749.1; -; mRNA.
DR EMBL; BK000624; DAA00307.1; ALT_FRAME; mRNA.
DR CCDS; CCDS49695.1; -. [Q6IMP4-1]
DR RefSeq; NP_001002005.2; NM_001002005.2. [Q6IMP4-1]
DR AlphaFoldDB; Q6IMP4; -.
DR SMR; Q6IMP4; -.
DR STRING; 10090.ENSMUSP00000124354; -.
DR GlyConnect; 2575; 1 N-Linked glycan (1 site).
DR GlyGen; Q6IMP4; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q6IMP4; -.
DR PhosphoSitePlus; Q6IMP4; -.
DR PaxDb; Q6IMP4; -.
DR PeptideAtlas; Q6IMP4; -.
DR PRIDE; Q6IMP4; -.
DR ProteomicsDB; 294326; -. [Q6IMP4-1]
DR ProteomicsDB; 294327; -. [Q6IMP4-2]
DR Antibodypedia; 14165; 186 antibodies from 29 providers.
DR DNASU; 406218; -.
DR Ensembl; ENSMUST00000161372; ENSMUSP00000125514; ENSMUSG00000058441. [Q6IMP4-2]
DR Ensembl; ENSMUST00000162424; ENSMUSP00000124354; ENSMUSG00000058441. [Q6IMP4-1]
DR GeneID; 406218; -.
DR KEGG; mmu:406218; -.
DR UCSC; uc007xfa.2; mouse. [Q6IMP4-1]
DR UCSC; uc011zxq.1; mouse. [Q6IMP4-2]
DR CTD; 56666; -.
DR MGI; MGI:1890615; Panx2.
DR VEuPathDB; HostDB:ENSMUSG00000058441; -.
DR eggNOG; ENOG502QT63; Eukaryota.
DR GeneTree; ENSGT00940000153972; -.
DR HOGENOM; CLU_027715_0_0_1; -.
DR InParanoid; Q6IMP4; -.
DR OMA; GQQDDKA; -.
DR OrthoDB; 334559at2759; -.
DR PhylomeDB; Q6IMP4; -.
DR TreeFam; TF333142; -.
DR Reactome; R-MMU-112303; Electric Transmission Across Gap Junctions.
DR BioGRID-ORCS; 406218; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q6IMP4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q6IMP4; protein.
DR Bgee; ENSMUSG00000058441; Expressed in medial vestibular nucleus and 103 other tissues.
DR ExpressionAtlas; Q6IMP4; baseline and differential.
DR Genevisible; Q6IMP4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0005243; F:gap junction channel activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR GO; GO:0022829; F:wide pore channel activity; IBA:GO_Central.
DR GO; GO:0006812; P:cation transport; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; ISO:MGI.
DR GO; GO:0032732; P:positive regulation of interleukin-1 production; IEA:InterPro.
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 Alternative splicing; Cell junction; Cell membrane; Gap junction;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..677
FT /note="Pannexin-2"
FT /id="PRO_0000208489"
FT TOPO_DOM 11..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 75..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 147..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 252..295
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT TOPO_DOM 317..617
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 394..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 75
FT /note="A -> AARVSSLPS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039093"
FT VAR_SEQ 632..677
FT /note="YEAREEEEGGPCAPSDMGDLLSIPPPQQILIATFEEPRTVVSTVEF -> SS
FT SPPSRSREQL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039094"
FT CONFLICT 47
FT /note="E -> G (in Ref. 1; ACA30452)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="G -> D (in Ref. 1; ACA30452)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="K -> E (in Ref. 1; ACA30452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 677 AA; 74614 MW; 38B0BE8B5771FD35 CRC64;
MHHLLEQSAD MATALLAGEK LRELILPGSQ DDKAGALAAL LLQLKLELPF DRVVTIGTVL
VPILLVTLVF TKNFAEEPIY CYTPHNFTRD QALYARGYCW TELRDALPGV DASLWPSLFE
HKFLPYALLA FAAIMYVPAL GWEFLASTRL TSELNFLLQE IDNCYHRAAE GRAPKIEKQI
QSKGPGITER EKREIIENAE KEKSPEQNLF EKYLERRGRS NFLAKLYLAR HVLILLLSVV
PISYLCTYYA TQKQNEFTCA LGASPDGPVG SAGPTVRVSC KLPSVQLQRI IAGVDIVLLC
FMNLIILVNL IHLFIFRKSN FIFDKLNKVG IKTRRQWRRS QFCDINILAM FCNENRDHIK
SLNRLDFITN ESDLMYDNVV RQLLAALAQS NHDTTPTVRD SGIQTVDPSI NPAEPDGSAE
PPVVKRPRKK MKWIPTSNPL PQPFKEQLAI MRVENSKTEK PKPVRRKTAT DTLIAPLLDA
GARAAHHYKG SGGDSGPSSA PPAASEKKHT RHFSLDVHPY ILGTKKAKTE AVPPALPASR
SQEGGFLSQT EECGLGLAAA PTKDAPLPEK EIPYPTEPAL PGLPSGGSFH VCSPPAAPAA
ASLSPGSLGK ADPLTILSRN ATHPLLHIST LYEAREEEEG GPCAPSDMGD LLSIPPPQQI
LIATFEEPRT VVSTVEF
