PANX2_RAT
ID PANX2_RAT Reviewed; 674 AA.
AC P60571;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Pannexin-2;
GN Name=Panx2; Synonyms=Px2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBUNIT.
RC STRAIN=Wistar; TISSUE=Hippocampus;
RX PubMed=14597722; DOI=10.1073/pnas.2233464100;
RA Bruzzone R., Hormuzdi S.G., Barbe M., Herb A., Monyer H.;
RT "Pannexins, a family of gap junction proteins expressed in brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13644-13649(2003).
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. {ECO:0000269|PubMed:14597722}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC junction.
CC -!- TISSUE SPECIFICITY: Expressed in the eye, thyroid, prostate, kidney and
CC liver. Abundantly expressed in the CNS, including hippocampus,
CC olfactory bulb, cortex, cerebellum. Not detected in the white matter.
CC {ECO:0000269|PubMed:14597722}.
CC -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00351}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD89523.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ557016; CAD89523.1; ALT_INIT; mRNA.
DR RefSeq; NP_955441.2; NM_199409.2.
DR AlphaFoldDB; P60571; -.
DR SMR; P60571; -.
DR STRING; 10116.ENSRNOP00000047054; -.
DR GlyGen; P60571; 1 site.
DR PaxDb; P60571; -.
DR PRIDE; P60571; -.
DR ABCD; P60571; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000089707; ENSRNOP00000069647; ENSRNOG00000055530.
DR GeneID; 362979; -.
DR KEGG; rno:362979; -.
DR CTD; 56666; -.
DR RGD; 735191; Panx2.
DR eggNOG; ENOG502QT63; Eukaryota.
DR InParanoid; P60571; -.
DR OrthoDB; 334559at2759; -.
DR PhylomeDB; P60571; -.
DR TreeFam; TF333142; -.
DR Reactome; R-RNO-112303; Electric Transmission Across Gap Junctions.
DR PRO; PR:P60571; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; IBA:GO_Central.
DR GO; GO:0015267; F:channel activity; ISO:RGD.
DR GO; GO:0005243; F:gap junction channel activity; IMP:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IMP:RGD.
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; IMP:RGD.
DR GO; GO:0032732; P:positive regulation of interleukin-1 production; IEA:InterPro.
DR GO; GO:0002931; P:response to ischemia; ISO:RGD.
DR GO; GO:0055085; P:transmembrane transport; ISO:RGD.
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 Cell junction; Cell membrane; Gap junction; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..674
FT /note="Pannexin-2"
FT /id="PRO_0000208490"
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..674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 394..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..510
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 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IMP4"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IMP4"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 674 AA; 74434 MW; 9E8C82865CDA4751 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 FIFDKLHKVG IKTRRQWRRS QFCDINILAM FCNENRDHIK
SLNRLDFITN ESDLMYDNVV RQLLAALAQS NHDTTPTVRD SGIQTVDPSI NPAEPEGSAE
PPVVKRPRKK MKWIPTSNPL PQPFKEQLAI MRVENSKTEK PKPVRRKTAT DTLIAPLLDA
GARAAHHYKG SGGDTGPSSA PPAASEKKHT RHFSLDVHPY ILGSKKAKTE AVPPALPASR
SQEGGFLSQT EECGLGLAAA PTKDAPLPEK EIPYPTESAL PSGGPFHVCS PPTASAAASL
SPSSLGKADP LTILSRNATH PLLHISTLYE AREEEEGGPC APSDMGDLLS IPPPQQILIA
TFEEPRTVVS TVEF
