ID   PANX3_RAT               Reviewed;         392 AA.
AC   P60572;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Pannexin-3;
GN   Name=Panx3; Synonyms=Px3;
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].
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap
CC       junction.
CC   -!- TISSUE SPECIFICITY: Skin.
CC   -!- SIMILARITY: Belongs to the pannexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00351}.
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DR   EMBL; AJ557017; CAD89524.1; -; mRNA.
DR   RefSeq; NP_955430.1; NM_199398.1.
DR   AlphaFoldDB; P60572; -.
DR   SMR; P60572; -.
DR   STRING; 10116.ENSRNOP00000041185; -.
DR   GlyGen; P60572; 1 site.
DR   PaxDb; P60572; -.
DR   PRIDE; P60572; -.
DR   Ensembl; ENSRNOT00000042717; ENSRNOP00000041185; ENSRNOG00000031675.
DR   GeneID; 315567; -.
DR   KEGG; rno:315567; -.
DR   UCSC; RGD:735137; rat.
DR   CTD; 116337; -.
DR   RGD; 735137; Panx3.
DR   eggNOG; ENOG502QRDI; Eukaryota.
DR   GeneTree; ENSGT00940000153972; -.
DR   HOGENOM; CLU_050054_1_0_1; -.
DR   InParanoid; P60572; -.
DR   OMA; SDPYVFW; -.
DR   OrthoDB; 623546at2759; -.
DR   PhylomeDB; P60572; -.
DR   TreeFam; TF333142; -.
DR   PRO; PR:P60572; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Genevisible; P60572; RN.
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: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   InterPro; IPR000990; Innexin.
DR   InterPro; IPR039099; Pannexin.
DR   PANTHER; PTHR15759; PTHR15759; 1.
DR   Pfam; PF00876; Innexin; 1.
DR   PROSITE; PS51013; PANNEXIN; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Gap junction; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..392
FT                   /note="Pannexin-3"
FT                   /id="PRO_0000208493"
FT   TOPO_DOM        1..39
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        61..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        135..215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        237..267
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00351"
FT   TOPO_DOM        289..392
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   392 AA;  44978 MW;  5D45C6FB4A3389F7 CRC64;
     MSLAHTAAEY MLSDALLPDR RGSRLKGLRL ELPLDKMVKF VTVGFPLLLM SLAFAQEFSS
     GSPISCFSPS NFSVRQAVFV DSSCWDSLAH YKQDEAGQYT VKSLWPHKAL PYSLLALAVA
     MYLPVLLWQY AAVPALSSDL LFIISELDKS YNRSIRLVQH MLKIRQKSSD PHVFWDELEK
     ARKERYFEFP LLERYLACKQ RSHWLVATYL LRNALLLLFT SATYLYLGHF HLDVFFQEEF
     SCSIKTGLLH EETHVPELIT CRLTSLSVFQ IVSVSSVAIY TVLVPVIIYN LTRLCRWDKR
     LLSIYEMLPA FDLLSRKMLG CPINDLNVIL LFLRANISEL ISFSWLSVLC VLKDTTTQKH
     NIDTVVDFMT LLAGLEPSKP KHLTQHTYDE HP