ID   CXD3_MOUSE              Reviewed;         278 AA.
AC   Q91YD1; Q80ZH0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 137.
DE   RecName: Full=Gap junction delta-3 protein;
DE   AltName: Full=Connexin-30.2;
DE            Short=Cx30.2;
DE   AltName: Full=Gap junction alpha-11 protein;
DE   AltName: Full=Gap junction chi-1 protein;
GN   Name=Gjd3; Synonyms=Gja11, Gjc1;
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 [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=12108537; DOI=10.1515/bc.2002.076;
RA   Willecke K., Eiberger J., Degen J., Eckardt D., Romualdi A., Guldenagel M.,
RA   Deutsch U., Soehl G.;
RT   "Structural and functional diversity of connexin genes in the mouse and
RT   human genome.";
RL   Biol. Chem. 383:725-737(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=12681499; DOI=10.1016/s0014-5793(03)00252-7;
RA   Nielsen P.A., Kumar N.M.;
RT   "Differences in expression patterns between mouse connexin-30.2 (Cx30.2)
RT   and its putative human orthologue, connexin-31.9.";
RL   FEBS Lett. 540:151-156(2003).
RN   [3]
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).
CC   -!- FUNCTION: One gap junction consists of a cluster of closely packed
CC       pairs of transmembrane channels, the connexons, through which materials
CC       of low MW diffuse from one cell to a neighboring cell. {ECO:0000250}.
CC   -!- SUBUNIT: A connexon is composed of a hexamer of connexins.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the connexin family. Delta-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ414561; CAC93843.1; -; Genomic_DNA.
DR   EMBL; AY166870; AAN65188.1; -; Genomic_DNA.
DR   EMBL; AL591067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS25369.1; -.
DR   RefSeq; NP_848711.2; NM_178596.2.
DR   AlphaFoldDB; Q91YD1; -.
DR   SMR; Q91YD1; -.
DR   BioGRID; 237256; 1.
DR   STRING; 10090.ENSMUSP00000055246; -.
DR   iPTMnet; Q91YD1; -.
DR   PhosphoSitePlus; Q91YD1; -.
DR   PaxDb; 10090-ENSMUSP00000055246; -.
DR   Antibodypedia; 51141; 34 antibodies from 13 providers.
DR   DNASU; 353155; -.
DR   Ensembl; ENSMUST00000062931.2; ENSMUSP00000055246.2; ENSMUSG00000047197.2.
DR   GeneID; 353155; -.
DR   KEGG; mmu:353155; -.
DR   UCSC; uc007lib.1; mouse.
DR   AGR; MGI:2384150; -.
DR   CTD; 125111; -.
DR   MGI; MGI:2384150; Gjd3.
DR   VEuPathDB; HostDB:ENSMUSG00000047197; -.
DR   eggNOG; ENOG502R6H2; Eukaryota.
DR   GeneTree; ENSGT01090000260005; -.
DR   HOGENOM; CLU_037388_4_2_1; -.
DR   InParanoid; Q91YD1; -.
DR   OMA; YSMHQAS; -.
DR   OrthoDB; 4504241at2759; -.
DR   PhylomeDB; Q91YD1; -.
DR   TreeFam; TF329606; -.
DR   Reactome; R-MMU-190861; Gap junction assembly.
DR   BioGRID-ORCS; 353155; 4 hits in 79 CRISPR screens.
DR   ChiTaRS; Gjd3; mouse.
DR   PRO; PR:Q91YD1; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q91YD1; Protein.
DR   Bgee; ENSMUSG00000047197; Expressed in spermatocyte and 28 other cell types or tissues.
DR   ExpressionAtlas; Q91YD1; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005922; C:connexin complex; IGI:MGI.
DR   GO; GO:0005921; C:gap junction; IDA:MGI.
DR   GO; GO:0005243; F:gap junction channel activity; ISO:MGI.
DR   GO; GO:0086077; F:gap junction channel activity involved in AV node cell-bundle of His cell electrical coupling; IMP:BHF-UCL.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IDA:MGI.
DR   GO; GO:0086053; P:AV node cell to bundle of His cell communication by electrical coupling; IMP:BHF-UCL.
DR   GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR   GO; GO:0016264; P:gap junction assembly; ISS:UniProtKB.
DR   GO; GO:1903780; P:negative regulation of cardiac conduction; IMP:BHF-UCL.
DR   GO; GO:1901845; P:negative regulation of cell communication by electrical coupling involved in cardiac conduction; IMP:BHF-UCL.
DR   GO; GO:0010459; P:negative regulation of heart rate; IMP:BHF-UCL.
DR   GO; GO:0009749; P:response to glucose; ISO:MGI.
DR   Gene3D; 1.20.1440.80; Gap junction channel protein cysteine-rich domain; 1.
DR   InterPro; IPR000500; Connexin.
DR   InterPro; IPR019570; Connexin_CCC.
DR   InterPro; IPR017990; Connexin_CS.
DR   InterPro; IPR013092; Connexin_N.
DR   InterPro; IPR038359; Connexin_N_sf.
DR   PANTHER; PTHR11984; CONNEXIN; 1.
DR   PANTHER; PTHR11984:SF5; GAP JUNCTION DELTA-3 PROTEIN; 1.
DR   Pfam; PF00029; Connexin; 1.
DR   PRINTS; PR00206; CONNEXIN.
DR   SMART; SM00037; CNX; 1.
DR   SMART; SM01089; Connexin_CCC; 1.
DR   PROSITE; PS00408; CONNEXINS_2; 1.
PE   3: Inferred from homology;
KW   Cell junction; Cell membrane; Gap junction; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..278
FT                   /note="Gap junction delta-3 protein"
FT                   /id="PRO_0000313009"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..76
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          223..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..240
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        13..16
FT                   /note="AVQL -> PLQV (in Ref. 2; AAN65188)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="A -> S (in Ref. 2; AAN65188)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   278 AA;  30220 MW;  A8A3DC827D070DE9 CRC64;
     MGEWAFLGSL LDAVQLQSPL VGRLWLVIML IFRILVLATV GGAVFEDEQE EFVCNTLQPG
     CRQTCYDRAF PVSHYRFWLF HILLLSAPPV LFVIYSMHQA SKEAGGAQLA PPCARGRAEA
     PCSPCALRAR RARRCYLLSV ALRLLAELAF LGGQALLYGF RVDPHYACAG PPCPHTVDCF
     VSRPTEKTVF VVFYFAVGLL SALLSVAELG HLLWKGRQRA KLLPPPPPSP SLPSQRGDPD
     PFGPPAYAHR SPAGDSEGEG GSGHSKASLA TVRQDLAI
//