CXA3_MOUSE
ID CXA3_MOUSE Reviewed; 417 AA.
AC Q64448; B2RRM1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Gap junction alpha-3 protein;
DE AltName: Full=Connexin-46;
DE Short=Cx46;
GN Name=Gja3;
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=C57BL/6 X CBA;
RA Kumar N.M., Nishi M., Klier F.G., Gilula N.B.;
RT "Characterization and expression of a lens gap junction connexin.";
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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).
CC -!- FUNCTION: Structural component of lens fiber gap junctions. Gap
CC junctions are dodecameric channels that connect the cytoplasm of
CC adjoining cells. They are formed by the docking of two hexameric
CC hemichannels, one from each cell membrane. Small molecules and ions
CC diffuse from one cell to a neighboring cell via the central pore.
CC {ECO:0000250|UniProtKB:Q9TU17}.
CC -!- SUBUNIT: A hemichannel or connexon is composed of a hexamer of
CC connexins. A functional gap junction is formed by the apposition of two
CC hemichannels. Forms heteromeric channels with GJA8.
CC {ECO:0000250|UniProtKB:Q9TU17}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9TU17};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9TU17}. Cell
CC junction, gap junction {ECO:0000250|UniProtKB:Q9TU17}.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
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DR EMBL; U44955; AAB03211.1; -; Genomic_DNA.
DR EMBL; CH466535; EDL36182.1; -; Genomic_DNA.
DR EMBL; CH466535; EDL36184.1; -; Genomic_DNA.
DR EMBL; BC138492; AAI38493.1; -; mRNA.
DR EMBL; BC138493; AAI38494.1; -; mRNA.
DR CCDS; CCDS27152.1; -.
DR RefSeq; NP_001258552.1; NM_001271623.1.
DR RefSeq; NP_058671.2; NM_016975.3.
DR RefSeq; XP_011243261.1; XM_011244959.1.
DR AlphaFoldDB; Q64448; -.
DR SMR; Q64448; -.
DR STRING; 10090.ENSMUSP00000059587; -.
DR PhosphoSitePlus; Q64448; -.
DR PaxDb; Q64448; -.
DR PRIDE; Q64448; -.
DR ProteomicsDB; 284071; -.
DR Antibodypedia; 22305; 217 antibodies from 31 providers.
DR DNASU; 14611; -.
DR Ensembl; ENSMUST00000061614; ENSMUSP00000059587; ENSMUSG00000048582.
DR GeneID; 14611; -.
DR KEGG; mmu:14611; -.
DR UCSC; uc007ucv.2; mouse.
DR CTD; 2700; -.
DR MGI; MGI:95714; Gja3.
DR VEuPathDB; HostDB:ENSMUSG00000048582; -.
DR eggNOG; ENOG502QUKJ; Eukaryota.
DR GeneTree; ENSGT01050000244864; -.
DR HOGENOM; CLU_037388_0_0_1; -.
DR InParanoid; Q64448; -.
DR OMA; VEMHAPP; -.
DR OrthoDB; 969321at2759; -.
DR PhylomeDB; Q64448; -.
DR TreeFam; TF329606; -.
DR Reactome; R-MMU-190861; Gap junction assembly.
DR BioGRID-ORCS; 14611; 0 hits in 74 CRISPR screens.
DR PRO; PR:Q64448; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q64448; protein.
DR Bgee; ENSMUSG00000048582; Expressed in epithelium of lens and 66 other tissues.
DR ExpressionAtlas; Q64448; baseline and differential.
DR Genevisible; Q64448; MM.
DR GO; GO:0005922; C:connexin complex; ISS:UniProtKB.
DR GO; GO:0005921; C:gap junction; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005243; F:gap junction channel activity; ISO:MGI.
DR GO; GO:0055077; F:gap junction hemi-channel activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:1990349; P:gap junction-mediated intercellular transport; ISS:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0009268; P:response to pH; ISO:MGI.
DR GO; GO:0007601; P:visual perception; IEA:InterPro.
DR Gene3D; 1.20.1440.80; -; 1.
DR InterPro; IPR000500; Connexin.
DR InterPro; IPR002262; Connexin46.
DR InterPro; IPR034634; Connexin_C.
DR InterPro; IPR019570; Connexin_CCC.
DR InterPro; IPR017990; Connexin_CS.
DR InterPro; IPR013092; Connexin_N.
DR InterPro; IPR038359; Connexin_N_sf.
DR PANTHER; PTHR11984; PTHR11984; 1.
DR PANTHER; PTHR11984:SF12; PTHR11984:SF12; 1.
DR Pfam; PF00029; Connexin; 1.
DR PRINTS; PR00206; CONNEXIN.
DR PRINTS; PR01133; CONNEXINA3.
DR SMART; SM00037; CNX; 1.
DR SMART; SM01089; Connexin_CCC; 1.
DR SUPFAM; SSF118220; SSF118220; 1.
DR PROSITE; PS00407; CONNEXINS_1; 1.
DR PROSITE; PS00408; CONNEXINS_2; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Disulfide bond; Gap junction; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT CHAIN 2..417
FT /note="Gap junction alpha-3 protein"
FT /id="PRO_0000057811"
FT INTRAMEM 2..15
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT TOPO_DOM 16..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT TOPO_DOM 41..71
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT TOPO_DOM 93..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT TOPO_DOM 180..207
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT TOPO_DOM 229..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 110..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 54..198
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT DISULFID 61..192
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT DISULFID 65..187
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT CONFLICT 261
FT /note="T -> A (in Ref. 1; AAB03211)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> G (in Ref. 1; AAB03211)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="H -> Y (in Ref. 1; AAB03211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 46321 MW; FF235977E26F55F0 CRC64;
MGDWSFLGRL LENAQEHSTV IGKVWLTVLF IFRILVLGAA AEEVWGDEQS DFTCNTQQPG
CENVCYDRAF PISHIRFWAL QIIFVSTPTL IYLGHVLHIV RMEEKKKERE EELLRRDNPQ
HGRGREPMRT GSPRDPPLRD DRGKVRIAGA LLRTYVFNII FKTLFEVGFI AGQYFLYGFQ
LQPLYRCDRW PCPNTVDCFI SRPTEKTIFV IFMLAVACAS LVLNMLEIYH LGWKKLKQGV
TNHFNPDASE ARHKPLDPLP TATSSGPPSV SIGFPPYYTH PACPTVQAKA IGFPGAPLSP
ADFTVVTLND AQGRNHPVKH CNGHHLTTEQ NWTRQVAEQQ TPASKPSSAA SSPDGRKGLI
DSSGSSLQES ALVVTPEEGE QALATTVEMH SPPLVLLDPG RSSKSSNGRA RPGDLAI
