CXA3_RAT
ID CXA3_RAT Reviewed; 416 AA.
AC P29414;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Gap junction alpha-3 protein;
DE AltName: Full=Connexin-46;
DE Short=Cx46 {ECO:0000303|PubMed:1659572};
GN Name=Gja3; Synonyms=Cxn-46;
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, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RC STRAIN=CD Charles River; TISSUE=Lens;
RX PubMed=1659572; DOI=10.1083/jcb.115.4.1077;
RA Paul D.L., Ebihara L., Takemoto L.J., Swenson K.I., Goodenough D.A.;
RT "Connexin46, a novel lens gap junction protein, induces voltage-gated
RT currents in nonjunctional plasma membrane of Xenopus oocytes.";
RL J. Cell Biol. 115:1077-1089(1991).
CC -!- FUNCTION: Structural component of lens fiber gap junctions (Probable).
CC Gap 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 (By similarity). Small
CC molecules and ions diffuse from one cell to a neighboring cell via the
CC central pore (Probable). {ECO:0000250|UniProtKB:Q9TU17,
CC ECO:0000305|PubMed:1659572}.
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:0000269|PubMed:1659572};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9TU17}. Cell
CC junction, gap junction {ECO:0000250|UniProtKB:Q9TU17}.
CC -!- TISSUE SPECIFICITY: Detected in eye lens (at protein level). Most
CC abundant in lens, but also present in heart and kidney.
CC {ECO:0000269|PubMed:1659572}.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
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DR EMBL; X57970; CAA41036.1; -; mRNA.
DR PIR; S25764; S25764.
DR RefSeq; NP_077352.1; NM_024376.2.
DR AlphaFoldDB; P29414; -.
DR SMR; P29414; -.
DR STRING; 10116.ENSRNOP00000011699; -.
DR PaxDb; P29414; -.
DR GeneID; 79217; -.
DR KEGG; rno:79217; -.
DR UCSC; RGD:621820; rat.
DR CTD; 2700; -.
DR RGD; 621820; Gja3.
DR eggNOG; ENOG502QUKJ; Eukaryota.
DR InParanoid; P29414; -.
DR OrthoDB; 969321at2759; -.
DR PhylomeDB; P29414; -.
DR Reactome; R-RNO-190861; Gap junction assembly.
DR PRO; PR:P29414; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005922; C:connexin complex; ISS:UniProtKB.
DR GO; GO:0005921; C:gap junction; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005243; F:gap junction channel activity; IDA:RGD.
DR GO; GO:0055077; F:gap junction hemi-channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0009268; P:response to pH; IDA:RGD.
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 1: Evidence at protein 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..416
FT /note="Gap junction alpha-3 protein"
FT /id="PRO_0000057812"
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..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 110..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..370
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"
SQ SEQUENCE 416 AA; 46013 MW; 8232B98E0C3A1F8C 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 VRHKPLDPLS EAANSGPPSV SIGLPPYYTH PACPTVQGKA TGFPGAPLLP
ADFTVVTLND AQGRGHPVKH CNGHHLTTEQ NWASLGAEPQ TPASKPSSAA SSPHGRKGLT
DSSGSSLEES ALVVTPEGEQ ALATTVEMHS PPLVLLDPER SSKSSSGRAR PGDLAI
