CXA8_RAT
ID CXA8_RAT Reviewed; 440 AA.
AC Q8K4Q9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Gap junction alpha-8 protein;
DE AltName: Full=Connexin-50;
DE Short=Cx50;
GN Name=Gja8;
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 [GENOMIC DNA], AND VARIANT CATARACT TRP-340.
RC STRAIN=Brown Norway; TISSUE=Liver;
RX PubMed=12356818;
RA Yamashita S., Furumoto K., Nobukiyo A., Kamohara M., Ushijima T.,
RA Furukawa T.;
RT "Mapping of a gene responsible for cataract formation and its modifier in
RT the UPL rat.";
RL Invest. Ophthalmol. Vis. Sci. 43:3153-3159(2002).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=1325220; DOI=10.1091/mbc.3.7.711;
RA White T.W., Bruzzone R., Goodenough D.A., Paul D.L.;
RT "Mouse Cx50, a functional member of the connexin family of gap junction
RT proteins, is the lens fiber protein MP70.";
RL Mol. Biol. Cell 3:711-720(1992).
CC -!- FUNCTION: Structural component of eye lens gap junctions. Gap junctions
CC are dodecameric channels that connect the cytoplasm of adjoining cells.
CC They are formed by the docking of two hexameric hemichannels, one from
CC each cell membrane. Small molecules and ions diffuse from one cell to a
CC neighboring cell via the central pore. {ECO:0000250|UniProtKB:P55917}.
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 GJA3.
CC {ECO:0000250|UniProtKB:P55917}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P55917};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P55917}. Cell
CC junction, gap junction {ECO:0000250|UniProtKB:P55917}.
CC -!- TISSUE SPECIFICITY: Detected in eye lens (at protein level).
CC {ECO:0000269|PubMed:1325220}.
CC -!- DISEASE: Note=Defects in Gja8 are the cause of cataract.
CC {ECO:0000269|PubMed:12356818}.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
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DR EMBL; AB078344; BAC06574.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8K4Q9; -.
DR SMR; Q8K4Q9; -.
DR STRING; 10116.ENSRNOP00000066975; -.
DR PhosphoSitePlus; Q8K4Q9; -.
DR PaxDb; Q8K4Q9; -.
DR Ensembl; ENSRNOT00000071622; ENSRNOP00000066975; ENSRNOG00000046703.
DR RGD; 628890; Gja8.
DR eggNOG; ENOG502QV1K; Eukaryota.
DR GeneTree; ENSGT01050000244864; -.
DR HOGENOM; CLU_037388_0_0_1; -.
DR InParanoid; Q8K4Q9; -.
DR OMA; MYVGHAV; -.
DR PhylomeDB; Q8K4Q9; -.
DR Reactome; R-RNO-190861; Gap junction assembly.
DR PRO; PR:Q8K4Q9; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000046703; Expressed in testis.
DR ExpressionAtlas; Q8K4Q9; baseline and differential.
DR GO; GO:0005922; C:connexin complex; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005243; F:gap junction channel activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR GO; GO:0007267; P:cell-cell signaling; IDA:RGD.
DR GO; GO:1990349; P:gap junction-mediated intercellular transport; ISS:UniProtKB.
DR GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD.
DR GO; GO:1902551; P:regulation of catalase activity; IMP:RGD.
DR GO; GO:1903282; P:regulation of glutathione peroxidase activity; IMP:RGD.
DR GO; GO:0032645; P:regulation of granulocyte macrophage colony-stimulating factor production; IMP:RGD.
DR Gene3D; 1.20.1440.80; -; 1.
DR InterPro; IPR000500; Connexin.
DR InterPro; IPR002266; Connexin50.
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:SF19; PTHR11984:SF19; 1.
DR Pfam; PF00029; Connexin; 1.
DR Pfam; PF03509; Connexin50; 1.
DR PRINTS; PR00206; CONNEXIN.
DR PRINTS; PR01137; CONNEXINA8.
DR SMART; SM00037; CNX; 1.
DR SMART; SM01089; Connexin_CCC; 1.
DR PROSITE; PS00407; CONNEXINS_1; 1.
DR PROSITE; PS00408; CONNEXINS_2; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Disease variant; Disulfide bond;
KW Gap junction; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P55917"
FT CHAIN 2..440
FT /note="Gap junction alpha-8 protein"
FT /id="PRO_0000313005"
FT INTRAMEM 2..12
FT /evidence="ECO:0000250|UniProtKB:P55917"
FT TOPO_DOM 13..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55917"
FT TOPO_DOM 43..71
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55917"
FT TOPO_DOM 93..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55917"
FT TOPO_DOM 183..210
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P55917"
FT TOPO_DOM 232..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 111..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 54..201
FT /evidence="ECO:0000250|UniProtKB:P55917"
FT DISULFID 61..195
FT /evidence="ECO:0000250|UniProtKB:P55917"
FT DISULFID 65..190
FT /evidence="ECO:0000250|UniProtKB:P55917"
FT VARIANT 340
FT /note="R -> W (in cataract)"
FT /evidence="ECO:0000269|PubMed:12356818"
SQ SEQUENCE 440 AA; 49401 MW; DDF57B9D6E1016AF CRC64;
MGDWSFLGNI LEEVNEHSTV IGRVWLTVLF IFRILILGTA AEFVWGDEQS DFVCNTQQPG
CENVCYDEAF PISHIRLWVL QIIFVSTPSL MYVGHAVHHV RMEEKRKDRE AEELCQQSRS
NGGERVPIAP DQASIRKSSS SSKGTKKFRL EGTLLRTYVC HIIFKTLFEV GFIVGHYFLY
GFRILPLYRC SRWPCPNVVD CFVSRPTEKT IFILFMLSVA FVSLFLNIME MSHLGMKGIR
SAFKRPAEQP LGEIAEKSLH SIAVSSIQKA KGYQLLEEEK IVSHYFPLTE VGMVETSPLS
AKPFSQFEEK IGTGPLADMS RGYQETLPSY AQVGAQEVER EEQPVEEAVE PEVGEKKQEA
EKVAPEGQET VAVPDGEKVE TPGVGKDDEK EELQAEKVTK QGLSAEKAPT LCPELTTDDN
RPLSRLSKAS SRARSDDLTI
