CXA8_MOUSE
ID CXA8_MOUSE Reviewed; 440 AA.
AC P28236;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Gap junction alpha-8 protein;
DE AltName: Full=Connexin-50;
DE Short=Cx50;
DE AltName: Full=Lens fiber protein MP70 {ECO:0000303|PubMed:1325220};
GN Name=Gja8;
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], FUNCTION, SUBCELLULAR LOCATION, AND
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).
RN [2]
RP PROTEIN SEQUENCE OF 379-390, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: Structural component of eye lens gap junctions
CC (PubMed:1325220). Gap junctions are dodecameric channels that connect
CC the cytoplasm of adjoining cells. They are formed by the docking of two
CC hexameric hemichannels, one from each cell membrane (By similarity).
CC Small molecules and ions diffuse from one cell to a neighboring cell
CC via the central pore (PubMed:1325220). {ECO:0000250|UniProtKB:P55917,
CC ECO:0000269|PubMed:1325220}.
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:0000269|PubMed:1325220};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P55917}. Cell
CC junction, gap junction {ECO:0000305|PubMed:1325220}.
CC -!- TISSUE SPECIFICITY: Detected in eye lens (at protein level). Eye lens.
CC {ECO:0000269|PubMed:1325220}.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
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DR EMBL; M91243; AAA37497.1; -; Genomic_DNA.
DR CCDS; CCDS17651.1; -.
DR PIR; I49624; I49624.
DR RefSeq; NP_032149.1; NM_008123.3.
DR AlphaFoldDB; P28236; -.
DR SMR; P28236; -.
DR STRING; 10090.ENSMUSP00000049532; -.
DR PhosphoSitePlus; P28236; -.
DR PaxDb; P28236; -.
DR PRIDE; P28236; -.
DR ProteomicsDB; 279243; -.
DR Antibodypedia; 33981; 258 antibodies from 27 providers.
DR DNASU; 14616; -.
DR Ensembl; ENSMUST00000062944; ENSMUSP00000049532; ENSMUSG00000049908.
DR GeneID; 14616; -.
DR KEGG; mmu:14616; -.
DR UCSC; uc008qon.2; mouse.
DR CTD; 2703; -.
DR MGI; MGI:99953; Gja8.
DR VEuPathDB; HostDB:ENSMUSG00000049908; -.
DR eggNOG; ENOG502QV1K; Eukaryota.
DR GeneTree; ENSGT01050000244864; -.
DR HOGENOM; CLU_037388_0_0_1; -.
DR InParanoid; P28236; -.
DR OMA; MYVGHAV; -.
DR OrthoDB; 814925at2759; -.
DR PhylomeDB; P28236; -.
DR TreeFam; TF329606; -.
DR Reactome; R-MMU-190861; Gap junction assembly.
DR BioGRID-ORCS; 14616; 3 hits in 71 CRISPR screens.
DR PRO; PR:P28236; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P28236; protein.
DR Bgee; ENSMUSG00000049908; Expressed in lens of camera-type eye and 5 other tissues.
DR ExpressionAtlas; P28236; baseline and differential.
DR Genevisible; P28236; MM.
DR GO; GO:0005922; C:connexin complex; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005243; F:gap junction channel activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0007267; P:cell-cell signaling; ISO:MGI.
DR GO; GO:1990349; P:gap junction-mediated intercellular transport; ISS:UniProtKB.
DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR GO; GO:1902551; P:regulation of catalase activity; ISO:MGI.
DR GO; GO:1903282; P:regulation of glutathione peroxidase activity; ISO:MGI.
DR GO; GO:0032645; P:regulation of granulocyte macrophage colony-stimulating factor production; ISO:MGI.
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; Direct protein sequencing; 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_0000057831"
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 338..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 371..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"
SQ SEQUENCE 440 AA; 49598 MW; 7FD80B0E15DC4C65 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
SAFKRPVEQP LGEIAEKSLH SIAVSSIQKA KGYQLLEEEK IVSHYFPLTE VGMVETSPLS
AKPFSQFEEK IGTGPLADMS RSYQETLPSY AQVGVQEVER EEPPIEEAVE PEVGEKKQEA
EKVAPEGQET VAVPDRERVE TPGVGKEDEK EELQAEKVTK QGLSAEKAPS LCPELTTDDN
RPLSRLSKAS SRARSDDLTI
