CXE1_DANRE
ID CXE1_DANRE Reviewed; 207 AA.
AC U3JA75;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Gap junction epsilon-1 protein {ECO:0000250|UniProtKB:Q9CX92};
DE AltName: Full=Connexin-23 {ECO:0000303|PubMed:18068130};
GN Name=cx23 {ECO:0000303|PubMed:18068130,
GN ECO:0000312|ZFIN:ZDB-GENE-050320-121};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2] {ECO:0000312|EMBL:AAH91468.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Singapore {ECO:0000312|EMBL:AAH91468.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH91468.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18068130; DOI=10.1016/j.febslet.2007.11.079;
RA Iovine M.K., Gumpert A.M., Falk M.M., Mendelson T.C.;
RT "Cx23, a connexin with only four extracellular-loop cysteines, forms
RT functional gap junction channels and hemichannels.";
RL FEBS Lett. 582:165-170(2008).
CC -!- FUNCTION: Has significant hemichannel activity. However, has only low-
CC efficiency gap junction activity and probably does not function as a
CC gap junction channel in vivo. {ECO:0000269|PubMed:18068130}.
CC -!- SUBUNIT: A connexon is composed of a hexamer of connexins.
CC {ECO:0000250|UniProtKB:P08050}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18068130};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed in lens at 24 hours post-fertilization.
CC {ECO:0000269|PubMed:18068130}.
CC -!- SIMILARITY: Belongs to the connexin family. Beta-type (group I)
CC subfamily. {ECO:0000305}.
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DR EMBL; BX855623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC091468; AAH91468.1; -; mRNA.
DR RefSeq; NP_001013564.1; NM_001013546.1.
DR AlphaFoldDB; U3JA75; -.
DR SMR; U3JA75; -.
DR STRING; 7955.ENSDARP00000127140; -.
DR PaxDb; U3JA75; -.
DR Ensembl; ENSDART00000153137; ENSDARP00000127140; ENSDARG00000054150.
DR GeneID; 541419; -.
DR KEGG; dre:541419; -.
DR CTD; 541419; -.
DR ZFIN; ZDB-GENE-050320-121; gje1a.
DR eggNOG; ENOG502RVMN; Eukaryota.
DR GeneTree; ENSGT01050000244962; -.
DR HOGENOM; CLU_115891_0_0_1; -.
DR OMA; IRMFFLG; -.
DR OrthoDB; 1100904at2759; -.
DR PhylomeDB; U3JA75; -.
DR PRO; PR:U3JA75; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000054150; Expressed in larva and 8 other tissues.
DR ExpressionAtlas; U3JA75; baseline.
DR GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005243; F:gap junction channel activity; IDA:ZFIN.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR Gene3D; 1.20.1440.80; -; 1.
DR InterPro; IPR000500; Connexin.
DR InterPro; IPR019570; Connexin_CCC.
DR InterPro; IPR013092; Connexin_N.
DR InterPro; IPR038359; Connexin_N_sf.
DR PANTHER; PTHR11984; PTHR11984; 1.
DR Pfam; PF00029; Connexin; 2.
DR PRINTS; PR00206; CONNEXIN.
DR SMART; SM01089; Connexin_CCC; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..207
FT /note="Gap junction epsilon-1 protein"
FT /id="PRO_0000442535"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..74
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..175
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT DISULFID 53..161
FT /evidence="ECO:0000250|UniProtKB:P29033"
FT DISULFID 64..147
FT /evidence="ECO:0000250|UniProtKB:P29033"
SQ SEQUENCE 207 AA; 23916 MW; B6651374C77A0C6A CRC64;
MSLNYIKNFY EGCLRPPTVI GQFHTLFFGS VRTFFLGVLG FAVYGNEALH FSCDPDKREL
NLYCYNQFRP ITPQVFWALQ LVTVLVPGAV FHLYAACKNI DQEEILHRPM STVFYIISVL
LRIILEVLAF WLQSHLFGFL VDPIFMCDVT GLGKILNVSK CMVPEHFEKT IFLSAMYTFT
IITILLCIAE IFEILFRRLG YLNQPMT
