ID   CXG1_DANRE              Reviewed;         380 AA.
AC   Q92052; Q92053;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Gap junction gamma-1 protein;
DE   AltName: Full=Connexin-43.4;
DE            Short=Cx43.4;
DE   AltName: Full=Gap junction alpha-7 protein;
GN   Name=gjc1; Synonyms=cx43.4, gja7;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RA   Marics I.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=8806823; DOI=10.1006/dbio.1996.0177;
RA   Essner J.J., Laing J.G., Beyer E.C., Johnson R.G., Hackett P.B. Jr.;
RT   "Expression of zebrafish connexin43.4 in the notochord and tail bud of
RT   wild-type and mutant no tail embryos.";
RL   Dev. Biol. 177:449-462(1996).
CC   -!- FUNCTION: One gap junction consists of a cluster of closely packed
CC       pairs of transmembrane channels, the connexons, through which materials
CC       of low MW diffuse from one cell to a neighboring cell. Participates in
CC       a developmental pathway for formation of the notochord and tail.
CC   -!- SUBUNIT: A connexon is composed of a hexamer of connexins.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC       junction, gap junction.
CC   -!- SIMILARITY: Belongs to the connexin family. Gamma-type subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X96712; CAA65473.1; -; mRNA.
DR   EMBL; L46801; AAB36619.1; -; mRNA.
DR   AlphaFoldDB; Q92052; -.
DR   SMR; Q92052; -.
DR   STRING; 7955.ENSDARP00000015225; -.
DR   PaxDb; Q92052; -.
DR   ZFIN; ZDB-GENE-990415-38; gjc4b.
DR   eggNOG; ENOG502QVY2; Eukaryota.
DR   InParanoid; Q92052; -.
DR   PhylomeDB; Q92052; -.
DR   PRO; PR:Q92052; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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; IBA:GO_Central.
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; IPR017990; Connexin_CS.
DR   InterPro; IPR013092; Connexin_N.
DR   InterPro; IPR038359; Connexin_N_sf.
DR   PANTHER; PTHR11984; PTHR11984; 1.
DR   Pfam; PF00029; Connexin; 1.
DR   PRINTS; PR00206; CONNEXIN.
DR   SMART; SM00037; CNX; 1.
DR   SMART; SM01089; Connexin_CCC; 1.
DR   PROSITE; PS00407; CONNEXINS_1; 1.
DR   PROSITE; PS00408; CONNEXINS_2; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Gap junction; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..380
FT                   /note="Gap junction gamma-1 protein"
FT                   /id="PRO_0000057829"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        23..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..75
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        96..171
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..228
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..380
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          337..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        122
FT                   /note="R -> A (in Ref. 2; AAB36619)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="R -> P (in Ref. 2; AAB36619)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   380 AA;  43578 MW;  7560894FC06C6C90 CRC64;
     MSWSFLTRLL DEISNHSTFV GKIWLTLFII FRIVLTVVGG ESIYYDEQSK FVCNTQQPGC
     ENVCYDAFAP LSHVRFWVFQ IILITTPTIM YLGFAMHKIA RSNDVEYRPV NRKRMPMINR
     GRNRDYEEAE DNGEEDPMIM EEIVPEKEKA PEKSAVKHDG RRRIKRDGLM KVYILQLLSR
     IIFEVGFLFG QYILYGFEVA PSYVCTRSPC PHTVDCFVSR PTEKTIFLLI MYAVSCLCLS
     LTVLEILHLG LSGIRDAFRR RARHQSVQRP RAPICRQVPT APPGYHTALK KDKLSLGMKP
     EYNLDSGRES FGDESSSRDI DRLRRHLKLA QQHLDLAYQN GESSPSRSSS PESNGTAVEQ
     NRLNFAQEKQ GSKCEKGIHA