ID   CXG1_MESAU              Reviewed;         396 AA.
AC   Q6PYT3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Gap junction gamma-1 protein;
DE   AltName: Full=Connexin-45;
DE            Short=Cx45;
DE   AltName: Full=Gap junction alpha-7 protein;
GN   Name=GJC1; Synonyms=GJA7;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16194882; DOI=10.1080/15419060500242877;
RA   Cruciani V., Heintz K.-M., Husoey T., Hovig E., Warren D.J.,
RA   Mikalsen S.-O.;
RT   "The detection of hamster connexins: a comparison of expression profiles
RT   with wild-type mouse and the cancer-prone min mouse.";
RL   Cell Commun. Adhes. 11:155-171(2004).
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. {ECO:0000250}.
CC   -!- SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts
CC       with CNST (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the connexin family. Gamma-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY570790; AAS83436.1; -; mRNA.
DR   RefSeq; NP_001268477.1; NM_001281548.1.
DR   AlphaFoldDB; Q6PYT3; -.
DR   BMRB; Q6PYT3; -.
DR   SMR; Q6PYT3; -.
DR   STRING; 10036.XP_005070173.1; -.
DR   GeneID; 101844542; -.
DR   CTD; 10052; -.
DR   eggNOG; ENOG502QV2G; Eukaryota.
DR   OrthoDB; 692491at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005922; C:connexin complex; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0086077; F:gap junction channel activity involved in AV node cell-bundle of His cell electrical coupling; IEA:Ensembl.
DR   GO; GO:0005216; F:ion channel activity; IEA:Ensembl.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
DR   GO; GO:0048468; P:cell development; IEA:Ensembl.
DR   GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0016264; P:gap junction assembly; IEA:Ensembl.
DR   GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR   GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR   Gene3D; 1.20.1440.80; -; 1.
DR   InterPro; IPR000500; Connexin.
DR   InterPro; IPR002265; Connexin45.
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   PRINTS; PR01136; CONNEXINA6.
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; Coiled coil; Gap junction; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..396
FT                   /note="Gap junction gamma-1 protein"
FT                   /id="PRO_0000369542"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..75
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..175
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        199..229
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..396
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          145..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          303..358
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        375..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  45666 MW;  9CD5721BB071B65C CRC64;
     MSWSFLTRLL EEIHNHSTFV GKIWLTVLIV FRIVLTAVGG ESIYYDEQSK FVCNTEQPGC
     ENVCYDAFAP LSHVRFWVFQ IILVATPSVM YLGYAIHKIA KMEHGEADKK AARSKPYAMR
     WKQHRALEET EEDHEEDPMM YPEMELESEK ENKEQSQPKP KHDGRRRIRE DGLMKIYVLQ
     LLARTVFEVG FLIGQYFLYG FQVHPFYVCS RLPCPHKIDC FISRPTEKTI FLLIMYGVTG
     LCLLLNIWEM LHLGFGTIRD SLNSKRRELD DPGAYNYPFT WNTPSAPPGY NIAVKPDQIQ
     YTELSNAKIA YKQNKANIAQ EQQYGSHEEH LPADLETLQR EIRMAQERLD LAIQAYHHQN
     NPHGPREKKA KVGSKSGSNK SSISSKSGDG KTSVWI