ID   CXB1_BOVIN              Reviewed;         284 AA.
AC   O18968;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Gap junction beta-1 protein;
DE   AltName: Full=Connexin-32;
DE            Short=Cx32;
GN   Name=GJB1; Synonyms=CXN-32;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8678997; DOI=10.1007/s003359900192;
RA   Castiglioni B., Ferretti L., Tenchini M.L., Mezzelani A., Simonic T.,
RA   Duga S.;
RT   "Physical mapping of connexin 32 (GJB1) and 43 (GJA1) genes to bovine
RT   chromosomes Xq22 and 9q15/16 by fluorescence in situ hybridization.";
RL   Mamm. Genome 7:634-635(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.
CC   -!- SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts
CC       with CNST (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC       junction, gap junction.
CC   -!- SIMILARITY: Belongs to the connexin family. Beta-type (group I)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X95311; CAA64623.1; -; mRNA.
DR   RefSeq; NP_776494.1; NM_174069.2.
DR   AlphaFoldDB; O18968; -.
DR   SMR; O18968; -.
DR   STRING; 9913.ENSBTAP00000027331; -.
DR   PaxDb; O18968; -.
DR   Ensembl; ENSBTAT00000027331; ENSBTAP00000027331; ENSBTAG00000020512.
DR   GeneID; 281194; -.
DR   KEGG; bta:281194; -.
DR   CTD; 2705; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020512; -.
DR   VGNC; VGNC:29376; GJB1.
DR   eggNOG; ENOG502R1QN; Eukaryota.
DR   GeneTree; ENSGT01030000234513; -.
DR   HOGENOM; CLU_037388_4_1_1; -.
DR   InParanoid; O18968; -.
DR   OMA; HVAYQQH; -.
DR   OrthoDB; 1131301at2759; -.
DR   TreeFam; TF329606; -.
DR   Reactome; R-BTA-190704; Oligomerization of connexins into connexons.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000020512; Expressed in corpus epididymis and 71 other tissues.
DR   ExpressionAtlas; O18968; baseline and differential.
DR   GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR   GO; GO:0005243; F:gap junction channel activity; ISS:AgBase.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR   GO; GO:0015868; P:purine ribonucleotide transport; ISS:AgBase.
DR   Gene3D; 1.20.1440.80; -; 1.
DR   InterPro; IPR000500; Connexin.
DR   InterPro; IPR002267; Connexin32.
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; PR01138; CONNEXINB1.
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; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..284
FT                   /note="Gap junction beta-1 protein"
FT                   /id="PRO_0000057847"
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..130
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        154..191
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        215..284
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08033"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08034"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08034"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08034"
SQ   SEQUENCE   284 AA;  32083 MW;  192A553978DB6BFF CRC64;
     MNWTGLYTLL SGVNRHSTAI GRVWLSVIFI FRIMVLVVAA ESVWGDEKSS FICNTLQPGC
     NSVCYDHFFP ISHVRLWSLQ LILVSTPALL VAMHVAHQQH IEKKMLRLEG HGDPLHLEEV
     KRHKVHISGT LWWTYVISVV FRLLFEAAFM YVFYLLYPGY AMVRLVKCDA YPCPNTVDCF
     VSRPTEKTIF TVFMLAASGI CIILNVAEVV YLIFRACARR AQRRSNPPSR KGSGGFGHRL
     SPEYKQNEIN KLLSEQDGSL KDILRRSPGT GAGLAEKSDR CSAC