CXB1_RAT
ID CXB1_RAT Reviewed; 283 AA.
AC P08033;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Gap junction beta-1 protein;
DE AltName: Full=Connexin-32;
DE Short=Cx32;
DE AltName: Full=GAP junction 28 kDa liver protein;
GN Name=Gjb1; Synonyms=Cxn-32;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=3013898; DOI=10.1083/jcb.103.1.123;
RA Paul D.L.;
RT "Molecular cloning of cDNA for rat liver gap junction protein.";
RL J. Cell Biol. 103:123-134(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-119.
RC TISSUE=Liver;
RX PubMed=3017758; DOI=10.1016/0014-5793(86)80865-1;
RA Heynkes R., Kozjek G., Traub O., Willecke K.;
RT "Identification of a rat liver cDNA and mRNA coding for the 28 kDa gap
RT junction protein.";
RL FEBS Lett. 205:56-60(1986).
RN [4]
RP PROTEIN SEQUENCE OF 1-40.
RX PubMed=2987225; DOI=10.1016/s0021-9258(18)88810-x;
RA Nicholson B.J., Gros D.B., Kent S.B.H., Hood L.E., Revel J.-P.;
RT "The Mr 28,000 gap junction proteins from rat heart and liver are different
RT but related.";
RL J. Biol. Chem. 260:6514-6517(1985).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RC STRAIN=Sprague-Dawley;
RX PubMed=2852976; DOI=10.1007/bf01121644;
RA Miller T., Dahl G., Werner R.;
RT "Structure of a gap junction gene: rat connexin-32.";
RL Biosci. Rep. 8:455-464(1988).
RN [6]
RP TOPOLOGY.
RX PubMed=3034905; DOI=10.1016/s0021-9258(18)47632-6;
RA Zimmer D.B., Green C.R., Evans W.H., Gilula N.B.;
RT "Topological analysis of the major protein in isolated intact rat liver gap
RT junctions and gap junction-derived single membrane structures.";
RL J. Biol. Chem. 262:7751-7763(1987).
RN [7]
RP TOPOLOGY.
RX PubMed=1667015; DOI=10.1242/jcs.100.3.567;
RA Rahman S., Evans W.H.;
RT "Topography of connexin32 in rat liver gap junctions. Evidence for an
RT intramolecular disulphide linkage connecting the two extracellular peptide
RT loops.";
RL J. Cell Sci. 100:567-578(1991).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-258 AND SER-266, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; X04070; CAA27705.1; -; mRNA.
DR EMBL; X04303; CAA27846.1; -; mRNA.
DR EMBL; M23565; AAA81569.1; -; Genomic_DNA.
DR EMBL; BC078868; AAH78868.1; -; mRNA.
DR EMBL; AH003192; AAA75195.1; -; Genomic_DNA.
DR PIR; A92745; GJRT.
DR PIR; I52552; I52552.
DR RefSeq; NP_058947.1; NM_017251.2.
DR RefSeq; XP_008771477.1; XM_008773255.2.
DR RefSeq; XP_017457434.1; XM_017601945.1.
DR AlphaFoldDB; P08033; -.
DR SMR; P08033; -.
DR BioGRID; 248217; 1.
DR IntAct; P08033; 2.
DR STRING; 10116.ENSRNOP00000068248; -.
DR TCDB; 1.A.24.1.2; the gap junction-forming connexin (connexin) family.
DR iPTMnet; P08033; -.
DR PhosphoSitePlus; P08033; -.
DR PaxDb; P08033; -.
DR Ensembl; ENSRNOT00000095443; ENSRNOP00000083358; ENSRNOG00000063213.
DR GeneID; 29584; -.
DR KEGG; rno:29584; -.
DR CTD; 2705; -.
DR RGD; 61926; Gjb1.
DR eggNOG; ENOG502R1QN; Eukaryota.
DR GeneTree; ENSGT01030000234513; -.
DR HOGENOM; CLU_037388_4_1_1; -.
DR InParanoid; P08033; -.
DR OMA; HVAYQQH; -.
DR OrthoDB; 1131301at2759; -.
DR PhylomeDB; P08033; -.
DR TreeFam; TF329606; -.
DR Reactome; R-RNO-190704; Oligomerization of connexins into connexons.
DR PRO; PR:P08033; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000003746; Expressed in liver and 17 other tissues.
DR ExpressionAtlas; P08033; baseline and differential.
DR Genevisible; P08033; RN.
DR GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005921; C:gap junction; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005243; F:gap junction channel activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0007154; P:cell communication; TAS:RGD.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:1905867; P:epididymis development; IEP:RGD.
DR GO; GO:0015868; P:purine ribonucleotide transport; IDA:RGD.
DR DisProt; DP01176; -.
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 1: Evidence at protein level;
KW Cell junction; Cell membrane; Direct protein sequencing; Gap junction;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..283
FT /note="Gap junction beta-1 protein"
FT /id="PRO_0000057852"
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..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16396499,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08034"
SQ SEQUENCE 283 AA; 32004 MW; C79FC46AA13BC5D7 CRC64;
MNWTGLYTLL SGVNRHSTAI GRVWLSVIFI FRIMVLVVAA ESVWGDEKSS FICNTLQPGC
NSVCYDHFFP ISHVRLWSLQ LILVSTPALL VAMHVAHQQH IEKKMLRLEG HGDPLHLEEV
KRHKVHISGT LWWTYVISVV FRLLFEAVFM YVFYLLYPGY AMVRLVKCEA FPCPNTVDCF
VSRPTEKTVF TVFMLAASGI CIILNVAEVV YLIIRACARR AQRRSNPPSR KGSGFGHRLS
PEYKQNEINK LLSEQDGSLK DILRRSPGTG AGLAEKSDRC SAC
