CXB4_RAT
ID CXB4_RAT Reviewed; 265 AA.
AC P36380;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Gap junction beta-4 protein;
DE AltName: Full=Connexin-30.3 {ECO:0000303|PubMed:20184948, ECO:0000303|PubMed:7517368};
DE Short=Cx30.3;
GN Name=Gjb4; Synonyms=Cxn-30.3;
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 STRAIN=Sprague-Dawley;
RX PubMed=7517368; DOI=10.1006/excr.1994.1194;
RA Tucker M.A., Barajas L.;
RT "Rat connexins 30.3 and 31 are expressed in the kidney.";
RL Exp. Cell Res. 213:224-230(1994).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=20184948; DOI=10.1016/j.heares.2010.02.008;
RA Wang W.H., Yang J.J., Lin Y.C., Yang J.T., Li S.Y.;
RT "Novel expression patterns of connexin 30.3 in adult rat cochlea.";
RL Hear. Res. 265:77-82(2010).
CC -!- FUNCTION: Structural component of gap junctions (By similarity). Gap
CC junctions are dodecameric channels that connect the cytoplasm of
CC adjoining cells. They are formed by the docking of two hexameric
CC hemichannels, one from each cell membrane (By similarity). Small
CC molecules and ions diffuse from one cell to a neighboring cell via the
CC central pore (By similarity). {ECO:0000250|UniProtKB:P29033,
CC ECO:0000250|UniProtKB:Q02738}.
CC -!- SUBUNIT: A hemichannel or connexon is composed of a hexamer of
CC connexins. A functional gap junction is formed by the apposition of two
CC hemichannels (By similarity). Forms heteromeric channels with GJB2 (By
CC similarity). {ECO:0000250|UniProtKB:P29033,
CC ECO:0000250|UniProtKB:Q02738}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q02738};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q02738}. Cell
CC junction, gap junction {ECO:0000250|UniProtKB:Q02738}. Note=Colocalizes
CC with GJB2 at gap junction plaques in the cochlea.
CC {ECO:0000250|UniProtKB:Q02738}.
CC -!- TISSUE SPECIFICITY: Detected in adult heart, kidney, skin and cochlea,
CC where it is detected in spiral ganglion, stria vascularis, spiral
CC limbus and spiral ligament (at protein level).
CC {ECO:0000269|PubMed:20184948}.
CC -!- SIMILARITY: Belongs to the connexin family. Beta-type (group I)
CC subfamily. {ECO:0000305}.
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DR EMBL; X76168; CAA53762.1; -; mRNA.
DR PIR; I60240; S38891.
DR RefSeq; NP_446436.1; NM_053984.2.
DR AlphaFoldDB; P36380; -.
DR SMR; P36380; -.
DR STRING; 10116.ENSRNOP00000033893; -.
DR PaxDb; P36380; -.
DR GeneID; 117055; -.
DR UCSC; RGD:621829; rat.
DR CTD; 127534; -.
DR RGD; 621829; Gjb4.
DR eggNOG; ENOG502R3YE; Eukaryota.
DR InParanoid; P36380; -.
DR OrthoDB; 955506at2759; -.
DR PhylomeDB; P36380; -.
DR Reactome; R-RNO-190861; Gap junction assembly.
DR PRO; PR:P36380; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005922; C:connexin complex; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005243; F:gap junction channel activity; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; ISS:UniProtKB.
DR GO; GO:1990349; P:gap junction-mediated intercellular transport; ISS:UniProtKB.
DR GO; GO:0042048; P:olfactory behavior; ISO:RGD.
DR GO; GO:0007608; P:sensory perception of smell; ISO:RGD.
DR Gene3D; 1.20.1440.80; -; 1.
DR InterPro; IPR000500; Connexin.
DR InterPro; IPR002270; Connexin-30.3.
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 PANTHER; PTHR11984:SF30; PTHR11984:SF30; 1.
DR Pfam; PF00029; Connexin; 1.
DR PRINTS; PR00206; CONNEXIN.
DR PRINTS; PR01142; CONNEXINB5.
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; Disulfide bond; Gap junction; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..265
FT /note="Gap junction beta-4 protein"
FT /id="PRO_0000057867"
FT INTRAMEM 2..13
FT /evidence="ECO:0000250|UniProtKB:P29033"
FT TOPO_DOM 14..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P29033"
FT TOPO_DOM 41..73
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P29033"
FT TOPO_DOM 95..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P29033"
FT TOPO_DOM 152..184
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P29033"
FT TOPO_DOM 206..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DISULFID 53..175
FT /evidence="ECO:0000250|UniProtKB:P29033"
FT DISULFID 60..169
FT /evidence="ECO:0000250|UniProtKB:P29033"
FT DISULFID 64..164
FT /evidence="ECO:0000250|UniProtKB:P29033"
SQ SEQUENCE 265 AA; 30352 MW; F7DA69C513093147 CRC64;
MNWGFLQGIL SGVNKYSTAL GRIWLSVVFI FRVLVYVVAA EEVWDDEQKD FICNTKQPGC
PNVCYDEFFP VSHVRLWALQ LILVTCPSLL VVMHVAYREE RERKHRLKHG PDAPALYSNL
SKKRGGLWWT YLLSLIFKAA VDSGFLYIFH CIYKDYDMPR VVACSVQPCP HTVDCYISRP
TEKKVFTYFM VVTAAICILL NLSEVAYLVG KRCMEVFRPR RQKTSRRHQL PDTCPPYVIS
KGHPQDESTV LTKAGMATVD AGVYP
