CXB4_MOUSE
ID CXB4_MOUSE Reviewed; 266 AA.
AC Q02738;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Gap junction beta-4 protein;
DE AltName: Full=Connexin-30.3 {ECO:0000303|PubMed:1512260};
DE Short=Cx30.3;
GN Name=Gjb4; Synonyms=Cxn-30.3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Skin;
RX PubMed=1512260; DOI=10.1016/s0021-9258(18)41916-3;
RA Hennemann H., Dahl E., White J.B., Schwarz H.J., Lalley P.A., Chang S.,
RA Nicholson B.J., Willecke K.;
RT "Two gap junction genes, connexin 31.1 and 30.3, are closely linked on
RT mouse chromosome 4 and preferentially expressed in skin.";
RL J. Biol. Chem. 267:17225-17233(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=15692151; DOI=10.1152/ajpcell.00341.2004;
RA Sun J., Ahmad S., Chen S., Tang W., Zhang Y., Chen P., Lin X.;
RT "Cochlear gap junctions coassembled from Cx26 and 30 show faster
RT intercellular Ca2+ signaling than homomeric counterparts.";
RL Am. J. Physiol. 288:C613-C623(2005).
CC -!- FUNCTION: Structural component of gap junctions (PubMed:15692151). 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 (PubMed:15692151). {ECO:0000250|UniProtKB:P29033,
CC ECO:0000269|PubMed:15692151}.
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
CC (PubMed:15692151). {ECO:0000250|UniProtKB:P29033,
CC ECO:0000269|PubMed:15692151}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15692151};
CC Multi-pass membrane protein {ECO:0000305}. Cell junction, gap junction
CC {ECO:0000269|PubMed:15692151}. Note=Colocalizes with GJB2 at gap
CC junction plaques in the cochlea. {ECO:0000269|PubMed:15692151}.
CC -!- TISSUE SPECIFICITY: Detected in cochlea (at protein level)
CC (PubMed:15692151). Detected in cochlea (PubMed:15692151). Expressed in
CC skin (PubMed:1512260). {ECO:0000269|PubMed:1512260,
CC ECO:0000269|PubMed:15692151}.
CC -!- DEVELOPMENTAL STAGE: Detected in cochlea after 15 dpc. Detected in the
CC spiral limbus in neoneates at 2, 8 and 10 days after birth, before the
CC onset of hearing. {ECO:0000269|PubMed:15692151}.
CC -!- SIMILARITY: Belongs to the connexin family. Beta-type (group I)
CC subfamily. {ECO:0000305}.
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DR EMBL; M91443; AAA37428.1; -; Genomic_DNA.
DR EMBL; BC064060; AAH64060.1; -; mRNA.
DR CCDS; CCDS18669.1; -.
DR PIR; A43433; A43433.
DR RefSeq; NP_032153.1; NM_008127.4.
DR AlphaFoldDB; Q02738; -.
DR SMR; Q02738; -.
DR STRING; 10090.ENSMUSP00000101696; -.
DR PhosphoSitePlus; Q02738; -.
DR MaxQB; Q02738; -.
DR PaxDb; Q02738; -.
DR PRIDE; Q02738; -.
DR ProteomicsDB; 279217; -.
DR Antibodypedia; 17219; 177 antibodies from 25 providers.
DR Ensembl; ENSMUST00000060419; ENSMUSP00000053307; ENSMUSG00000046623.
DR Ensembl; ENSMUST00000106090; ENSMUSP00000101696; ENSMUSG00000046623.
DR GeneID; 14621; -.
DR KEGG; mmu:14621; -.
DR UCSC; uc008uuu.1; mouse.
DR CTD; 127534; -.
DR MGI; MGI:95722; Gjb4.
DR VEuPathDB; HostDB:ENSMUSG00000046623; -.
DR eggNOG; ENOG502R3YE; Eukaryota.
DR GeneTree; ENSGT01030000234513; -.
DR HOGENOM; CLU_037388_4_1_1; -.
DR InParanoid; Q02738; -.
DR OMA; QDYDMPR; -.
DR OrthoDB; 955506at2759; -.
DR PhylomeDB; Q02738; -.
DR TreeFam; TF329606; -.
DR Reactome; R-MMU-190861; Gap junction assembly.
DR BioGRID-ORCS; 14621; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Gjb4; mouse.
DR PRO; PR:Q02738; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q02738; protein.
DR Bgee; ENSMUSG00000046623; Expressed in lip and 60 other tissues.
DR ExpressionAtlas; Q02738; baseline and differential.
DR Genevisible; Q02738; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005922; C:connexin complex; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005243; F:gap junction channel activity; IDA:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; IDA:UniProtKB.
DR GO; GO:1990349; P:gap junction-mediated intercellular transport; IDA:UniProtKB.
DR GO; GO:0042048; P:olfactory behavior; IMP:MGI.
DR GO; GO:0007608; P:sensory perception of smell; IMP:MGI.
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..266
FT /note="Gap junction beta-4 protein"
FT /id="PRO_0000057866"
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..266
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 266 AA; 30389 MW; 0772D708C004EFC1 CRC64;
MNWGFLQGIL SGVNKYSTAL GRIWLSVVFI FRVLVYVVAA EEVWDDDQKD FICNTKQPGC
PNVCYDEFFP VSHVRLWALQ LILVTCPSLL VVMHVAYREE RERKHRLKHG PNAPALYSNL
SKKRGGLWWT YLLSLIFKAA VDSGFLYIFH CIYKDYDMPR VVACSVTPCP HTVDCYIARP
TEKKVFTYFM VVTAAICILL NLSEVVYLVG KRCMEVFRPR RRKASRRHQL PDTCPPYVIS
KGGHPQDESV ILTKAGMATV DAGVYP
