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   24-JAN-2024, entry version 154.
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; 10090-ENSMUSP00000101696; -.
DR   ProteomicsDB; 279217; -.
DR   Antibodypedia; 17219; 193 antibodies from 25 providers.
DR   Ensembl; ENSMUST00000060419.2; ENSMUSP00000053307.2; ENSMUSG00000046623.9.
DR   Ensembl; ENSMUST00000106090.8; ENSMUSP00000101696.2; ENSMUSG00000046623.9.
DR   GeneID; 14621; -.
DR   KEGG; mmu:14621; -.
DR   UCSC; uc008uuu.1; mouse.
DR   AGR; MGI:95722; -.
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; IFHRLYQ; -.
DR   OrthoDB; 5301774at2759; -.
DR   PhylomeDB; Q02738; -.
DR   TreeFam; TF329606; -.
DR   Reactome; R-MMU-190861; Gap junction assembly.
DR   BioGRID-ORCS; 14621; 3 hits in 79 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 63 other cell types or tissues.
DR   ExpressionAtlas; Q02738; baseline and differential.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0005922; C:connexin complex; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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; Gap junction channel protein cysteine-rich domain; 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; CONNEXIN; 1.
DR   PANTHER; PTHR11984:SF30; GAP JUNCTION BETA-4 PROTEIN; 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.
DR   Genevisible; Q02738; MM.
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
//