CXB3_MOUSE
ID CXB3_MOUSE Reviewed; 270 AA.
AC P28231;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Gap junction beta-3 protein;
DE AltName: Full=Connexin-31;
DE Short=Cx31;
GN Name=Gjb3; Synonyms=Cxn-31;
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 [MRNA].
RX PubMed=1322300;
RA Hennemann H., Schwarz H.J., Willecke K.;
RT "Characterization of gap junction genes expressed in F9 embryonic carcinoma
RT cells: molecular cloning of mouse connexin31 and -45 cDNAs.";
RL Eur. J. Cell Biol. 57:51-58(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP INTERACTION WITH CNST.
RX PubMed=19864490; DOI=10.1093/hmg/ddp490;
RA del Castillo F.J., Cohen-Salmon M., Charollais A., Caille D., Lampe P.D.,
RA Chavrier P., Meda P., Petit C.;
RT "Consortin, a trans-Golgi network cargo receptor for the plasma membrane
RT targeting and recycling of connexins.";
RL Hum. Mol. Genet. 19:262-275(2010).
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. {ECO:0000269|PubMed:19864490}.
CC -!- INTERACTION:
CC P28231; P23242: Gja1; NbExp=2; IntAct=EBI-1767245, EBI-298630;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X63099; CAA44813.1; -; mRNA.
DR EMBL; AK083716; BAC39002.1; -; mRNA.
DR EMBL; BC024387; AAH24387.1; -; mRNA.
DR CCDS; CCDS18668.1; -.
DR PIR; S23590; S23590.
DR RefSeq; NP_001153484.1; NM_001160012.1.
DR RefSeq; NP_032152.1; NM_008126.2.
DR AlphaFoldDB; P28231; -.
DR SMR; P28231; -.
DR BioGRID; 199933; 3.
DR IntAct; P28231; 2.
DR STRING; 10090.ENSMUSP00000046755; -.
DR iPTMnet; P28231; -.
DR PhosphoSitePlus; P28231; -.
DR MaxQB; P28231; -.
DR PaxDb; P28231; -.
DR PeptideAtlas; P28231; -.
DR PRIDE; P28231; -.
DR ProteomicsDB; 283985; -.
DR Antibodypedia; 31497; 313 antibodies from 30 providers.
DR DNASU; 14620; -.
DR Ensembl; ENSMUST00000046532; ENSMUSP00000046755; ENSMUSG00000042367.
DR Ensembl; ENSMUST00000106091; ENSMUSP00000101697; ENSMUSG00000042367.
DR GeneID; 14620; -.
DR KEGG; mmu:14620; -.
DR UCSC; uc008uus.2; mouse.
DR CTD; 2707; -.
DR MGI; MGI:95721; Gjb3.
DR VEuPathDB; HostDB:ENSMUSG00000042367; -.
DR eggNOG; ENOG502QRC0; Eukaryota.
DR GeneTree; ENSGT01030000234513; -.
DR HOGENOM; CLU_037388_4_1_1; -.
DR InParanoid; P28231; -.
DR OMA; CIVLTVC; -.
DR OrthoDB; 902090at2759; -.
DR PhylomeDB; P28231; -.
DR TreeFam; TF329606; -.
DR Reactome; R-MMU-190861; Gap junction assembly.
DR BioGRID-ORCS; 14620; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Gjb3; mouse.
DR PRO; PR:P28231; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P28231; protein.
DR Bgee; ENSMUSG00000042367; Expressed in ectoplacental cone and 108 other tissues.
DR ExpressionAtlas; P28231; baseline and differential.
DR Genevisible; P28231; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005921; C:gap junction; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005243; F:gap junction channel activity; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0043588; P:skin development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 1.20.1440.80; -; 1.
DR InterPro; IPR000500; Connexin.
DR InterPro; IPR002269; Connexin31.
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:SF65; PTHR11984:SF65; 1.
DR Pfam; PF00029; Connexin; 1.
DR PRINTS; PR00206; CONNEXIN.
DR PRINTS; PR01140; CONNEXINB3.
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; Gap junction; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..270
FT /note="Gap junction beta-3 protein"
FT /id="PRO_0000057863"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 246..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 270 AA; 30902 MW; A91AB784E03E5869 CRC64;
MDWKKLQDLL SGVNQYSTAF GRIWLSVVFV FRVLVYVVAA ERVWGDEQKD FDCNTRQPGC
TNVCYDNFFP ISNIRLWALQ LIFVTCPSML VILHVAYREE RERKHRQKHG EQCAKLYSHP
GKKHGGLWWT YLFSLIFKLI IELVFLYVLH TLWHGFTMPR LVQCASIVPC PNTVDCYIAR
PTEKKVFTYF MVGASAVCII LTICEICYLI FHRIMRGISK GKSTKSISSP KSSSRASTCR
CHHKLLESGD PEADPASEKL QASAPSLTPI
