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CXD4_MOUSE
ID   CXD4_MOUSE              Reviewed;         364 AA.
AC   Q8BSD4; B2RQL7; Q8C6W6; Q91YD0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Gap junction delta-4 protein;
DE   AltName: Full=Connexin-39;
DE            Short=Cx39;
GN   Name=Gjd4;
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].
RC   STRAIN=129/Sv;
RX   PubMed=12108537; DOI=10.1515/bc.2002.076;
RA   Willecke K., Eiberger J., Degen J., Eckardt D., Romualdi A., Guldenagel M.,
RA   Deutsch U., Soehl G.;
RT   "Structural and functional diversity of connexin genes in the mouse and
RT   human genome.";
RL   Biol. Chem. 383:725-737(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
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   TISSUE=Brain;
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).
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. {ECO:0000250}.
CC   -!- SUBUNIT: A connexon is composed of a hexamer of connexins.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the connexin family. Delta-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ414562; CAC93844.1; -; mRNA.
DR   EMBL; AK034663; BAC28788.1; -; mRNA.
DR   EMBL; AK053016; BAC35240.1; -; mRNA.
DR   EMBL; BC137984; AAI37985.1; -; mRNA.
DR   CCDS; CCDS29049.1; -.
DR   RefSeq; NP_694726.2; NM_153086.5.
DR   AlphaFoldDB; Q8BSD4; -.
DR   SMR; Q8BSD4; -.
DR   STRING; 10090.ENSMUSP00000035472; -.
DR   PhosphoSitePlus; Q8BSD4; -.
DR   PaxDb; Q8BSD4; -.
DR   PRIDE; Q8BSD4; -.
DR   Antibodypedia; 26696; 48 antibodies from 13 providers.
DR   DNASU; 225152; -.
DR   Ensembl; ENSMUST00000041007; ENSMUSP00000035472; ENSMUSG00000036855.
DR   GeneID; 225152; -.
DR   KEGG; mmu:225152; -.
DR   UCSC; uc008eah.1; mouse.
DR   CTD; 219770; -.
DR   MGI; MGI:2444990; Gjd4.
DR   VEuPathDB; HostDB:ENSMUSG00000036855; -.
DR   eggNOG; ENOG502QWIV; Eukaryota.
DR   GeneTree; ENSGT01050000244962; -.
DR   HOGENOM; CLU_037388_3_0_1; -.
DR   InParanoid; Q8BSD4; -.
DR   OMA; LRTTQWV; -.
DR   OrthoDB; 721800at2759; -.
DR   PhylomeDB; Q8BSD4; -.
DR   TreeFam; TF329606; -.
DR   Reactome; R-MMU-190861; Gap junction assembly.
DR   BioGRID-ORCS; 225152; 1 hit in 72 CRISPR screens.
DR   PRO; PR:Q8BSD4; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q8BSD4; protein.
DR   Bgee; ENSMUSG00000036855; Expressed in lower leg mesenchyme and 19 other tissues.
DR   Genevisible; Q8BSD4; MM.
DR   GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA: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:0014717; P:regulation of satellite cell activation involved in skeletal muscle regeneration; IMP:MGI.
DR   Gene3D; 1.20.1440.80; -; 1.
DR   InterPro; IPR000500; Connexin.
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; 2.
DR   Pfam; PF00029; Connexin; 2.
DR   PRINTS; PR00206; CONNEXIN.
DR   SMART; SM00037; CNX; 1.
DR   SMART; SM01089; Connexin_CCC; 1.
DR   PROSITE; PS00407; CONNEXINS_1; 1.
DR   PROSITE; PS00408; CONNEXINS_2; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Gap junction; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..364
FT                   /note="Gap junction delta-4 protein"
FT                   /id="PRO_0000313011"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..76
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..128
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..173
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..364
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          331..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        198
FT                   /note="L -> P (in Ref. 2; BAC35240)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="A -> T (in Ref. 2; BAC35240)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        345
FT                   /note="C -> G (in Ref. 1; CAC93844)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  40042 MW;  FA58BCCFB1E6B758 CRC64;
     MEKLNLLGFL IITLNCNVTI MGMIWLIVEV LLRMLVVVLA GSPIYEDEQE RFICNTLQPG
     CANVCYDLFS PVSPLRFWLV QSLALLLPSV VFGTYTLHRG AKLAAVGGAC RPQVPDLSTA
     YLVHLLLRML LEAGLAFLHY FLFGFSVPAR VSCSHVPCSG AVDCYVSRPT EKSLLILFFW
     AVSALSFLLS LADLLWILPR RKTLRTTQWV NGEARPVCEV PAPPPCLLQN PQGYLSQGQV
     DQEDRQEEQV VPEFPCMWTA GQSDNSNVGQ ACVSGLLEHS DQDASEATSS AGDRLTVAHT
     AHELRFHRET SLDLGGKNTQ ADELSLATQS HLARHSSASK PQAPCRLTTS GSAPHLRTKK
     SEWV
 
 
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