CXG2_MOUSE
ID CXG2_MOUSE Reviewed; 440 AA.
AC Q8BQU6; Q6TLV2; Q8BQS2; Q9EPM1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Gap junction gamma-2 protein;
DE AltName: Full=Connexin-47;
DE Short=Cx47;
DE AltName: Full=Gap junction alpha-12 protein;
GN Name=Gjc2; Synonyms=Gja12;
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 FUNCTION.
RC STRAIN=129/SvJ;
RX PubMed=11160382; DOI=10.1523/jneurosci.21-04-01117.2001;
RA Teubner B., Odermatt B., Gueldenagel M., Soehl G., Degen J.,
RA Bukauskas F.F., Kronengold J., Verselis V.K., Jung Y.T., Kozak C.A.,
RA Schilling K., Willecke K.;
RT "Functional expression of the new gap junction gene connexin47 transcribed
RT in mouse brain and spinal cord neurons.";
RL J. Neurosci. 21:1117-1126(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Corpora quadrigemina;
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 [MRNA] OF 1-79.
RC STRAIN=Swiss Webster;
RX PubMed=15676282; DOI=10.1016/j.ygeno.2004.11.007;
RA Anderson C.L., Zundel M.A., Werner R.;
RT "Variable promoter usage and alternative splicing in five mouse connexin
RT genes.";
RL Genomics 85:238-244(2005).
RN [4]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=12805295; DOI=10.1523/jneurosci.23-11-04549.2003;
RA Odermatt B., Wellershaus K., Wallraff A., Seifert G., Degen J., Euwens C.,
RA Fuss B., Buessow H., Schilling K., Steinhaeuser C., Willecke K.;
RT "Connexin 47 (Cx47)-deficient mice with enhanced green fluorescent protein
RT reporter gene reveal predominant oligodendrocytic expression of Cx47 and
RT display vacuolized myelin in the CNS.";
RL J. Neurosci. 23:4549-4559(2003).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=12843301; DOI=10.1523/jneurosci.23-13-05963.2003;
RA Menichella D.M., Goodenough D.A., Sirkowski E., Scherer S.S., Paul D.L.;
RT "Connexins are critical for normal myelination in the CNS.";
RL J. Neurosci. 23:5963-5973(2003).
RN [6]
RP INTERACTION WITH TJP1, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15183511; DOI=10.1016/j.neuroscience.2004.03.063;
RA Li X., Ionescu A.V., Lynn B.D., Lu S., Kamasawa N., Morita M.,
RA Davidson K.G.V., Yasumura T., Rash J.E., Nagy J.I.;
RT "Connexin47, connexin29 and connexin32 co-expression in oligodendrocytes
RT and Cx47 association with zonula occludens-1 (ZO-1) in mouse brain.";
RL Neuroscience 126:611-630(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(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. May play a role
CC in myelination in central and peripheral nervous systems.
CC {ECO:0000269|PubMed:11160382, ECO:0000269|PubMed:12843301}.
CC -!- SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts
CC with TJP1. {ECO:0000269|PubMed:15183511}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15183511};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15183511}. Cell
CC junction, gap junction {ECO:0000269|PubMed:15183511}.
CC -!- TISSUE SPECIFICITY: Mainly expressed by oligodendrocytes in the central
CC nervous system (at protein level). {ECO:0000269|PubMed:12805295,
CC ECO:0000269|PubMed:12843301, ECO:0000269|PubMed:15183511}.
CC -!- DEVELOPMENTAL STAGE: Expression starts after birth in the central
CC nervous system and parallels myelination process.
CC {ECO:0000269|PubMed:12843301}.
CC -!- DISRUPTION PHENOTYPE: Mice display myelination abnormalities
CC characterized by extracellular vacuolation along nerve fibers. Mice
CC lacking both Gja12 and Gjb1 display a more severe demyelination
CC phenotype associated with oligodendrocyte death. These mice develop
CC action tremors, tonic seizures, sporadic convulsions and loss of
CC consciousness preceding death in the sixth week after birth.
CC {ECO:0000269|PubMed:12805295, ECO:0000269|PubMed:12843301}.
CC -!- SIMILARITY: Belongs to the connexin family. Gamma-type subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32806.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC19434.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ276435; CAC19434.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK046421; BAC32722.1; -; mRNA.
DR EMBL; AK046609; BAC32806.1; ALT_INIT; mRNA.
DR EMBL; AY394498; AAR05823.1; -; mRNA.
DR EMBL; AY394499; AAR05824.1; -; mRNA.
DR EMBL; AY394500; AAR05825.1; -; mRNA.
DR CCDS; CCDS24760.1; -.
DR RefSeq; NP_536702.3; NM_080454.4.
DR RefSeq; NP_780661.2; NM_175452.4.
DR AlphaFoldDB; Q8BQU6; -.
DR SMR; Q8BQU6; -.
DR IntAct; Q8BQU6; 1.
DR MINT; Q8BQU6; -.
DR STRING; 10090.ENSMUSP00000104421; -.
DR TCDB; 1.A.24.2.1; the gap junction-forming connexin (connexin) family.
DR iPTMnet; Q8BQU6; -.
DR PhosphoSitePlus; Q8BQU6; -.
DR PaxDb; Q8BQU6; -.
DR PRIDE; Q8BQU6; -.
DR ProteomicsDB; 279226; -.
DR Antibodypedia; 34662; 194 antibodies from 28 providers.
DR DNASU; 118454; -.
DR Ensembl; ENSMUST00000108790; ENSMUSP00000104418; ENSMUSG00000043448.
DR Ensembl; ENSMUST00000108793; ENSMUSP00000104421; ENSMUSG00000043448.
DR GeneID; 118454; -.
DR KEGG; mmu:118454; -.
DR UCSC; uc007jde.2; mouse.
DR CTD; 57165; -.
DR MGI; MGI:2153060; Gjc2.
DR VEuPathDB; HostDB:ENSMUSG00000043448; -.
DR eggNOG; ENOG502QV2G; Eukaryota.
DR GeneTree; ENSGT01050000244833; -.
DR HOGENOM; CLU_037388_4_0_1; -.
DR InParanoid; Q8BQU6; -.
DR OMA; EMCHLGI; -.
DR OrthoDB; 959629at2759; -.
DR PhylomeDB; Q8BQU6; -.
DR TreeFam; TF329606; -.
DR Reactome; R-MMU-190861; Gap junction assembly.
DR BioGRID-ORCS; 118454; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q8BQU6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BQU6; protein.
DR Bgee; ENSMUSG00000043448; Expressed in lumbar subsegment of spinal cord and 138 other tissues.
DR Genevisible; Q8BQU6; MM.
DR GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR GO; GO:0005921; C:gap junction; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0033270; C:paranode region of axon; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:1990769; C:proximal neuron projection; ISO:MGI.
DR GO; GO:0005243; F:gap junction channel activity; IDA:MGI.
DR GO; GO:1903763; F:gap junction channel activity involved in cell communication by electrical coupling; ISO:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0010644; P:cell communication by electrical coupling; ISO:MGI.
DR GO; GO:0007267; P:cell-cell signaling; IDA:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:1904427; P:positive regulation of calcium ion transmembrane transport; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; ISO:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0009636; P:response to toxic substance; IDA: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; 1.
DR Pfam; PF00029; Connexin; 1.
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 1: Evidence at protein level;
KW Cell junction; Cell membrane; Gap junction; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..440
FT /note="Gap junction gamma-2 protein"
FT /id="PRO_0000057843"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..78
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 108..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 216
FT /note="L -> V (in Ref. 2; BAC32722)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="V -> A (in Ref. 1; CAC19434)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="S -> G (in Ref. 1; CAC19434)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 47008 MW; 2D11040FE28ADB1E CRC64;
MTNMSWSFLT RLLEEIHNHS TFVGKVWLTV LVVFRIVLTA VGGESIYSDE QSKFTCNTRQ
PGCDNVCYDA FAPLSHVRFW VFQIVVISTP SVMYLGYAVH RLARASEQER RRALRRRPGT
RRLPRAQLPP PPPGWPDTTD LGEAEPILAL EEDEDEEPGA PEGPGEDTEE ERAEDVAAKG
GGGDGKTVVT PGPAGQHDGR RRIQREGLMR VYVAQLVVRA AFEVAFLVGQ YLLYGFEVPP
FFACSRQPCP HVVDCFVSRP TEKTVFLLVM YVVSCLCLLL NLCEMAHLGL GSAQDAVRGR
RGASAAGPGP TPRPPPCAFP AAAAGLACPP DYSLVVRAAE RARAHDQNLA NLALQALRDG
AAVAAVSADR DSPPCAGLNA TSRGAPRVGG LASGTGSATS GGTVGEQSRP GAQEQLATKP
RAGSEKGSTG SRDGKATVWI
