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   24-JAN-2024, entry version 158.
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; 10090-ENSMUSP00000104421; -.
DR   ProteomicsDB; 279226; -.
DR   Antibodypedia; 34662; 228 antibodies from 28 providers.
DR   DNASU; 118454; -.
DR   Ensembl; ENSMUST00000108790.2; ENSMUSP00000104418.2; ENSMUSG00000043448.14.
DR   Ensembl; ENSMUST00000108793.9; ENSMUSP00000104421.3; ENSMUSG00000043448.14.
DR   GeneID; 118454; -.
DR   KEGG; mmu:118454; -.
DR   UCSC; uc007jde.2; mouse.
DR   AGR; MGI:2153060; -.
DR   CTD; 57165; -.
DR   MGI; MGI:2153060; Gjc2.
DR   VEuPathDB; HostDB:ENSMUSG00000043448; -.
DR   eggNOG; ENOG502QV2G; Eukaryota.
DR   GeneTree; ENSGT01090000260005; -.
DR   HOGENOM; CLU_037388_4_0_1; -.
DR   InParanoid; Q8BQU6; -.
DR   OMA; ACTKGAG; -.
DR   OrthoDB; 4214922at2759; -.
DR   PhylomeDB; Q8BQU6; -.
DR   TreeFam; TF329606; -.
DR   Reactome; R-MMU-190861; Gap junction assembly.
DR   BioGRID-ORCS; 118454; 3 hits in 76 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 140 other cell types or tissues.
DR   GO; GO:0005922; C:connexin complex; IBA:GO_Central.
DR   GO; GO:0005921; C:gap junction; IDA:MGI.
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: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; Gap junction channel protein cysteine-rich domain; 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; CONNEXIN; 1.
DR   PANTHER; PTHR11984:SF52; GAP JUNCTION GAMMA-2 PROTEIN; 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.
DR   Genevisible; Q8BQU6; MM.
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
//