CXG2_RAT
ID CXG2_RAT Reviewed; 440 AA.
AC Q80XF7;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 129.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-434.
RX PubMed=16194882; DOI=10.1080/15419060500242877;
RA Cruciani V., Heintz K.-M., Husoey T., Hovig E., Warren D.J.,
RA Mikalsen S.-O.;
RT "The detection of hamster connexins: a comparison of expression profiles
RT with wild-type mouse and the cancer-prone min mouse.";
RL Cell Commun. Adhes. 11:155-171(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=15293232; DOI=10.1002/glia.20043;
RA Kleopa K.A., Orthmann J.L., Enriquez A., Paul D.L., Scherer S.S.;
RT "Unique distributions of the gap junction proteins connexin29, connexin32,
RT and connexin47 in oligodendrocytes.";
RL Glia 47:346-357(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. May play a role
CC in myelination in central and peripheral nervous systems (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts
CC with TJP1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC junction, gap junction.
CC -!- TISSUE SPECIFICITY: Mainly expressed by oligodendrocytes in the central
CC nervous system. Expressed in optic nerve (at protein level).
CC {ECO:0000269|PubMed:15293232}.
CC -!- SIMILARITY: Belongs to the connexin family. Gamma-type subfamily.
CC {ECO:0000305}.
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DR EMBL; AABR03074951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY233216; AAP04733.1; -; Genomic_DNA.
DR RefSeq; NP_001094254.1; NM_001100784.1.
DR RefSeq; XP_006246577.1; XM_006246515.3.
DR RefSeq; XP_017452934.1; XM_017597445.1.
DR RefSeq; XP_017452935.1; XM_017597446.1.
DR RefSeq; XP_017452936.1; XM_017597447.1.
DR AlphaFoldDB; Q80XF7; -.
DR SMR; Q80XF7; -.
DR BioGRID; 269223; 1.
DR STRING; 10116.ENSRNOP00000064383; -.
DR iPTMnet; Q80XF7; -.
DR PhosphoSitePlus; Q80XF7; -.
DR PaxDb; Q80XF7; -.
DR PRIDE; Q80XF7; -.
DR Ensembl; ENSRNOT00000058362; ENSRNOP00000064383; ENSRNOG00000038328.
DR GeneID; 497913; -.
DR KEGG; rno:497913; -.
DR UCSC; RGD:1562712; rat.
DR CTD; 57165; -.
DR RGD; 1562712; Gjc2.
DR eggNOG; ENOG502QV2G; Eukaryota.
DR GeneTree; ENSGT01050000244833; -.
DR HOGENOM; CLU_037388_4_0_1; -.
DR InParanoid; Q80XF7; -.
DR OMA; EMCHLGI; -.
DR OrthoDB; 959629at2759; -.
DR PhylomeDB; Q80XF7; -.
DR Reactome; R-RNO-190861; Gap junction assembly.
DR PRO; PR:Q80XF7; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000038328; Expressed in cerebellum and 15 other tissues.
DR Genevisible; Q80XF7; RN.
DR GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR GO; GO:0005921; C:gap junction; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043209; C:myelin sheath; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0033270; C:paranode region of axon; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:1990769; C:proximal neuron projection; IDA:RGD.
DR GO; GO:0005243; F:gap junction channel activity; ISO:RGD.
DR GO; GO:1903763; F:gap junction channel activity involved in cell communication by electrical coupling; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0010644; P:cell communication by electrical coupling; ISO:RGD.
DR GO; GO:0007267; P:cell-cell signaling; ISO:RGD.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:RGD.
DR GO; GO:1904427; P:positive regulation of calcium ion transmembrane transport; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; IMP:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
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_0000057844"
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 368..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Pro residues"
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:0000250|UniProtKB:Q8BQU6"
SQ SEQUENCE 440 AA; 46990 MW; 7B5D30A849687AE5 CRC64;
MTNMSWSFLT RLLEEIHNHS TFVGKVWLTV LVVFRIVLTA VGGESIYSDE QSKFTCNTRQ
PGCDNVCYDA FAPLSHVRFW VFQIVVISTP SVMYLGYAVH RLARASEQER RRALRRRPGP
RRLPRAQLPP PPPGWPDTTD LGEAEPILAL EEDEDEEPGA PEGPGEDTEE ERTEDVAAKG
GGGDGKTVVT PGPAGQHDGR RRIQREGLMR VYVAQLVVRA AFEVAFLVGQ YLLYGFEVPP
FFACSRQPCP HVVDCFVSRP TEKTVFLLVM YVVSCLCLLL NLCEMAHLGL GSAQDAVRGR
RGASAAGPGP APRPPPCAFP AAAAGLACPP DYSLVVRAAE RARAHDQNLA NLALQALRDG
AAVAAVSADR DSPPCSGLNA TSRGPPRAGG PASGTGSATS GGTVGEQGRS GAQEQLATKP
RVGSEKGSTG SRDGKATVWI
