CXG3_HUMAN
ID CXG3_HUMAN Reviewed; 279 AA.
AC Q8NFK1; A4D296; Q86XI9;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Gap junction gamma-3 protein;
DE AltName: Full=Connexin-30.2;
DE Short=Cx30.2;
DE AltName: Full=Connexin-31.3;
DE Short=Cx31.3;
DE AltName: Full=Gap junction epsilon-1 protein;
GN Name=GJC3; Synonyms=GJE1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12151525; DOI=10.1523/jneurosci.22-15-06458.2002;
RA Altevogt B.M., Kleopa K.A., Postma F.R., Scherer S.S., Paul D.L.;
RT "Connexin29 is uniquely distributed within myelinating glial cells of the
RT central and peripheral nervous systems.";
RL J. Neurosci. 22:6458-6470(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Corpus callosum;
RA Enriquez A.D., Scherer S.S.;
RT "Human connexin 31.3 ORF.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-279.
RC TISSUE=Pancreas;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=12881038; DOI=10.1080/15419060302063;
RA Soehl G., Nielsen P.A., Eiberger J., Willecke K.;
RT "Expression profiles of the novel human connexin genes hCx30.2, hCx40.1,
RT and hCx62 differ from their putative mouse orthologues.";
RL Cell Commun. Adhes. 10:27-36(2003).
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 -!- INTERACTION:
CC Q8NFK1; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-20110678, EBI-12070086;
CC Q8NFK1; O15400: STX7; NbExp=3; IntAct=EBI-20110678, EBI-3221827;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: CNS specific. Expression is restricted to brain,
CC spinal cord, and sciatic nerve. According to PubMed:12881038,
CC expression is abundant in skeletal muscle, liver, and heart, and to a
CC minor degree in pancreas and kidney. {ECO:0000269|PubMed:12151525,
CC ECO:0000269|PubMed:12881038}.
CC -!- SIMILARITY: Belongs to the connexin family. Gamma-type subfamily.
CC {ECO:0000305}.
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DR EMBL; AF503615; AAM21145.1; -; mRNA.
DR EMBL; AY297109; AAP51161.1; -; mRNA.
DR EMBL; CH236956; EAL23863.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76624.1; -; Genomic_DNA.
DR EMBL; BC043381; AAH43381.1; -; mRNA.
DR CCDS; CCDS34697.1; -.
DR RefSeq; NP_853516.1; NM_181538.2.
DR PDB; 6L3T; EM; 2.34 A; A/B/C/D/E/F=1-279.
DR PDB; 6L3U; EM; 2.53 A; A/B/C/D/E/F=1-279.
DR PDB; 6L3V; EM; 2.63 A; A/B/C/D/E/F=1-279.
DR PDBsum; 6L3T; -.
DR PDBsum; 6L3U; -.
DR PDBsum; 6L3V; -.
DR AlphaFoldDB; Q8NFK1; -.
DR SMR; Q8NFK1; -.
DR BioGRID; 131549; 2.
DR IntAct; Q8NFK1; 2.
DR STRING; 9606.ENSP00000325775; -.
DR TCDB; 1.A.24.1.7; the gap junction-forming connexin (connexin) family.
DR iPTMnet; Q8NFK1; -.
DR PhosphoSitePlus; Q8NFK1; -.
DR BioMuta; GJC3; -.
DR DMDM; 32171365; -.
DR MassIVE; Q8NFK1; -.
DR PaxDb; Q8NFK1; -.
DR PeptideAtlas; Q8NFK1; -.
DR PRIDE; Q8NFK1; -.
DR ProteomicsDB; 73321; -.
DR Antibodypedia; 3109; 181 antibodies from 27 providers.
DR DNASU; 349149; -.
DR Ensembl; ENST00000312891.3; ENSP00000325775.2; ENSG00000176402.6.
DR GeneID; 349149; -.
DR KEGG; hsa:349149; -.
DR MANE-Select; ENST00000312891.3; ENSP00000325775.2; NM_181538.3; NP_853516.1.
DR UCSC; uc011kjd.2; human.
DR CTD; 349149; -.
DR DisGeNET; 349149; -.
DR GeneCards; GJC3; -.
DR HGNC; HGNC:17495; GJC3.
DR HPA; ENSG00000176402; Tissue enhanced (breast, pancreas, salivary gland).
DR MIM; 611925; gene.
DR neXtProt; NX_Q8NFK1; -.
DR OpenTargets; ENSG00000176402; -.
DR PharmGKB; PA162389705; -.
DR VEuPathDB; HostDB:ENSG00000176402; -.
DR eggNOG; ENOG502QVY2; Eukaryota.
DR GeneTree; ENSGT01050000244962; -.
DR HOGENOM; CLU_037388_4_0_1; -.
DR InParanoid; Q8NFK1; -.
DR OMA; CYDAFHP; -.
DR OrthoDB; 1092887at2759; -.
DR PhylomeDB; Q8NFK1; -.
DR TreeFam; TF329606; -.
DR PathwayCommons; Q8NFK1; -.
DR SignaLink; Q8NFK1; -.
DR BioGRID-ORCS; 349149; 11 hits in 1066 CRISPR screens.
DR GeneWiki; GJC3; -.
DR GenomeRNAi; 349149; -.
DR Pharos; Q8NFK1; Tbio.
DR PRO; PR:Q8NFK1; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8NFK1; protein.
DR Bgee; ENSG00000176402; Expressed in tibial nerve and 88 other tissues.
DR GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0005243; F:gap junction channel activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
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 3D-structure; Cell junction; Cell membrane; Gap junction; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..279
FT /note="Gap junction gamma-3 protein"
FT /id="PRO_0000057874"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 238..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:6L3T"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:6L3T"
FT HELIX 24..44
FT /evidence="ECO:0007829|PDB:6L3T"
FT TURN 45..50
FT /evidence="ECO:0007829|PDB:6L3T"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:6L3T"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:6L3T"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:6L3T"
FT HELIX 86..103
FT /evidence="ECO:0007829|PDB:6L3T"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:6L3T"
FT HELIX 130..159
FT /evidence="ECO:0007829|PDB:6L3T"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:6L3T"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6L3T"
FT HELIX 185..211
FT /evidence="ECO:0007829|PDB:6L3T"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:6L3T"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:6L3T"
SQ SEQUENCE 279 AA; 31299 MW; 71810BB8E30533BC CRC64;
MCGRFLRRLL AEESRRSTPV GRLLLPVLLG FRLVLLAASG PGVYGDEQSE FVCHTQQPGC
KAACFDAFHP LSPLRFWVFQ VILVAVPSAL YMGFTLYHVI WHWELSGKGK EEETLIQGRE
GNTDVPGAGS LRLLWAYVAQ LGARLVLEGA ALGLQYHLYG FQMPSSFACR REPCLGSITC
NLSRPSEKTI FLKTMFGVSG FCLLFTFLEL VLLGLGRWWR TWKHKSSSSK YFLTSESTRR
HKKATDSLPV VETKEQFQEA VPGRSLAQEK QRPVGPRDA
