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   27-MAR-2024, entry version 163.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   EMDB; EMD-0825; -.
DR   EMDB; EMD-0826; -.
DR   EMDB; EMD-0827; -.
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; 9606-ENSP00000325775; -.
DR   PeptideAtlas; Q8NFK1; -.
DR   ProteomicsDB; 73321; -.
DR   Antibodypedia; 3109; 214 antibodies from 28 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   AGR; HGNC:17495; -.
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; ENSGT01090000260005; -.
DR   HOGENOM; CLU_037388_4_0_1; -.
DR   InParanoid; Q8NFK1; -.
DR   OMA; GCKAACY; -.
DR   OrthoDB; 5262791at2759; -.
DR   PhylomeDB; Q8NFK1; -.
DR   TreeFam; TF329606; -.
DR   PathwayCommons; Q8NFK1; -.
DR   SignaLink; Q8NFK1; -.
DR   BioGRID-ORCS; 349149; 11 hits in 1144 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 cell types or tissues.
DR   GO; GO:0005922; C:connexin complex; IBA:GO_Central.
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; 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:SF56; GAP JUNCTION GAMMA-3 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.
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
//