CXG1_HUMAN
ID CXG1_HUMAN Reviewed; 396 AA.
AC P36383; B3KW68; Q4VAY0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Gap junction gamma-1 protein;
DE AltName: Full=Connexin-45;
DE Short=Cx45;
DE AltName: Full=Gap junction alpha-7 protein;
GN Name=GJC1; Synonyms=GJA7;
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 [GENOMIC DNA].
RX PubMed=7966354; DOI=10.1006/jmcc.1994.1103;
RA Kanter H.L., Saffitz J.E., Beyer E.C.;
RT "Molecular cloning of two human cardiac gap junction proteins, connexin40
RT and connexin45.";
RL J. Mol. Cell. Cardiol. 26:861-868(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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.
CC -!- SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts
CC with CNST (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P36383; O95236-2: APOL3; NbExp=3; IntAct=EBI-11979659, EBI-11976321;
CC P36383; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11979659, EBI-16439278;
CC P36383; Q6ZP29-3: SLC66A1; NbExp=3; IntAct=EBI-11979659, EBI-12889586;
CC P36383; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-11979659, EBI-12015604;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC junction, gap junction.
CC -!- SIMILARITY: Belongs to the connexin family. Gamma-type subfamily.
CC {ECO:0000305}.
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DR EMBL; U03493; AAA60458.1; -; Genomic_DNA.
DR EMBL; AK124339; BAG54030.1; -; mRNA.
DR EMBL; AC005180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096213; AAH96213.1; -; mRNA.
DR EMBL; BC096214; AAH96214.1; -; mRNA.
DR EMBL; BC096215; AAH96215.1; -; mRNA.
DR EMBL; BC096216; AAH96216.1; -; mRNA.
DR CCDS; CCDS11487.1; -.
DR PIR; I38430; I38430.
DR RefSeq; NP_001073852.1; NM_001080383.1.
DR RefSeq; NP_005488.2; NM_005497.3.
DR RefSeq; XP_005256977.1; XM_005256920.1.
DR RefSeq; XP_005256978.1; XM_005256921.1.
DR PDB; 3SHW; X-ray; 2.90 A; B=387-396.
DR PDBsum; 3SHW; -.
DR AlphaFoldDB; P36383; -.
DR SMR; P36383; -.
DR BioGRID; 115363; 44.
DR ELM; P36383; -.
DR IntAct; P36383; 17.
DR MINT; P36383; -.
DR STRING; 9606.ENSP00000411528; -.
DR TCDB; 1.A.24.2.4; the gap junction-forming connexin (connexin) family.
DR iPTMnet; P36383; -.
DR PhosphoSitePlus; P36383; -.
DR BioMuta; GJC1; -.
DR DMDM; 226693517; -.
DR EPD; P36383; -.
DR jPOST; P36383; -.
DR MassIVE; P36383; -.
DR MaxQB; P36383; -.
DR PaxDb; P36383; -.
DR PeptideAtlas; P36383; -.
DR PRIDE; P36383; -.
DR ProteomicsDB; 55181; -.
DR Antibodypedia; 29882; 359 antibodies from 33 providers.
DR DNASU; 10052; -.
DR Ensembl; ENST00000330514.4; ENSP00000333193.3; ENSG00000182963.11.
DR Ensembl; ENST00000590758.3; ENSP00000466339.1; ENSG00000182963.11.
DR Ensembl; ENST00000592524.6; ENSP00000467201.1; ENSG00000182963.11.
DR GeneID; 10052; -.
DR KEGG; hsa:10052; -.
DR MANE-Select; ENST00000592524.6; ENSP00000467201.1; NM_005497.4; NP_005488.2.
DR UCSC; uc002ihj.4; human.
DR CTD; 10052; -.
DR DisGeNET; 10052; -.
DR GeneCards; GJC1; -.
DR HGNC; HGNC:4280; GJC1.
DR HPA; ENSG00000182963; Tissue enhanced (placenta, smooth muscle).
DR MIM; 608655; gene.
DR neXtProt; NX_P36383; -.
DR OpenTargets; ENSG00000182963; -.
DR PharmGKB; PA164741588; -.
DR VEuPathDB; HostDB:ENSG00000182963; -.
DR eggNOG; ENOG502QV2G; Eukaryota.
DR GeneTree; ENSGT01050000244833; -.
DR HOGENOM; CLU_037388_0_0_1; -.
DR InParanoid; P36383; -.
DR OMA; VRWKQHR; -.
DR OrthoDB; 692491at2759; -.
DR PhylomeDB; P36383; -.
DR TreeFam; TF329606; -.
DR PathwayCommons; P36383; -.
DR Reactome; R-HSA-112303; Electric Transmission Across Gap Junctions.
DR Reactome; R-HSA-190861; Gap junction assembly.
DR SignaLink; P36383; -.
DR BioGRID-ORCS; 10052; 22 hits in 1077 CRISPR screens.
DR ChiTaRS; GJC1; human.
DR GeneWiki; GJC1; -.
DR GenomeRNAi; 10052; -.
DR Pharos; P36383; Tbio.
DR PRO; PR:P36383; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P36383; protein.
DR Bgee; ENSG00000182963; Expressed in cauda epididymis and 164 other tissues.
DR ExpressionAtlas; P36383; baseline and differential.
DR Genevisible; P36383; HS.
DR GO; GO:0005922; C:connexin complex; ISS:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005921; C:gap junction; TAS:ProtInc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014704; C:intercalated disc; TAS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005243; F:gap junction channel activity; IBA:GO_Central.
DR GO; GO:0086077; F:gap junction channel activity involved in AV node cell-bundle of His cell electrical coupling; ISS:BHF-UCL.
DR GO; GO:0086020; F:gap junction channel activity involved in SA node cell-atrial cardiac muscle cell electrical coupling; NAS:BHF-UCL.
DR GO; GO:0005216; F:ion channel activity; IEA:Ensembl.
DR GO; GO:0086014; P:atrial cardiac muscle cell action potential; TAS:BHF-UCL.
DR GO; GO:0086053; P:AV node cell to bundle of His cell communication by electrical coupling; ISS:BHF-UCL.
DR GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
DR GO; GO:0048468; P:cell development; IEA:Ensembl.
DR GO; GO:0007043; P:cell-cell junction assembly; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0016264; P:gap junction assembly; ISS:BHF-UCL.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:0086021; P:SA node cell to atrial cardiac muscle cell communication by electrical coupling; NAS:BHF-UCL.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR Gene3D; 1.20.1440.80; -; 1.
DR InterPro; IPR000500; Connexin.
DR InterPro; IPR002265; Connexin45.
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 PRINTS; PR01136; CONNEXINA6.
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..396
FT /note="Gap junction gamma-1 protein"
FT /id="PRO_0000057826"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 145..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 382
FT /note="T -> A (in Ref. 2; BAG54030)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="T -> N (in Ref. 1; AAA60458 and 4; AAH96213/
FT AAH96214/AAH96215/AAH96216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 45470 MW; C9F67C1D926D40DF CRC64;
MSWSFLTRLL EEIHNHSTFV GKIWLTVLIV FRIVLTAVGG ESIYYDEQSK FVCNTEQPGC
ENVCYDAFAP LSHVRFWVFQ IILVATPSVM YLGYAIHKIA KMEHGEADKK AARSKPYAMR
WKQHRALEET EEDNEEDPMM YPEMELESDK ENKEQSQPKP KHDGRRRIRE DGLMKIYVLQ
LLARTVFEVG FLIGQYFLYG FQVHPFYVCS RLPCPHKIDC FISRPTEKTI FLLIMYGVTG
LCLLLNIWEM LHLGFGTIRD SLNSKRRELE DPGAYNYPFT WNTPSAPPGY NIAVKPDQIQ
YTELSNAKIA YKQNKANTAQ EQQYGSHEEN LPADLEALQR EIRMAQERLD LAVQAYSHQN
NPHGPREKKA KVGSKAGSNK STASSKSGDG KTSVWI
