CXA1_XENLA
ID CXA1_XENLA Reviewed; 379 AA.
AC P16863; Q6GNU5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Gap junction alpha-1 protein;
DE AltName: Full=Connexin-43;
DE Short=Cx43;
GN Name=gja1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=2155241; DOI=10.1083/jcb.110.3.597;
RA Gimlich R.L., Kumar N.M., Gilula N.B.;
RT "Differential regulation of the levels of three gap junction mRNAs in
RT Xenopus embryos.";
RL J. Cell Biol. 110:597-605(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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. Plays an
CC essential role in gap junction communication in the ventricles.
CC {ECO:0000250|UniProtKB:O57474, ECO:0000250|UniProtKB:P23242}.
CC -!- SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts
CC with TMEM65. {ECO:0000250|UniProtKB:P23242}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17302};
CC Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction
CC {ECO:0000250|UniProtKB:P17302}. Note=Localizes at the intercalated disk
CC (ICD) in cardiomyocytes and proper localization at ICD is dependent on
CC TMEM65. {ECO:0000250|UniProtKB:P23242}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues. Highest levels found in
CC eye and brain.
CC -!- DEVELOPMENTAL STAGE: Appears during organogenesis.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
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DR EMBL; X17243; CAA35108.1; -; mRNA.
DR EMBL; BC073407; AAH73407.1; -; mRNA.
DR PIR; A34575; A34575.
DR RefSeq; NP_001079129.1; NM_001085660.1.
DR RefSeq; XP_018117108.1; XM_018261619.1.
DR AlphaFoldDB; P16863; -.
DR SMR; P16863; -.
DR DNASU; 373664; -.
DR GeneID; 373664; -.
DR KEGG; xla:373664; -.
DR CTD; 373664; -.
DR Xenbase; XB-GENE-876609; gja1.L.
DR OMA; LIQWYMY; -.
DR OrthoDB; 823525at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 373664; Expressed in brain and 16 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005922; C:connexin complex; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055077; F:gap junction hemi-channel activity; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR GO; GO:0007507; P:heart development; IEA:InterPro.
DR GO; GO:0099111; P:microtubule-based transport; ISS:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR Gene3D; 1.20.1440.80; -; 1.
DR Gene3D; 1.20.5.1130; -; 1.
DR InterPro; IPR035091; Alpha_helix_dom_sf.
DR InterPro; IPR000500; Connexin.
DR InterPro; IPR002261; Connexin43.
DR InterPro; IPR013124; Connexin43_C.
DR InterPro; IPR034634; Connexin_C.
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 PANTHER; PTHR11984:SF33; PTHR11984:SF33; 1.
DR Pfam; PF00029; Connexin; 1.
DR Pfam; PF03508; Connexin43; 1.
DR PRINTS; PR00206; CONNEXIN.
DR PRINTS; PR01132; CONNEXINA1.
DR SMART; SM00037; CNX; 1.
DR SMART; SM01089; Connexin_CCC; 1.
DR SUPFAM; SSF118220; SSF118220; 1.
DR PROSITE; PS00407; CONNEXINS_1; 1.
DR PROSITE; PS00408; CONNEXINS_2; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Disulfide bond; Gap junction; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT CHAIN 2..379
FT /note="Gap junction alpha-1 protein"
FT /id="PRO_0000057806"
FT TOPO_DOM 2..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..76
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..207
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT REGION 322..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 54..192
FT /evidence="ECO:0000250|UniProtKB:P17302"
FT DISULFID 187..198
FT /evidence="ECO:0000250|UniProtKB:P17302"
SQ SEQUENCE 379 AA; 42961 MW; 4FD12B031F595DDD CRC64;
MGDWSALGRL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS AFVCNTQQPG
CENVCYDKSF PISHVRFWVL QIIFVSTPTL LYLAHVFYLM RKEEKLNRKE EELKMVQNEG
GNVDMHLKQI EIKKFKYGLE EHGKVKMRGG LLRTYIISIL FKSVFEVGFI IIQWYMYGFS
LSAIYTCKRD PCPHQVDCFL SRPTEKTIFI WFMLIVSIVS LALNIIELFY VTYKSIKDGI
KGKKDPFSAT NDAVISGKEC GSPKYAYFNG CSSPTAPMSP PGYKLVTGER NPSSCRNYNK
QASEQNWANY SAEQNRMGQA GSTISNTHAQ PFDFSDEHQN TKKMAPGHEM QPLTILDQRP
SSRASSHASS RPRPDDLEI
