CXA1_CHICK
ID CXA1_CHICK Reviewed; 381 AA.
AC P14154; Q90ZE0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Gap junction alpha-1 protein;
DE AltName: Full=Connexin-43;
DE Short=Cx43;
GN Name=GJA1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=2166164; DOI=10.1007/bf01868674;
RA Musil L.S., Beyer E.C., Goodenough D.A.;
RT "Expression of the gap junction protein connexin43 in embryonic chick lens:
RT molecular cloning, ultrastructural localization, and post-translational
RT phosphorylation.";
RL J. Membr. Biol. 116:163-175(1990).
RN [2]
RP SEQUENCE REVISION TO 49-50 AND 132.
RA Beyer E.C., Berthoud V.M.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 13-146.
RX PubMed=12487409; DOI=10.1080/15419060214149;
RA Sokolova I.V., Martinez A.-M., Fletcher W.H.;
RT "The highly conserved Gln49 and Ser50 of mammalian connexin43 are present
RT in chick connexin43 and essential for functional gap junction channels.";
RL Cell Commun. Adhes. 9:75-86(2002).
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: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: In all tissues, but mostly in lens.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
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DR EMBL; M29003; AAA48715.2; -; mRNA.
DR EMBL; AF233738; AAK58512.1; -; Genomic_DNA.
DR PIR; A48171; A48171.
DR RefSeq; NP_989917.1; NM_204586.2.
DR AlphaFoldDB; P14154; -.
DR SMR; P14154; -.
DR STRING; 9031.ENSGALP00000023950; -.
DR PaxDb; P14154; -.
DR GeneID; 395278; -.
DR KEGG; gga:395278; -.
DR CTD; 2697; -.
DR VEuPathDB; HostDB:geneid_395278; -.
DR eggNOG; ENOG502QRAE; Eukaryota.
DR InParanoid; P14154; -.
DR OrthoDB; 823525at2759; -.
DR PhylomeDB; P14154; -.
DR PRO; PR:P14154; -.
DR Proteomes; UP000000539; Unplaced.
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:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005243; F:gap junction channel activity; IBA:GO_Central.
DR GO; GO:0055077; F:gap junction hemi-channel activity; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IEA:InterPro.
DR GO; GO:0099111; P:microtubule-based transport; ISS: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..381
FT /note="Gap junction alpha-1 protein"
FT /id="PRO_0000057805"
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..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P08050"
FT REGION 338..381
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"
FT CONFLICT 132
FT /note="S -> I (in Ref. 3; AAK58512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 43125 MW; 6714ED97A17DB75F CRC64;
MGDWSALGKL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS AFRCNTQQPG
CENVCYDKSF PISHVRFWVL QIIFVSVPTL LYLAHVFYVM RKEEKLNKRE EELKVVQNDG
VNVDMHLKQI ESKKFKYGIE EHGKVKMRGG LLRTYIISIL FKSVFEVAFL LIQWYIYGFS
LSAIYTCERD PCPHRVDCFL SRPTEKTIFI VFMLVVSLVS LALNIIELFY VFFKGVKDRV
KGKTDPYSHS GTMSPSKDCG SPKYAYYNGC SSPTAPLSPM SPPGYKLVTG DRNNSSCRNY
NKQASEQNWA NYSAEQNRMG QAGSTISNSH AQPFDFADEH QNTKKLASGH ELQPLTIVDQ
RPPSRASSRA SSRPRPDDLE I
