ID   CXA2_XENLA              Reviewed;         334 AA.
AC   P16864;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Gap junction alpha-2 protein;
DE   AltName: Full=Connexin-38;
DE            Short=Cx38;
GN   Name=gja2;
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 [MRNA].
RX   PubMed=2466337; DOI=10.1126/science.2466337;
RA   Ebihara L., Beyer E.C., Swenson K.I., Paul D.L., Goodenough D.A.;
RT   "Cloning and expression of a Xenopus embryonic gap junction protein.";
RL   Science 243:1194-1194(1989).
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.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC       junction, gap junction.
CC   -!- TISSUE SPECIFICITY: Resides primarily in the ovary, oocytes and early
CC       embryos.
CC   -!- DEVELOPMENTAL STAGE: It is a maternal protein that disappears by the
CC       late gastrula stage.
CC   -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC       subfamily. {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; X17242; CAA35107.1; -; mRNA.
DR   EMBL; J03091; AAA49680.1; -; mRNA.
DR   PIR; A40166; A40166.
DR   PIR; B34575; B34575.
DR   RefSeq; XP_018103585.1; XM_018248096.1.
DR   RefSeq; XP_018103586.1; XM_018248097.1.
DR   AlphaFoldDB; P16864; -.
DR   SMR; P16864; -.
DR   DNASU; 397866; -.
DR   GeneID; 397866; -.
DR   CTD; 397866; -.
DR   Xenbase; XB-GENE-22062680; cx38.S.
DR   OMA; SKMVCNT; -.
DR   OrthoDB; 1716699at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 397866; Expressed in ovary and 5 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:0007154; P:cell communication; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Gap junction; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..334
FT                   /note="Gap junction alpha-2 protein"
FT                   /id="PRO_0000057808"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..75
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        99..153
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..334
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        73
FT                   /note="S -> Y (in Ref. 2; AAA49680)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="I -> T (in Ref. 2; AAA49680)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="H -> Y (in Ref. 2; AAA49680)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235
FT                   /note="S -> P (in Ref. 2; AAA49680)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        267
FT                   /note="S -> A (in Ref. 2; AAA49680)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        279
FT                   /note="R -> S (in Ref. 2; AAA49680)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        323
FT                   /note="S -> R (in Ref. 2; AAA49680)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  37832 MW;  8E339B5E22E2CAE7 CRC64;
     MAGWELLKLL LDDVQEHSTL IGKVWLTVLF IFRIFILSVA GESVWTDEQS DFICNTQQPG
     CTNVCYDQAF PISHVRYWVL QFLFVSTPTL IYLGHMVYLS KKEEKERQKE NESRILVANE
     AQTEVHSSAT KKIRIQGPLM CTYTTSVVFK SIFEAGFLLG QWYIYGFVMS PIFVCERIPC
     KHKVECFVSR PMEKTIFIIF MLVVSLISLL LNLMELIHLS FKCFQHGIKE GATCSPTGIP
     FNGAGNRMPP QEYTNPPSSN QDIDLPSYNK MSGGHNWSRI QMEQQVNGLV KPKCQCDCWS
     QSAISVVVSG APGIISNMDA VKSNHQTSSK QQYV