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CXG2_BOVIN
ID   CXG2_BOVIN              Reviewed;         429 AA.
AC   Q29RK8;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Gap junction gamma-2 protein;
DE   AltName: Full=Gap junction alpha-12 protein;
GN   Name=GJC2; Synonyms=GJA12;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) 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. May play a role
CC       in myelination in central and peripheral nervous systems (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts
CC       with TJP1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the connexin family. Gamma-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC114129; AAI14130.1; -; mRNA.
DR   RefSeq; NP_001039905.1; NM_001046440.1.
DR   RefSeq; XP_005208463.1; XM_005208406.3.
DR   RefSeq; XP_005208464.1; XM_005208407.3.
DR   AlphaFoldDB; Q29RK8; -.
DR   SMR; Q29RK8; -.
DR   STRING; 9913.ENSBTAP00000019857; -.
DR   PaxDb; Q29RK8; -.
DR   Ensembl; ENSBTAT00000019857; ENSBTAP00000019857; ENSBTAG00000014916.
DR   GeneID; 538745; -.
DR   KEGG; bta:538745; -.
DR   CTD; 57165; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014916; -.
DR   VGNC; VGNC:29383; GJC2.
DR   eggNOG; ENOG502QV2G; Eukaryota.
DR   GeneTree; ENSGT01050000244833; -.
DR   InParanoid; Q29RK8; -.
DR   OMA; PPYNYAY; -.
DR   OrthoDB; 959629at2759; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000014916; Expressed in pons and 68 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:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0005243; F:gap junction channel activity; IBA:GO_Central.
DR   GO; GO:1903763; F:gap junction channel activity involved in cell communication by electrical coupling; IEA:Ensembl.
DR   GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
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; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..429
FT                   /note="Gap junction gamma-2 protein"
FT                   /id="PRO_0000244876"
FT   TOPO_DOM        1..25
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..78
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..214
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        236..263
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        285..429
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          106..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..139
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..170
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         366
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BQU6"
SQ   SEQUENCE   429 AA;  46067 MW;  068C71AFEBBE9E6B CRC64;
     MTNMSWSFLT RLLEEIHNHS TFVGKVWLTV LVVFRIVLTA VGGESIYSDE QTKFTCNTRQ
     PGCDNVCYDA FAPLSHVRFW VFQIVVISTP SVMYLGYAVH RLARASQDER RRASRRRPSR
     RAPRPPLPLP PPPHPGWPEP ADLGEEEPML GLGEEDEDPG VAEGLGEDEE AEDTGAAKGA
     GGDTKVAGVP GPAGQHDGRR RIQREGLMRV YVAQLVARAA FEVAFLVGQY LLYGFEVRPF
     FACSRQPCPH VVDCFVSRPT EKTVFLLVMY VVSCLCLLLN LCEMAHLGLG NAQDAVRGRR
     PLPASPGPMP RPPPCALPAA PSGLACPPDY SLVVRTAEHA RAQDQELASL ALQALQDRRA
     LGDLDSPPGP GLPANARGPP KPGAPASGSG SATSGGTVGG QGRQGIKPRM GSEKGSGSSS
     REGKTTVWI
 
 
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