CXA3_CHICK
ID CXA3_CHICK Reviewed; 511 AA.
AC P29415;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Gap junction alpha-3 protein;
DE AltName: Full=Connexin-56;
DE Short=Cx56;
GN Name=GJA3;
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 [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=7678009; DOI=10.1016/s0021-9258(18)54209-5;
RA Rup D.M., Veenstra R.D., Wang H.Z., Brink P.R., Beyer E.C.;
RT "Chick connexin-56, a novel lens gap junction protein. Molecular cloning
RT and functional expression.";
RL J. Biol. Chem. 268:706-712(1993).
RN [2]
RP SEQUENCE REVISION TO 365-366; 369; 383-385 AND 389.
RA Beyer E.C., Berthoud V.M.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH MIP.
RX PubMed=14762116; DOI=10.1242/jcs.00945;
RA Yu X.S., Jiang J.X.;
RT "Interaction of major intrinsic protein (aquaporin-0) with fiber connexins
RT in lens development.";
RL J. Cell Sci. 117:871-880(2004).
CC -!- FUNCTION: Structural component of lens fiber gap junctions
CC (PubMed:7678009). Gap junctions are dodecameric channels that connect
CC the cytoplasm of adjoining cells. They are formed by the docking of two
CC hexameric hemichannels, one from each cell membrane (By similarity).
CC Small molecules and ions diffuse from one cell to a neighboring cell
CC via the central pore (PubMed:7678009). {ECO:0000250|UniProtKB:Q9TU17,
CC ECO:0000269|PubMed:7678009}.
CC -!- SUBUNIT: A hemichannel or connexon is composed of a hexamer of
CC connexins. A functional gap junction is formed by the apposition of two
CC hemichannels (By similarity). During early stages of lens development,
CC interacts with the C-terminus of MIP (PubMed:14762116).
CC {ECO:0000250|UniProtKB:Q9TU17, ECO:0000269|PubMed:14762116}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9TU17};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9TU17}. Cell
CC junction, gap junction {ECO:0000250|UniProtKB:Q9TU17}.
CC -!- TISSUE SPECIFICITY: Detected in eye lens. {ECO:0000269|PubMed:7678009}.
CC -!- SIMILARITY: Belongs to the connexin family. {ECO:0000305}.
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DR EMBL; L02838; AAA48737.2; -; Genomic_DNA.
DR PIR; A45338; A45338.
DR RefSeq; NP_001035734.1; NM_001040644.1.
DR RefSeq; XP_015133694.1; XM_015278208.1.
DR RefSeq; XP_015133700.1; XM_015278214.1.
DR AlphaFoldDB; P29415; -.
DR SMR; P29415; -.
DR STRING; 9031.ENSGALP00000027629; -.
DR iPTMnet; P29415; -.
DR PaxDb; P29415; -.
DR Ensembl; ENSGALT00000027682; ENSGALP00000027629; ENSGALG00000017137.
DR GeneID; 428084; -.
DR KEGG; gga:428084; -.
DR CTD; 2700; -.
DR VEuPathDB; HostDB:geneid_428084; -.
DR eggNOG; ENOG502QUKJ; Eukaryota.
DR GeneTree; ENSGT01050000244864; -.
DR HOGENOM; CLU_037388_0_2_1; -.
DR InParanoid; P29415; -.
DR OMA; RGRIRMG; -.
DR OrthoDB; 969321at2759; -.
DR PhylomeDB; P29415; -.
DR TreeFam; TF329606; -.
DR Reactome; R-GGA-190861; Gap junction assembly.
DR PRO; PR:P29415; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000017137; Expressed in spleen and 2 other tissues.
DR GO; GO:0005922; C:connexin complex; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of 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:1990349; P:gap junction-mediated intercellular transport; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:InterPro.
DR Gene3D; 1.20.1440.80; -; 1.
DR InterPro; IPR000500; Connexin.
DR InterPro; IPR002262; Connexin46.
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:SF12; PTHR11984:SF12; 1.
DR Pfam; PF00029; Connexin; 1.
DR PRINTS; PR00206; CONNEXIN.
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 1: Evidence at protein 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:Q9TU17"
FT CHAIN 2..511
FT /note="Gap junction alpha-3 protein"
FT /id="PRO_0000057878"
FT INTRAMEM 2..15
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT TOPO_DOM 16..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT TOPO_DOM 41..71
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT TOPO_DOM 93..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT TOPO_DOM 196..223
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT TOPO_DOM 245..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 110..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 54..214
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT DISULFID 61..208
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT DISULFID 65..203
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
SQ SEQUENCE 511 AA; 55793 MW; 7A19FA40079B42DB CRC64;
MGDWSFLGRL LENAQEHSTV IGKVWLTVLF IFRILVLGAA AEEVWGDEQS DFTCNTQQPG
CENVCYDKAF PISHIRFWVL QIIFVSTPTL IYLGHVLHIV RMEEKRKEKE EELKKRGSVK
DNNYPGAATS GGGSGGGNNF KDPPIKMGKE KLPIRDERGR IRMGGALLRT YIFNIIFKTL
FEVGFIVGQY FLYGFELKPV YQCSRPPCPH TVDCFISRPT EKTIFIIFML VVASVSLLLN
MLEIYHLGWK KLKQGMTSQY SLEMPVTTLT PVMVTGESKP VSLPPPAPPV VVTTTAPAPV
LPDTRAVTPL LAPVTMAPYY AAAAPRTRPP SNTASMASYP VAPPVPENRH RAVTPTPVST
PVTIPTPIPT PTPAIINYFN SKSNALAAEQ NWVNMAAEQQ GKAPSSSAGS STPSSVRHPL
PEQEEPLEQL LPLPAGPPIT TTNSGSSTSL SGASGSKWDV EGEEELAEER PISATCTTVE
MHEPPLLVDT RRLSRASKSS SSRARSDDLA V
