CXA3_BOVIN
ID CXA3_BOVIN Reviewed; 407 AA.
AC P41987;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Gap junction alpha-3 protein;
DE AltName: Full=Connexin-44;
DE Short=Cx44;
GN Name=GJA3;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Lens;
RX PubMed=8088962;
RA Gupta V.K., Berthoud V.M., Atal N., Jarillo J.A., Barrio L.C., Beyer E.C.;
RT "Bovine connexin44, a lens gap junction protein: molecular cloning,
RT immunologic characterization, and functional expression.";
RL Invest. Ophthalmol. Vis. Sci. 35:3747-3758(1994).
RN [2]
RP SEQUENCE REVISION TO 115-120; 207; 253; 285-295; 300-316; 340-365 AND 402.
RA Beyer E.C., Berthoud V.M.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Structural component of lens fiber gap junctions
CC (PubMed:8088962). 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:8088962). {ECO:0000250|UniProtKB:Q9TU17,
CC ECO:0000269|PubMed:8088962}.
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). Forms heteromeric channels with GJA8 (By
CC similarity). {ECO:0000250|UniProtKB:Q9TU17}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8088962};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8088962}. Cell
CC junction, gap junction {ECO:0000269|PubMed:8088962}.
CC -!- TISSUE SPECIFICITY: Only detected in the lens.
CC {ECO:0000269|PubMed:8088962}.
CC -!- DEVELOPMENTAL STAGE: Higher expression in pre-natal (1-5 months
CC gestation) than in postnatal (4-6 months) calf lens.
CC {ECO:0000269|PubMed:8088962}.
CC -!- PTM: Phosphorylated on multiple threonine and serine residues.
CC Phosphorylation may have a role in assembling connexins into connexons
CC and gap junctional plaques, as well as channel gating.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
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DR EMBL; U08213; AAA50954.2; -; Genomic_DNA.
DR PIR; I46053; I46053.
DR RefSeq; NP_001159768.1; NM_001166296.1.
DR RefSeq; XP_005213817.1; XM_005213760.3.
DR AlphaFoldDB; P41987; -.
DR SMR; P41987; -.
DR STRING; 9913.ENSBTAP00000027188; -.
DR iPTMnet; P41987; -.
DR PaxDb; P41987; -.
DR PRIDE; P41987; -.
DR Ensembl; ENSBTAT00000027188; ENSBTAP00000027188; ENSBTAG00000020400.
DR GeneID; 100140301; -.
DR KEGG; bta:100140301; -.
DR CTD; 2700; -.
DR VEuPathDB; HostDB:ENSBTAG00000020400; -.
DR VGNC; VGNC:29372; GJA3.
DR eggNOG; ENOG502QUKJ; Eukaryota.
DR GeneTree; ENSGT01050000244864; -.
DR HOGENOM; CLU_037388_0_1_1; -.
DR InParanoid; P41987; -.
DR OMA; VEMHAPP; -.
DR OrthoDB; 969321at2759; -.
DR TreeFam; TF329606; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000020400; Expressed in cardiac ventricle and 7 other tissues.
DR ExpressionAtlas; P41987; baseline.
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 PRINTS; PR01133; CONNEXINA3.
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 Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT CHAIN 2..407
FT /note="Gap junction alpha-3 protein"
FT /id="PRO_0000057809"
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..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT TOPO_DOM 170..197
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT TOPO_DOM 219..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 108..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 54..188
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT DISULFID 61..182
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
FT DISULFID 65..177
FT /evidence="ECO:0000250|UniProtKB:Q9TU17"
SQ SEQUENCE 407 AA; 43611 MW; 24E705B8A9BF0053 CRC64;
MGDWSFLGRL LENAQEHSTV IGKVWLTVLF IFRILVLGAA AEEVWGDEQS DFTCNTQQPG
CENVCYDRAF PISHVRFWVL QIIFVSTPTL IYLGHVLHLV RMEEKRKERE EEPPKAAGPE
GHQDPAPVRD DRGKVRIAGA LLRTYVFNII FKTLFEVGFI AGQYFLYGFQ LKPLYRCDRW
PCPNTVDCFI SRPTEKTIFI LFMLAVACVS LLLNVLEIYH LGWKKLKQGM TSPFRPDTPG
SRAGSVKPVG GSPLLLPPNS APPAVTIGFP PYYAPSASSL GQASAPGYPE PPPPAALPGT
PGTPGGGGNQ GLRARAQNWA NREAEPQTSS RKASPPAPTP PAAESPGGGP QQSLPEGAAG
SSGDSDGEGA VTAVELHAPP EPPADPGRSS KASKSSGGRA RAGDLAI
