CXA3_SHEEP
ID CXA3_SHEEP Reviewed; 413 AA.
AC Q9TU17;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Gap junction alpha-3 protein;
DE AltName: Full=Connexin-44;
DE Short=Cx44 {ECO:0000303|PubMed:30542154};
GN Name=GJA3;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Eye;
RX PubMed=10937579;
RA Yang D.-I., Louis C.F.;
RT "Molecular cloning of ovine connexin44 and temporal expression of gap
RT junction proteins in a lens cell culture.";
RL Invest. Ophthalmol. Vis. Sci. 41:2658-2664(2000).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 2-348, PROTEIN
RP SEQUENCE OF 2-9, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, TISSUE
RP SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, AND DISULFIDE BOND.
RX PubMed=30542154; DOI=10.1038/s41586-018-0786-7;
RA Myers J.B., Haddad B.G., O'Neill S.E., Chorev D.S., Yoshioka C.C.,
RA Robinson C.V., Zuckerman D.M., Reichow S.L.;
RT "Structure of native lens connexin 46/50 intercellular channels by cryo-
RT EM.";
RL Nature 564:372-377(2018).
CC -!- FUNCTION: Structural component of lens fiber gap junctions. Gap
CC junctions are dodecameric channels that connect the cytoplasm of
CC adjoining cells. They are formed by the docking of two hexameric
CC hemichannels, one from each cell membrane. Small molecules and ions
CC diffuse from one cell to a neighboring cell via the central pore.
CC {ECO:0000269|PubMed:30542154}.
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 (PubMed:30542154). Forms heteromeric channels with GJA8
CC (PubMed:30542154). {ECO:0000269|PubMed:30542154}.
CC -!- INTERACTION:
CC Q9TU17; P55917: GJA8; NbExp=2; IntAct=EBI-21347162, EBI-21347179;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30542154};
CC Multi-pass membrane protein {ECO:0000269|PubMed:30542154}. Cell
CC junction, gap junction {ECO:0000269|PubMed:30542154}.
CC -!- TISSUE SPECIFICITY: Detected in eye lens (at protein level)
CC (PubMed:30542154). Only detected in the lens. Not detected in heart,
CC kidney, liver, or lung. {ECO:0000269|PubMed:10937579,
CC ECO:0000269|PubMed:30542154}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
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DR EMBL; AF177912; AAD56220.1; -; Genomic_DNA.
DR PDB; 6MHQ; EM; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L=2-348.
DR PDB; 7JKC; EM; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-413.
DR PDB; 7JMD; EM; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-413.
DR PDB; 7JN0; EM; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-413.
DR PDB; 7JN1; EM; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-413.
DR PDBsum; 6MHQ; -.
DR PDBsum; 7JKC; -.
DR PDBsum; 7JMD; -.
DR PDBsum; 7JN0; -.
DR PDBsum; 7JN1; -.
DR AlphaFoldDB; Q9TU17; -.
DR SMR; Q9TU17; -.
DR IntAct; Q9TU17; 1.
DR eggNOG; ENOG502QUKJ; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005922; C:connexin complex; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0055077; F:gap junction hemi-channel activity; ISS:UniProtKB.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Gap junction; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:30542154"
FT CHAIN 2..413
FT /note="Gap junction alpha-3 protein"
FT /id="PRO_0000057813"
FT INTRAMEM 2..15
FT /evidence="ECO:0000269|PubMed:30542154"
FT TOPO_DOM 16..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TOPO_DOM 41..71
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TOPO_DOM 93..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TOPO_DOM 171..198
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TOPO_DOM 220..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30542154"
FT REGION 108..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 54..189
FT /evidence="ECO:0000269|PubMed:30542154,
FT ECO:0007744|PDB:6MHQ"
FT DISULFID 61..183
FT /evidence="ECO:0000269|PubMed:30542154,
FT ECO:0007744|PDB:6MHQ"
FT DISULFID 65..178
FT /evidence="ECO:0000269|PubMed:30542154,
FT ECO:0007744|PDB:6MHQ"
FT HELIX 5..16
FT /evidence="ECO:0007829|PDB:7JKC"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:7JKC"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:7JKC"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:7JKC"
FT TURN 45..51
FT /evidence="ECO:0007829|PDB:7JKC"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:7JKC"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:7JKC"
FT HELIX 74..108
FT /evidence="ECO:0007829|PDB:7JKC"
FT HELIX 141..168
FT /evidence="ECO:0007829|PDB:7JKC"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:7JKC"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6MHQ"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:7JKC"
FT HELIX 194..223
FT /evidence="ECO:0007829|PDB:7JKC"
SQ SEQUENCE 413 AA; 43989 MW; 2E9AD57278A67A0A CRC64;
MGDWSFLGRL LENAQEHSTV IGKVWLTVLF IFRILVLGAA AEEVWGDEQS DFTCNTQQPG
CENVCYDRAF PISHVRFWVL QIIFVSTPTL IYLGHVLHLV RMEEKRKERE EEPPKAAGPA
EEHQDPAPVR DDRGKVRIAG ALLRTYVFNI IFKTLFEVGF IAGQYFLYGF QLKPLYRCDR
WPCPNTVDCF ISRPTEKTIF ILFMLAVACV SLLLNVLEIY HLGWKKLKQG MTSPFRPDTP
GSRAGSAKPM GGSPLLLPPN SAPPAVTIGF PPYYAPSASS LGQASAPGYP EPPLPAALPG
TPGTPGTPGT LGGGGGNQGL RAPAQNCANR EAEPQTSARK ASPPASTPPA APAGGPQQFL
PGGAAGSSGD SDGEGAVTAV ELHAPPEPPA DPGRSSKASK SSGGRARAAD LAI
