CXA8_SHEEP
ID CXA8_SHEEP Reviewed; 440 AA.
AC P55917; Q9MYL3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Gap junction alpha-8 protein;
DE AltName: Full=Connexin-49 {ECO:0000303|PubMed:8654111};
DE Short=Cx49 {ECO:0000303|PubMed:30542154};
DE AltName: Full=Lens fiber protein MP70 {ECO:0000303|PubMed:8654111};
DE AltName: Full=MP38;
DE AltName: Full=MP64;
GN Name=GJA8;
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.
RX PubMed=8654111; DOI=10.3109/02713689609007625;
RA Yang D.-I., Louis C.F.;
RT "Molecular cloning of sheep connexin49 and its identity with MP70.";
RL Curr. Eye Res. 15:307-314(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yang D.-I., Louis C.F.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-21.
RC TISSUE=Lens;
RX PubMed=2830542; DOI=10.1038/331721a0;
RA Kistler J., Christie D., Bullivant S.;
RT "Homologies between gap junction proteins in lens, heart and liver.";
RL Nature 331:721-723(1988).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, TOPOLOGY, SUBUNIT, TISSUE SPECIFICITY, IDENTIFICATION BY MASS
RP SPECTROMETRY, DISULFIDE BONDS, AND PARTIAL PROTEIN SEQUENCE.
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 eye lens gap junctions. Gap junctions
CC are dodecameric channels that connect the cytoplasm of adjoining cells.
CC They are formed by the docking of two hexameric hemichannels, one from
CC each cell membrane. Small molecules and ions diffuse from one cell to a
CC neighboring cell via the central pore. {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 GJA3
CC (PubMed:30542154). {ECO:0000269|PubMed:30542154}.
CC -!- INTERACTION:
CC P55917; Q9TU17: GJA3; NbExp=2; IntAct=EBI-21347179, EBI-21347162;
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). Eye lens (PubMed:8654111).
CC {ECO:0000269|PubMed:30542154, ECO:0000269|PubMed:8654111}.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
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DR EMBL; AF177913; AAF01367.1; -; Genomic_DNA.
DR RefSeq; NP_001123510.1; NM_001130038.1.
DR PDB; 6MHY; EM; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L=2-440.
DR PDB; 7JJP; EM; 1.94 A; A/B/C/D/E/F/G/H/I/J/K/L=1-440.
DR PDB; 7JLW; EM; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-440.
DR PDB; 7JM9; EM; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-440.
DR PDB; 7JMC; EM; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-440.
DR PDBsum; 6MHY; -.
DR PDBsum; 7JJP; -.
DR PDBsum; 7JLW; -.
DR PDBsum; 7JM9; -.
DR PDBsum; 7JMC; -.
DR AlphaFoldDB; P55917; -.
DR SMR; P55917; -.
DR IntAct; P55917; 1.
DR STRING; 9940.ENSOARP00000013175; -.
DR PRIDE; P55917; -.
DR GeneID; 100170231; -.
DR KEGG; oas:100170231; -.
DR CTD; 2703; -.
DR eggNOG; ENOG502QV1K; Eukaryota.
DR OrthoDB; 814925at2759; -.
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:0005243; F:gap junction 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 Gene3D; 1.20.1440.80; -; 1.
DR InterPro; IPR000500; Connexin.
DR InterPro; IPR002266; Connexin50.
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:SF19; PTHR11984:SF19; 1.
DR Pfam; PF00029; Connexin; 1.
DR Pfam; PF03509; Connexin50; 1.
DR PRINTS; PR00206; CONNEXIN.
DR PRINTS; PR01137; CONNEXINA8.
DR SMART; SM00037; CNX; 1.
DR SMART; SM01089; Connexin_CCC; 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; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2830542,
FT ECO:0000269|PubMed:30542154"
FT CHAIN 2..440
FT /note="Gap junction alpha-8 protein"
FT /id="PRO_0000057832"
FT INTRAMEM 2..12
FT /evidence="ECO:0000269|PubMed:30542154"
FT TOPO_DOM 13..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TOPO_DOM 43..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..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TOPO_DOM 183..210
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30542154"
FT TOPO_DOM 232..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:30542154"
FT REGION 108..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 54..201
FT /evidence="ECO:0000269|PubMed:30542154,
FT ECO:0007744|PDB:6MHY"
FT DISULFID 61..195
FT /evidence="ECO:0000269|PubMed:30542154,
FT ECO:0007744|PDB:6MHY"
FT DISULFID 65..190
FT /evidence="ECO:0000269|PubMed:30542154,
FT ECO:0007744|PDB:6MHY"
FT VARIANT 9
FT /note="N -> R"
FT VARIANT 10
FT /note="I -> L"
FT VARIANT 14
FT /note="V -> A"
FT CONFLICT 13
FT /note="E -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="N -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="E -> D (in Ref. 2; AAF01367)"
FT /evidence="ECO:0000305"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:7JJP"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:7JJP"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:7JJP"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:7JJP"
FT TURN 45..51
FT /evidence="ECO:0007829|PDB:7JJP"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:7JJP"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:7JJP"
FT HELIX 74..108
FT /evidence="ECO:0007829|PDB:7JJP"
FT HELIX 153..180
FT /evidence="ECO:0007829|PDB:7JJP"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:7JJP"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:7JLW"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:7JJP"
FT HELIX 206..235
FT /evidence="ECO:0007829|PDB:7JJP"
SQ SEQUENCE 440 AA; 49160 MW; BE6E478B98D83891 CRC64;
MGDWSFLGNI LEEVNEHSTV IGRVWLTVLF IFRILILGTA AEFVWGDEQS DFVCNTQQPG
CENVCYDEAF PISHIRLWVL QIIFVSTPSL VYVGHAVHHV RMEEKRKERE AEELSQQSPG
NGGERAPLAA DQGSVKKSSS SSKGTKKFRL EGTLLRTYVC HIIFKTLFEV GFIVGHYFLY
GFRILPLYRC SRWPCPNVVD CFVSRPTEKT IFILFMLSVA SVSLFLNILE MSHLGLKKIR
SAFKRPVEQP LGEIPEKSLH SIAVSSIQKA KGYQLLEEEK IVSHYFPLTE VGMVEASPLS
AKPFSQFEEK VGPGPLGDLS RAYQETLPSY AQVGAQEGVE EEQPIEAAAE PEVGDKSQEA
ERVSTEGEET LAVLEEEKVE PPEVEKEAEK EETPPEKVSK QELTPEKAPS LCAELPGEDT
RPLSRLSKAS SRARSDDLTV
