CXA10_MOUSE
ID CXA10_MOUSE Reviewed; 505 AA.
AC Q9WUS4; A2ANV0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Gap junction alpha-10 protein;
DE AltName: Full=Connexin-57;
DE Short=Cx57;
GN Name=Gja10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10329667; DOI=10.1074/jbc.274.21.14716;
RA Manthey D., Bukauskas F., Kozak C., Willecke K., Lee C.G.;
RT "Molecular cloning and functional expression of the mouse gap junction gene
RT connexin-57 in human HeLa cells.";
RL J. Biol. Chem. 274:14716-14723(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 478-505 (ISOFORM 2), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15147297; DOI=10.1111/j.0953-816x.2004.03360.x;
RA Hombach S., Janssen-Bienhold U., Soehl G., Schubert T., Buessow H., Ott T.,
RA Weiler R., Willecke K.;
RT "Functional expression of connexin57 in horizontal cells of the mouse
RT retina.";
RL Eur. J. Neurosci. 19:2633-2640(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12881038; DOI=10.1080/15419060302063;
RA Soehl G., Nielsen P.A., Eiberger J., Willecke K.;
RT "Expression profiles of the novel human connexin genes hCx30.2, hCx40.1,
RT and hCx62 differ from their putative mouse orthologues.";
RL Cell Commun. Adhes. 10:27-36(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16820008; DOI=10.1111/j.1460-9568.2006.04848.x;
RA Shelley J., Dedek K., Schubert T., Feigenspan A., Schultz K., Hombach S.,
RA Willecke K., Weiler R.;
RT "Horizontal cell receptive fields are reduced in connexin57-deficient
RT mice.";
RL Eur. J. Neurosci. 23:3176-3186(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17681699; DOI=10.1016/j.neuroscience.2007.06.003;
RA Ciolofan C., Lynn B.D., Wellershaus K., Willecke K., Nagy J.I.;
RT "Spatial relationships of connexin36, connexin57 and zonula occludens-1 in
RT the outer plexiform layer of mouse retina.";
RL Neuroscience 148:473-488(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18320035; DOI=10.1371/journal.pone.0001714;
RA Dedek K., Pandarinath C., Alam N.M., Wellershaus K., Schubert T.,
RA Willecke K., Prusky G.T., Weiler R., Nirenberg S.;
RT "Ganglion cell adaptability: does the coupling of horizontal cells play a
RT role?";
RL PLoS ONE 3:E1714-E1714(2008).
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. Involved in
CC tracer coupling between horizontal cells of the retina. May play a role
CC in the regulation of horizontal cell patterning.
CC {ECO:0000269|PubMed:15147297, ECO:0000269|PubMed:16820008,
CC ECO:0000269|PubMed:17681699, ECO:0000269|PubMed:18320035}.
CC -!- SUBUNIT: A connexon is composed of a hexamer of connexins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17681699};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17681699}. Cell
CC junction, gap junction {ECO:0000269|PubMed:17681699}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WUS4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WUS4-2; Sequence=VSP_035809;
CC -!- TISSUE SPECIFICITY: Low levels were detected in skin, heart, kidney,
CC testis, ovary, intestine. Expression not detected in brain, sciatic
CC nerve or liver. According to PubMed:15147297 expression is detected
CC only in horizontal cells in the inner nuclear layer of the retina and
CC not in other neurons of the central nervous system or tissues. Detected
CC in the outer plexiform layer of the retina (at protein level).
CC {ECO:0000269|PubMed:12881038, ECO:0000269|PubMed:15147297,
CC ECO:0000269|PubMed:17681699}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the retina from 16.5 dpc to P1, in
CC the thymus from 18.5 dpc to P1, and in kidney from 16.5 dpc to 18.5
CC dpc. {ECO:0000269|PubMed:15147297}.
CC -!- DISRUPTION PHENOTYPE: Mice are fertile and show no obvious anatomical
CC or behavioral abnormalities. In horizontal cells of the retina tracer
CC coupling is abolished but the spatial tuning of ganglion cells is
CC unchanged. {ECO:0000269|PubMed:15147297, ECO:0000269|PubMed:16820008,
CC ECO:0000269|PubMed:18320035}.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ010741; CAB40358.1; -; Genomic_DNA.
DR EMBL; AL831746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18015.1; -. [Q9WUS4-1]
DR RefSeq; NP_034419.2; NM_010289.2. [Q9WUS4-1]
DR AlphaFoldDB; Q9WUS4; -.
DR SMR; Q9WUS4; -.
DR STRING; 10090.ENSMUSP00000061742; -.
DR PaxDb; Q9WUS4; -.
DR PRIDE; Q9WUS4; -.
DR Antibodypedia; 56329; 54 antibodies from 12 providers.
DR DNASU; 14610; -.
DR Ensembl; ENSMUST00000056517; ENSMUSP00000061742; ENSMUSG00000051056. [Q9WUS4-1]
DR Ensembl; ENSMUST00000219644; ENSMUSP00000151323; ENSMUSG00000051056. [Q9WUS4-2]
DR GeneID; 14610; -.
DR KEGG; mmu:14610; -.
DR UCSC; uc008sev.1; mouse. [Q9WUS4-1]
DR CTD; 84694; -.
DR MGI; MGI:1339969; Gja10.
DR VEuPathDB; HostDB:ENSMUSG00000051056; -.
DR eggNOG; ENOG502QQPH; Eukaryota.
DR GeneTree; ENSGT01050000244914; -.
DR HOGENOM; CLU_037388_1_0_1; -.
DR InParanoid; Q9WUS4; -.
DR OMA; WEQSQDL; -.
DR OrthoDB; 714519at2759; -.
DR PhylomeDB; Q9WUS4; -.
DR TreeFam; TF329606; -.
DR Reactome; R-MMU-112303; Electric Transmission Across Gap Junctions.
DR Reactome; R-MMU-190861; Gap junction assembly.
DR BioGRID-ORCS; 14610; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9WUS4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9WUS4; protein.
DR Bgee; ENSMUSG00000051056; Expressed in animal zygote and 13 other tissues.
DR ExpressionAtlas; Q9WUS4; baseline and differential.
DR Genevisible; Q9WUS4; MM.
DR GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR GO; GO:0005921; C:gap junction; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005243; F:gap junction channel activity; IDA:MGI.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:MGI.
DR GO; GO:0007276; P:gamete generation; IDA:MGI.
DR GO; GO:0009416; P:response to light stimulus; IMP:MGI.
DR GO; GO:0007416; P:synapse assembly; IMP:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Gap junction; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..505
FT /note="Gap junction alpha-10 protein"
FT /id="PRO_0000057841"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..76
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 371..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 481..505
FT /note="VSKSSHVDSPPHSSFIIHETYVYVY -> NMLLELSSIMKK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15147297"
FT /id="VSP_035809"
FT CONFLICT 143
FT /note="R -> K (in Ref. 1; CAB40358)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="I -> V (in Ref. 1; CAB40358)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="A -> T (in Ref. 1; CAB40358)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 57127 MW; F7FAFBA21EDE2A7B CRC64;
MGDWNLLGGI LEEVHSHSTI VGKIWLTILF IFRMLVLGVA AEDVWDDEQS AFACNTQQPG
CNNICYDDAF PISLIRFWVL QIIFVSSPSL VYMGHALYRL RDFEKQRQKK KLYLRAQMEN
PELDLEEQQR VDKELRRLEE QKRIHKVPLK GCLLRTYVLH ILTRSVLEVG FMIGQYILYG
FQMHPIYKCT QAPCPNSVDC FVSRPTEKTI FMLFMHSIAA ISLLLNILEI FHLGIRKIMR
ALDGKSSSGN TENETGPPFH STNYSGTQQC MICSSLPERI SLLQANNKQQ VIRVNIPRSK
SMWQIPHPRQ LEVDVSCGKR DWAEKIESCA QLHVHSPCPH DRSARIQHPG QQPCHSVFGP
KNAMSQSWFG TMTASQHRPS SALETWERSQ GPEASGRSLT DRQSHFQGSD GSARESGVWT
DRLGPGSRKA SFLSRLMSEK GQRHSDSGSS RSLNSSCLDF SHGENSPSPL PSATGHRASM
VSKSSHVDSP PHSSFIIHET YVYVY
