CX32_DANRE
ID CX32_DANRE Reviewed; 277 AA.
AC Q7T047; Q0P3V1; Q5TYN7;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Gap junction Cx32.2 protein;
DE AltName: Full=Connexin-32.2;
GN Name=cx32.2 {ECO:0000312|ZFIN:ZDB-GENE-050303-1};
GN Synonyms=gjae {ECO:0000312|EMBL:CAH69064.1};
GN ORFNames=si:dkey-261a18.5, zgc:153825;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000312|EMBL:AAQ17184.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15895415; DOI=10.1002/dvdy.20426;
RA Chatterjee B., Chin A.J., Valdimarsson G., Finis C., Sonntag J.M.,
RA Choi B.Y., Tao L., Balasubramanian K., Bell C., Krufka A., Kozlowski D.J.,
RA Johnson R.G., Lo C.W.;
RT "Developmental regulation and expression of the zebrafish connexin43
RT gene.";
RL Dev. Dyn. 233:890-906(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAH69064.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=WIK;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000305}.
CC -!- SUBUNIT: A connexon is composed of a hexamer of connexins.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC junction, gap junction.
CC -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC subfamily. {ECO:0000255}.
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DR EMBL; AY340236; AAQ17184.1; -; Genomic_DNA.
DR EMBL; CR352322; CAH69064.1; -; Genomic_DNA.
DR EMBL; BC122427; AAI22428.1; -; mRNA.
DR RefSeq; NP_001025381.2; NM_001030210.2.
DR AlphaFoldDB; Q7T047; -.
DR SMR; Q7T047; -.
DR STRING; 7955.ENSDARP00000091787; -.
DR PaxDb; Q7T047; -.
DR Ensembl; ENSDART00000101014; ENSDARP00000091787; ENSDARG00000076789.
DR Ensembl; ENSDART00000181279; ENSDARP00000151259; ENSDARG00000076789.
DR GeneID; 566647; -.
DR KEGG; dre:566647; -.
DR CTD; 566647; -.
DR ZFIN; ZDB-GENE-050303-1; gja13.2.
DR eggNOG; ENOG502QT6R; Eukaryota.
DR GeneTree; ENSGT01050000244864; -.
DR HOGENOM; CLU_037388_4_1_1; -.
DR InParanoid; Q7T047; -.
DR OMA; GAECFMS; -.
DR OrthoDB; 938208at2759; -.
DR PhylomeDB; Q7T047; -.
DR TreeFam; TF329606; -.
DR PRO; PR:Q7T047; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000076789; Expressed in spleen and 15 other tissues.
DR GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005243; F:gap junction channel activity; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
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 2: Evidence at transcript 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"
FT CHAIN 2..277
FT /note="Gap junction Cx32.2 protein"
FT /id="PRO_0000057876"
FT TOPO_DOM 2..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..76
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DISULFID 54..175
FT /evidence="ECO:0000250"
FT DISULFID 170..180
FT /evidence="ECO:0000250"
FT CONFLICT 231
FT /note="N -> D (in Ref. 1; AAQ17184)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 31885 MW; 13B84F85FAC1245E CRC64;
MGDWGFLSAL LDKVQSHSTV IGKIWMSVLF IFRILVLGAG AENVWGDERS NLVCNTNTPG
CDNLCYDWQF PISHIRFWVM QIIFISTPTL VYLGHVVHII HQENKQRELL KSNPMAKSPK
YTDENGKVEI KGSMLGSYLT QLFIKIILEV AFIVGQYYLF GFIIDHKFIC ERSPCMRAEC
FVSRPTEKSI FIIFMLVVAC VSLALNVLEI FYLLCRRISR RSKKCRQAMY NGESRYPGHF
TTELESMNGM RHNEFNVAFQ NKWSQRKGSL DAAKPEA
