ID H3C889_TETNG Unreviewed; 385 AA.
AC H3C889;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Gap junction protein {ECO:0000256|RuleBase:RU000630};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000004461.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000004461.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|RuleBase:RU000630}.
CC -!- SUBUNIT: A connexon is composed of a hexamer of connexins.
CC {ECO:0000256|RuleBase:RU000630}.
CC -!- SUBCELLULAR LOCATION: Cell junction, gap junction
CC {ECO:0000256|ARBA:ARBA00004610}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU000630}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the connexin family.
CC {ECO:0000256|RuleBase:RU000630}.
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DR AlphaFoldDB; H3C889; -.
DR STRING; 99883.ENSTNIP00000004461; -.
DR Ensembl; ENSTNIT00000004602.1; ENSTNIP00000004461.1; ENSTNIG00000002041.1.
DR GeneTree; ENSGT01090000260005; -.
DR HOGENOM; CLU_037388_4_0_1; -.
DR InParanoid; H3C889; -.
DR OMA; EKGTAAC; -.
DR TreeFam; TF329606; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR Gene3D; 1.20.1440.80; Gap junction channel protein cysteine-rich domain; 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; CONNEXIN; 1.
DR PANTHER; PTHR11984:SF117; GAP JUNCTION PROTEIN; 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 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Gap junction {ECO:0000256|ARBA:ARBA00022868,
KW ECO:0000256|RuleBase:RU000630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000630};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..75
FT /note="Connexin N-terminal"
FT /evidence="ECO:0000259|SMART:SM00037"
FT DOMAIN 185..251
FT /note="Gap junction protein cysteine-rich"
FT /evidence="ECO:0000259|SMART:SM01089"
FT REGION 142..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 385 AA; 44102 MW; 818EC0BFA77AC757 CRC64;
MSWSFLTRLL DEISNHSTFV GKIWLTILII FRIVLTAVGG ETIYYDEQSK FVCNTQQPGC
ENVCYDAFAP LSHVRFWIFQ VILITTPTIM YLGFAMHKIA RMNDSEYRVV RKAKKKMPIV
NRGPRDYEEA EDNGEEDPMI AEEIEQEKPD KAEKGPEKKH DGRRRIQRDG LMKVYVCQLL
WRSSFEVAFL FGQYVLYGFE VHASYVCTRS PCPHTVDCFV SRPTEKTIFL LVMYVVSFLC
LLLTLFEMLH LGIGGVRDTF RRASALNQRA PRLTAPRSIA TAPPGYHATM KKEKLKGRLR
DSPMGDSGRE SFGDEGPSSR ELERLRRHLK LAQQHLDQAY QVEDRSPSRS SSPEVNTAAQ
TAAEQNRLNF AQEKQGEPSE KGKEM
//
