ID A0A091GUV1_BUCRH Unreviewed; 412 AA.
AC A0A091GUV1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE RecName: Full=Gap junction protein {ECO:0000256|RuleBase:RU000630};
GN ORFNames=N320_06405 {ECO:0000313|EMBL:KFO86190.1};
OS Buceros rhinoceros silvestris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO86190.1, ECO:0000313|Proteomes:UP000054064};
RN [1] {ECO:0000313|EMBL:KFO86190.1, ECO:0000313|Proteomes:UP000054064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO86190.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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.
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 EMBL; KL510225; KFO86190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GUV1; -.
DR Proteomes; UP000054064; 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:SF52; GAP JUNCTION GAMMA-2 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:UP000054064};
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..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..256
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 188..254
FT /note="Gap junction protein cysteine-rich"
FT /evidence="ECO:0000259|SMART:SM01089"
FT REGION 145..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 46856 MW; E9DB99A3F932DD99 CRC64;
MSWSFLTRLL EEIHNHSTFV GKVWLTVLIV FRIVLTAVGG ESIYSDEQSK FTCNTKQPGC
DNVCYDAFAP LSHVRFWVFQ IIMISTPSVM YLGYAIHRIA RSAEEEKKFK GFKKKKQFAL
NWQAVRNMED PMEADEEEPM ISDDAAEHEK AKAKPKSKEP QKHDGRRRIQ QEGLMKIYVF
QLLTRASFEV CFLIGQYLLY GFEVEAYYVC NRVPCPHTVD CFVSRPTEKT IFLLVMYVVS
CLCLLLNMCE MFHLGFGTIR DAIRNRKINS FRQPPYNYAY PKNISCPPEY NLVVKSEKPT
KIPNSLMAHE QNLANVAQEQ QCTSPDENLP ADLSTLHKHL RVAQEQLDIA FQSYSSTQGN
TQPSRTSSPA SGGTVVEQNR ANTAQEKQGA KPKACLEKGS SSSKDGKTSV WI
//
