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Database: UniProt
Entry: A0A6Q2Y636_ESOLU
LinkDB: A0A6Q2Y636_ESOLU
Original site: A0A6Q2Y636_ESOLU 
ID   A0A6Q2Y636_ESOLU        Unreviewed;       440 AA.
AC   A0A6Q2Y636;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Gap junction protein {ECO:0000256|RuleBase:RU000630};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000061460.1, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000061460.1, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000061460.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A6Q2Y636; -.
DR   Ensembl; ENSELUT00000053066.1; ENSELUP00000061460.1; ENSELUG00000034173.1.
DR   GeneTree; ENSGT01050000244864; -.
DR   InParanoid; A0A6Q2Y636; -.
DR   OMA; NWTNLAV; -.
DR   Proteomes; UP000265140; LG16.
DR   Bgee; ENSELUG00000034173; Expressed in camera-type eye and 3 other cell types or tissues.
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; IPR034634; Connexin_C.
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:SF12; GAP JUNCTION ALPHA-3 PROTEIN; 1.
DR   Pfam; PF00029; Connexin; 1.
DR   PRINTS; PR00206; CONNEXIN.
DR   SMART; SM00037; CNX; 1.
DR   SMART; SM01089; Connexin_CCC; 1.
DR   SUPFAM; SSF118220; Connexin43; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000265140};
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        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        168..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        221..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          43..76
FT                   /note="Connexin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00037"
FT   DOMAIN          178..244
FT                   /note="Gap junction protein cysteine-rich"
FT                   /evidence="ECO:0000259|SMART:SM01089"
FT   REGION          129..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          99..126
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        267..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  47918 MW;  C0DEA6C44E216C2F CRC64;
     MGDWSFLGRL LENAQEHSTV IGKVWLTVLF IFRILVLGAA AEDVWGDEQS DFTCNTQQPG
     CENVCYDQAF PISHIRFWVL QIIFVSTPTL IYLGHVLHIV RMEEKRKEKE EELRKATRLQ
     EEKELLYNGG GDAGGGGGRG GRGGKKEKPP IRDEHGKIRI RGALLRTYVF NIIFKTLFEV
     GFILGQYFLY GFQLRPLYKC ERWPCPNTVD CFISRPTEKT IFIIFMLVVA CVSLLLNLLE
     IYHLGWKKVK QGMANPDHAL LPHSNGARPE SVTSASRTAP PNLSSPPTYT DVTAGSGAFL
     PPAAKSSTAE YKTDPTQEEP SSSYHGSGGG GGGGNHGLAA RQNWANLATE QQTREMKASS
     PSPSSDSERQ PGDAAAPLTP TTSVSPSSSG GSVSGENGGQ EEGQGTTTVE MHEPPVTDPR
     RLSRASKSSS LRARPGDLAV
//
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