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Database: UniProt
Entry: G1P848_MYOLU
LinkDB: G1P848_MYOLU
Original site: G1P848_MYOLU 
ID   G1P848_MYOLU            Unreviewed;       426 AA.
AC   G1P848;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Gap junction protein {ECO:0000256|RuleBase:RU000630};
GN   Name=GJC2 {ECO:0000313|Ensembl:ENSMLUP00000006327.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000006327.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000006327.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000006327.2}
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   EMBL; AAPE02040269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02040270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1P848; -.
DR   STRING; 59463.ENSMLUP00000006327; -.
DR   Ensembl; ENSMLUT00000006923.2; ENSMLUP00000006327.2; ENSMLUG00000006940.2.
DR   eggNOG; ENOG502QV2G; Eukaryota.
DR   GeneTree; ENSGT01090000260005; -.
DR   HOGENOM; CLU_037388_0_0_1; -.
DR   InParanoid; G1P848; -.
DR   OMA; ACTKGAG; -.
DR   TreeFam; TF329606; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:1903763; F:gap junction channel activity involved in cell communication by electrical coupling; IEA:Ensembl.
DR   GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
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:UP000001074};
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..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        207..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        263..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          45..78
FT                   /note="Connexin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00037"
FT   DOMAIN          218..283
FT                   /note="Gap junction protein cysteine-rich"
FT                   /evidence="ECO:0000259|SMART:SM01089"
FT   REGION          108..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..134
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..312
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  46107 MW;  CB33AE9E51BCDE83 CRC64;
     MTNMSWSFLT RLLEEIHHHS TFVGKVWLTV LVVFRIVLTA VGGESIYSDE QTKFTCNTRQ
     PGCDNVCYDA FAPLSHVRFW VFQIVVISTP SVMYLGYAVH RLARAAKHER RRAPRRKRGP
     RAPLPLPPSS HPTWPEPIDL GEEEPMLSLG EEEEEPGVAE GLGAEDEVED ASAAKGLGAD
     AKAAGTPSPN GPHDGRRRIQ REGLMRVYVA QLVARAAFEV AFLVGQYLLY GFEVPPFFPC
     SRRPCPHVVD CFVSRPTEKT FLLVMYVISC LCLLLNLCEM AHLGLGQRQG RRARPSPCAS
     PGPAPRPLPC PLPPAPAVLS TARLQPFLPP DYSLVLRERA HDQDLPSPAL RTLRDARALG
     DRDHPPCSGL PAATRGPPRA GASASGSGSA TSGGTGGDQG RPGAKPRAGS EKGSASSREG
     KATVWI
//
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