ID A0A3Q4HX30_NEOBR Unreviewed; 391 AA.
AC A0A3Q4HX30;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Gap junction protein {ECO:0000256|RuleBase:RU000630};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000025748.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000025748.1}
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; A0A3Q4HX30; -.
DR STRING; 32507.ENSNBRP00000025748; -.
DR Ensembl; ENSNBRT00000026425.1; ENSNBRP00000025748.1; ENSNBRG00000019698.1.
DR GeneTree; ENSGT01090000260005; -.
DR OMA; EKGTAAC; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000019698; Expressed in blood and 5 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; 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:UP000261580};
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 176..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..255
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 187..253
FT /note="Gap junction protein cysteine-rich"
FT /evidence="ECO:0000259|SMART:SM01089"
FT REGION 127..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 44719 MW; 907E000CAF199FDC CRC64;
MSWSFLTRLL DEISNHSTFV GKVWLTVLII FRIVLTAVGG ETIYYDEQSK FVCNTQQPGC
ENVCYDAFAP LSHVRFWIFQ VIMITTPTIM YLGFAMHKIA RMEETDFRPG PKRKKRIPII
KRGAARDYEE VEDNGEEDPM IAEEIEPEKT DKAEQSRAAK KHDGRRRILR DGLMKVYVCQ
LLWRSAFEVA FLFGQYILYG FEVIPSYVCT RSPCPHTVDC FVSRPTEKTI FLLVMYVVSF
LCLLLTILEI IHLGIGSIRD TFRRRATLNT RTSRPPASRS MPTAPPGYHA TMKKEKMKEL
RDLPMGDSGR ESIGDEGPSS RELERLRRHL RLAQQHLDLA YQVDEGSPSR SSSPEVNTAA
QTAAEQNRLN FAQEKQGEAS EKAHMGMQSD H
//
