ID A0A2U3XMB8_LEPWE Unreviewed; 273 AA.
AC A0A2U3XMB8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Gap junction protein {ECO:0000256|RuleBase:RU000630};
GN Name=GJB5 {ECO:0000313|RefSeq:XP_006732630.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006732630.1};
RN [1] {ECO:0000313|RefSeq:XP_006732630.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006732630.1};
RG RefSeq;
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 RefSeq; XP_006732630.1; XM_006732567.2.
DR AlphaFoldDB; A0A2U3XMB8; -.
DR STRING; 9713.A0A2U3XMB8; -.
DR GeneID; 102728308; -.
DR KEGG; lww:102728308; -.
DR CTD; 2709; -.
DR OrthoDB; 5301774at2759; -.
DR Proteomes; UP000245341; Unplaced.
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; IPR002271; Connexin311.
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:SF29; GAP JUNCTION BETA-5 PROTEIN; 1.
DR Pfam; PF00029; Connexin; 1.
DR PRINTS; PR00206; CONNEXIN.
DR PRINTS; PR01141; CONNEXINB4.
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:UP000245341};
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..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..203
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 141..208
FT /note="Gap junction protein cysteine-rich"
FT /evidence="ECO:0000259|SMART:SM01089"
SQ SEQUENCE 273 AA; 30852 MW; 7197B0665C5DFAA3 CRC64;
MNWGIFEGLL SGVNKYSTAF GRIWLSLVFI FRMLVYLVTA ERVWSDDHKD FDCNTKQPGC
SNVCFDEFFP VSHVRLWALQ LILVTCPSLL VVMHVAYREA REKKHREVVG EDGGRLYPNP
SKKRGGLWWT YVCSLVFKAG VDTAFLYVFH SFYPKYTLPH VVKCHIAPCP NMVDCFISKP
SEKNIFTLFM VVTAAICILL NLIELTYLVS KRCHEGLAAR RARATGVGHC PAWATSPCKG
DDLLAGDLIF LGSDSHPPLL PDLPRDHVKK TIL
//