ID A0A1S3FHM0_DIPOR Unreviewed; 333 AA.
AC A0A1S3FHM0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Gap junction protein {ECO:0000256|RuleBase:RU000630};
GN Name=Gja4 {ECO:0000313|RefSeq:XP_012876001.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012876001.1};
RN [1] {ECO:0000313|RefSeq:XP_012876001.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012876001.1};
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|ARBA:ARBA00003922, ECO:0000256|RuleBase:RU000630}.
CC -!- SUBUNIT: A connexon is composed of a hexamer of connexins.
CC {ECO:0000256|ARBA:ARBA00011455, 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_012876001.1; XM_013020547.1.
DR AlphaFoldDB; A0A1S3FHM0; -.
DR STRING; 10020.ENSDORP00000015325; -.
DR GeneID; 105988813; -.
DR KEGG; dord:105988813; -.
DR CTD; 2701; -.
DR InParanoid; A0A1S3FHM0; -.
DR OMA; FHLCCKN; -.
DR OrthoDB; 5301774at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005922; C:connexin complex; IEA:InterPro.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
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; IPR002263; Connexin37.
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:SF54; GAP JUNCTION ALPHA-4 PROTEIN; 1.
DR Pfam; PF00029; Connexin; 1.
DR PRINTS; PR00206; CONNEXIN.
DR PRINTS; PR01134; CONNEXINA4.
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:UP000081671};
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..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..232
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 165..231
FT /note="Gap junction protein cysteine-rich"
FT /evidence="ECO:0000259|SMART:SM01089"
FT REGION 305..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 333 AA; 37884 MW; DE1E21D935875FBA CRC64;
MGDWSLLEKL LDQVQEHSTV VGKIWLTVLF IFRILILGLA GESVWGDERS DFECNTIQPG
CTNVCYDQAF PISHIRYWVL QFLFVSTPTL IYLGHVLYLS RLEEKLRQKE GELRALPSKD
PHVDRALASI ERQIAKISVR EDGRLRIRGA LMGSYMVSVV CKSVFEAGFL YGQWCLYGWI
MQPLYVCHRV PCPHSVDCYV SRPTEKTIFI IFMLVMGLIS LVLNLLELVH LLRHYIRRGL
RLWHSKEEPT AQDPSSHPYP DQVFFYLPMG EGPSSPPCPT YNGLSSTEQN WANLTTEERL
ASSKAPLFLD PPPQCMGKSP SGPSGSISKM QYV
//
