CXG1_CRIGR
ID CXG1_CRIGR Reviewed; 396 AA.
AC Q6R4A8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Gap junction gamma-1 protein;
DE AltName: Full=Connexin-45;
DE Short=Cx45;
DE AltName: Full=Gap junction alpha-7 protein;
GN Name=GJC1; Synonyms=GJA7;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=16194882; DOI=10.1080/15419060500242877;
RA Cruciani V., Heintz K.-M., Husoey T., Hovig E., Warren D.J.,
RA Mikalsen S.-O.;
RT "The detection of hamster connexins: a comparison of expression profiles
RT with wild-type mouse and the cancer-prone min mouse.";
RL Cell Commun. Adhes. 11:155-171(2004).
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. {ECO:0000250}.
CC -!- SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts
CC with CNST (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the connexin family. Gamma-type subfamily.
CC {ECO:0000305}.
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DR EMBL; AY514680; AAR98617.1; -; mRNA.
DR RefSeq; NP_001233715.1; NM_001246786.1.
DR RefSeq; XP_007643222.1; XM_007645032.1.
DR RefSeq; XP_007643223.1; XM_007645033.1.
DR RefSeq; XP_007643224.1; XM_007645034.1.
DR AlphaFoldDB; Q6R4A8; -.
DR BMRB; Q6R4A8; -.
DR SMR; Q6R4A8; -.
DR STRING; 10029.NP_001233715.1; -.
DR Ensembl; ENSCGRT00001010196; ENSCGRP00001006483; ENSCGRG00001008773.
DR GeneID; 100689357; -.
DR KEGG; cge:100689357; -.
DR CTD; 10052; -.
DR eggNOG; ENOG502QV2G; Eukaryota.
DR GeneTree; ENSGT01050000244833; -.
DR OMA; VRWKQHR; -.
DR OrthoDB; 692491at2759; -.
DR GO; GO:0005922; C:connexin complex; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0086077; F:gap junction channel activity involved in AV node cell-bundle of His cell electrical coupling; IEA:Ensembl.
DR GO; GO:0005216; F:ion channel activity; IEA:Ensembl.
DR GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
DR GO; GO:0048468; P:cell development; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0016264; P:gap junction assembly; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR Gene3D; 1.20.1440.80; -; 1.
DR InterPro; IPR000500; Connexin.
DR InterPro; IPR002265; Connexin45.
DR InterPro; IPR019570; Connexin_CCC.
DR InterPro; IPR017990; Connexin_CS.
DR InterPro; IPR013092; Connexin_N.
DR InterPro; IPR038359; Connexin_N_sf.
DR PANTHER; PTHR11984; PTHR11984; 1.
DR Pfam; PF00029; Connexin; 1.
DR PRINTS; PR00206; CONNEXIN.
DR PRINTS; PR01136; CONNEXINA6.
DR SMART; SM00037; CNX; 1.
DR SMART; SM01089; Connexin_CCC; 1.
DR PROSITE; PS00407; CONNEXINS_1; 1.
DR PROSITE; PS00408; CONNEXINS_2; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Coiled coil; Gap junction; Membrane;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..396
FT /note="Gap junction gamma-1 protein"
FT /id="PRO_0000369541"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 145..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 303..358
FT /evidence="ECO:0000255"
FT COMPBIAS 375..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 45666 MW; 9CD5721BB071B65C CRC64;
MSWSFLTRLL EEIHNHSTFV GKIWLTVLIV FRIVLTAVGG ESIYYDEQSK FVCNTEQPGC
ENVCYDAFAP LSHVRFWVFQ IILVATPSVM YLGYAIHKIA KMEHGEADKK AARSKPYAMR
WKQHRALEET EEDHEEDPMM YPEMELESEK ENKEQSQPKP KHDGRRRIRE DGLMKIYVLQ
LLARTVFEVG FLIGQYFLYG FQVHPFYVCS RLPCPHKIDC FISRPTEKTI FLLIMYGVTG
LCLLLNIWEM LHLGFGTIRD SLNSKRRELD DPGAYNYPFT WNTPSAPPGY NIAVKPDQIQ
YTELSNAKIA YKQNKANIAQ EQQYGSHEEH LPADLETLQR EIRMAQERLD LAIQAYHHQN
NPHGPREKKA KVGSKSGSNK SSISSKSGDG KTSVWI