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CXG1_CANLF
ID   CXG1_CANLF              Reviewed;         396 AA.
AC   P28228; Q5J7U4;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 124.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1310450; DOI=10.1161/01.res.70.2.438;
RA   Kanter H.L., Saffitz J.E., Beyer E.C.;
RT   "Cardiac myocytes express multiple gap junction proteins.";
RL   Circ. Res. 70:438-444(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Werner P., Raducha M.G., Prociuk U., Ostrander E.A., Spielman R.S.,
RA   Kirkness E.F., Henthorn P.S., Patterson D.F.;
RT   "Genome-wide scan for conotruncal heart defect loci in a canine model.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: A connexon is composed of a hexamer of connexins. Interacts
CC       with CNST (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC       junction, gap junction.
CC   -!- SIMILARITY: Belongs to the connexin family. Gamma-type subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M81348; AAA30839.1; -; Genomic_DNA.
DR   EMBL; AY438630; AAR99071.1; -; Genomic_DNA.
DR   PIR; B49024; B49024.
DR   RefSeq; NP_001018648.1; NM_001020812.2.
DR   RefSeq; XP_005624400.1; XM_005624343.2.
DR   RefSeq; XP_005624401.1; XM_005624344.2.
DR   AlphaFoldDB; P28228; -.
DR   SMR; P28228; -.
DR   STRING; 9615.ENSCAFP00000020776; -.
DR   PaxDb; P28228; -.
DR   PRIDE; P28228; -.
DR   GeneID; 490936; -.
DR   KEGG; cfa:490936; -.
DR   CTD; 10052; -.
DR   eggNOG; ENOG502QV2G; Eukaryota.
DR   InParanoid; P28228; -.
DR   OrthoDB; 692491at2759; -.
DR   TreeFam; TF329606; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005922; C:connexin complex; IDA:BHF-UCL.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005243; F:gap junction channel activity; IBA:GO_Central.
DR   GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
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   3: Inferred from homology;
KW   Cell junction; Cell membrane; Gap junction; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..396
FT                   /note="Gap junction gamma-1 protein"
FT                   /id="PRO_0000057825"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        23..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..75
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        96..175
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        199..228
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        249..396
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          145..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        30
FT                   /note="A -> V (in Ref. 2; AAR99071)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34
FT                   /note="A -> V (in Ref. 2; AAR99071)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        345
FT                   /note="V -> A (in Ref. 2; AAR99071)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392
FT                   /note="N -> T (in Ref. 2; AAR99071)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   396 AA;  45533 MW;  E72AB416178ED3CE CRC64;
     MSWSFLTRLL EEIHNHSTFV GKIWLTVLIA FRIALTAVGG ESIYYDEQSK FVCNTEQPGC
     ENVCYDAFAP LSHVRFWVFQ IILVATPSVM YLGYAIHKIA KMEHGEADKK AARSKPYAMR
     WKQHRALEET EEDHEEDPMM YPEMELESEK ENKEQNQPKP KHDGRRRIRE DGLMKIYVLQ
     LLARTVFEVG FLIGQYFLYG FQVHPFYVCS RLPCPHKIDC FISRPTEKTI FLLIMYGVTG
     LCLLLNIWEM LHLGFGTIRD SLNSKRRELE DPGAYNYPFT WNTPSAPPGY NIAVKPDQIQ
     YTELSNAKIA YKQNKANIAQ EQQYGSHEEN LPADLETLQR EIKMVQERLD LAIQAYSHQN
     NPHGPREKKA KVGSKAGSNK SSASSKSGDG KNSVWI
 
 
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