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KCNK7_MOUSE
ID   KCNK7_MOUSE             Reviewed;         307 AA.
AC   Q9Z2T1; Q9QXY0; Q9QYE8; Q9R1V1; Q9R242;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 3.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Potassium channel subfamily K member 7;
DE   AltName: Full=Double-pore K(+) channel 3;
DE   AltName: Full=Neuromuscular two p domain potassium channel;
DE   AltName: Full=Putative potassium channel DP3;
GN   Name=Kcnk7; Synonyms=Dpkch3, Kcnk6, Kcnk8, Knot1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain, and Lung;
RX   PubMed=10206991; DOI=10.1074/jbc.274.17.11751;
RA   Salinas M., Reyes R., Lesage F., Fosset M., Heurteaux C., Romey G.,
RA   Lazdunski M.;
RT   "Cloning of a new mouse two-P domain channel subunit and a human homologue
RT   with a unique pore structure.";
RL   J. Biol. Chem. 274:11751-11760(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ishibashi K., Suzuki M., Imai M.;
RT   "Cloning of a new double-pore K channel expressed predominantly in tesis.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 1-289.
RA   Bockenhauer D., Nimmakayalu M.A., Ward D.C., Goldstein S.A.N.,
RA   Gallagher P.G.;
RT   "Cloning, localization, and expression of the murine 2 P domain potassium
RT   channel KCNK6.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 2-307.
RA   Gan L., Joiner W.J., Quinn A.M., Wang L.-Y., Hughes T., Kaczmarek L.K.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 15-307.
RC   TISSUE=Brain;
RA   Lopes C.M.B., Buck M., Goldstein S.A.N.;
RT   "A new two P domain potassium channel subfamily from mouse excitable
RT   tissues.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable potassium channel subunit. No channel activity
CC       observed in vitro as protein remains in the endoplasmic reticulum. May
CC       need to associate with an as yet unknown partner in order to reach the
CC       plasma membrane.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Detected in embryo, eye, lung and liver. Weakly
CC       expressed in colon, testis, atria, kidney, intestine, bladder, uterus,
CC       ovary, salivary gland, thymus and brain stem. Not detected in brain,
CC       cerebellum, spinal cord, heart, ventricle, skeletal muscle, liver,
CC       placenta and pancreas. In the eye, highly expressed in the retinal
CC       ganglion cell layer and inner nuclear layer.
CC   -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC       1.A.1.8) family. {ECO:0000305}.
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DR   EMBL; AF110521; AAD29577.1; ALT_TERM; mRNA.
DR   EMBL; AB015729; BAA35074.1; -; mRNA.
DR   EMBL; AF158234; AAF14528.1; -; Genomic_DNA.
DR   EMBL; AF022820; AAD09337.1; -; mRNA.
DR   EMBL; AF012324; AAF21603.1; -; mRNA.
DR   RefSeq; NP_034739.2; NM_010609.3.
DR   AlphaFoldDB; Q9Z2T1; -.
DR   SMR; Q9Z2T1; -.
DR   STRING; 10090.ENSMUSP00000051278; -.
DR   GlyGen; Q9Z2T1; 1 site.
DR   PaxDb; Q9Z2T1; -.
DR   PRIDE; Q9Z2T1; -.
DR   DNASU; 16530; -.
DR   GeneID; 16530; -.
DR   KEGG; mmu:16530; -.
DR   CTD; 10089; -.
DR   MGI; MGI:1341841; Kcnk7.
DR   eggNOG; KOG1418; Eukaryota.
DR   InParanoid; Q9Z2T1; -.
DR   OrthoDB; 1211599at2759; -.
DR   Reactome; R-MMU-1299308; Tandem of pore domain in a weak inwardly rectifying K+ channels (TWIK).
DR   Reactome; R-MMU-5576886; Phase 4 - resting membrane potential.
DR   BioGRID-ORCS; 16530; 1 hit in 70 CRISPR screens.
DR   ChiTaRS; Kcnk6; mouse.
DR   PRO; PR:Q9Z2T1; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9Z2T1; protein.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR   GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR   GO; GO:0005267; F:potassium channel activity; ISS:MGI.
DR   GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR   InterPro; IPR003280; 2pore_dom_K_chnl.
DR   InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
DR   InterPro; IPR005408; 2pore_dom_K_chnl_TWIK.
DR   InterPro; IPR013099; K_chnl_dom.
DR   PANTHER; PTHR11003; PTHR11003; 1.
DR   Pfam; PF07885; Ion_trans_2; 2.
DR   PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
DR   PRINTS; PR01333; 2POREKCHANEL.
DR   PRINTS; PR01586; TWIKCHANNEL.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..307
FT                   /note="Potassium channel subfamily K member 7"
FT                   /id="PRO_0000101752"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        92..118
FT                   /note="Pore-forming; Name=Pore-forming 1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        141..172
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        199..227
FT                   /note="Pore-forming; Name=Pore-forming 2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..307
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        1..3
FT                   /note="MGS -> MTHSREFGPRGQEFGTR (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2..3
FT                   /note="GS -> TR (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="S -> G (in Ref. 1; AAD29577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231..232
FT                   /note="YH -> SP (in Ref. 2; BAA35074)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293
FT                   /note="T -> P (in Ref. 2; BAA35074)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   307 AA;  32199 MW;  83EC6BB7E4C6BD9B CRC64;
     MGSLKPWARY LLLLMAHLLA MGLGAVVLQA LEGPPARHLQ AQVQAELASF QAEHRACLPP
     EALEELLGAV LRAQAHGVSS LGNSSETSNW DLPSALLFTA SILTTTGYGH MAPLSSGGKA
     FCVVYAALGL PASLALVAAL RHCLLPVFSR PGDWVAIRWQ LAPAQAALLQ AAGLGLLVAC
     VFMLLPALVL WGVQGDCSLL EAIYFCFGSL STIGLGDLLP AHGRGLHPAI YHLGQFALLG
     YLLLGLLAML LAVETFSELP QVRAMVKFFG PSGSRTDEDQ DGILGQDELA LSTVLPDAPV
     LGPTTPA
 
 
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