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KCNKD_RAT
ID   KCNKD_RAT               Reviewed;         405 AA.
AC   Q9ERS0;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Potassium channel subfamily K member 13;
DE   AltName: Full=Tandem pore domain halothane-inhibited potassium channel 1;
DE            Short=THIK-1;
GN   Name=Kcnk13;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=Wistar; TISSUE=Brain, and Heart;
RX   PubMed=11060316; DOI=10.1074/jbc.m008985200;
RA   Rajan S., Wischmeyer E., Karschin C., Preisig-Mueller R., Grzeschik K.-H.,
RA   Daut J., Karschin A., Derst C.;
RT   "THIK-1 and THIK-2, a novel subfamily of tandem pore domain K+ channels.";
RL   J. Biol. Chem. 276:7302-7311(2001).
CC   -!- FUNCTION: Potassium channel displaying weak inward rectification in
CC       symmetrical K(+) solution.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. In brain expression is rather low and
CC       restricted to the olfactory bulb and tubercle, to the ventromedial
CC       hypothalamic nucleus, lateral septal nucleus dorsal, lateral mammillary
CC       nucleus, lateral parabrachial nuclei, reticular nucleus and reunions
CC       nuclei.
CC   -!- MISCELLANEOUS: Weakly sensitive to low extracellular pH. Activated by
CC       arachidonic acid; inhibited by halothane and Ba++.
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; AF287301; AAG32312.1; -; mRNA.
DR   RefSeq; NP_071629.1; NM_022293.1.
DR   AlphaFoldDB; Q9ERS0; -.
DR   SMR; Q9ERS0; -.
DR   STRING; 10116.ENSRNOP00000067310; -.
DR   GlyGen; Q9ERS0; 2 sites.
DR   PaxDb; Q9ERS0; -.
DR   GeneID; 64120; -.
DR   KEGG; rno:64120; -.
DR   UCSC; RGD:68941; rat.
DR   CTD; 56659; -.
DR   RGD; 68941; Kcnk13.
DR   eggNOG; KOG4404; Eukaryota.
DR   InParanoid; Q9ERS0; -.
DR   OrthoDB; 645335at2759; -.
DR   PhylomeDB; Q9ERS0; -.
DR   Reactome; R-RNO-1299287; Tandem pore domain halothane-inhibited K+ channel (THIK).
DR   Reactome; R-RNO-5576886; Phase 4 - resting membrane potential.
DR   PRO; PR:Q9ERS0; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
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; IPR005410; 2pore_dom_K_chnl_THIK.
DR   InterPro; IPR013099; K_chnl_dom.
DR   PANTHER; PTHR11003; PTHR11003; 1.
DR   Pfam; PF07885; Ion_trans_2; 2.
DR   PRINTS; PR01333; 2POREKCHANEL.
DR   PRINTS; PR01588; THIKCHANNEL.
PE   1: Evidence at protein 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..405
FT                   /note="Potassium channel subfamily K member 13"
FT                   /id="PRO_0000101764"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        95..115
FT                   /note="Pore-forming; Name=Pore-forming 1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        146..193
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        224..244
FT                   /note="Pore-forming; Name=Pore-forming 2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        284..405
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   405 AA;  45081 MW;  441EB3EB2EC28C62 CRC64;
     MAGRGCSCSP GHLNEDNARF LLLAGLILLY LLGGAAVFSA LELAQELQAK QRWEERLANF
     SRGHNLSREE LRGFLRHYEE ATKAGIRMDS VRPRWDFTGA FYFVGTVVTT IGFGMTTPAT
     TGGKVFLIFY GLIGCASTIL FFNLFLERLI TVIAYVMRTC HHQQLRRRGT VARDNRKAPR
     KGEADSLAGW KPSVYYVMLI LCLASVAISC GASALYTTME GWSYFDSVYF CFVASSTIGF
     GDLVSSQNAQ YENEGLYRFV NFFFILMGVC CIYSMFNVIS ILIKQTVNWI LRKLDSGCFP
     QCQRGLLRSR RNVVMPGNIR NRCNISIETD GVMESDTDGR RLSGEMISMK DTNKVSLAIL
     QKQLSEMANG GPHQTSTSSR DDEFSGGVGA FAVMNNRLAE TSGDR
 
 
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