KCNKD_HUMAN
ID KCNKD_HUMAN Reviewed; 408 AA.
AC Q9HB14; B5TJL8; Q96E79;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 168.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=18516069; DOI=10.1038/bjp.2008.213;
RA Gierten J., Ficker E., Bloehs R., Schlomer K., Kathofer S., Scholz E.,
RA Zitron E., Kiesecker C., Bauer A., Becker R., Katus H.A., Karle C.A.,
RA Thomas D.;
RT "Regulation of two-pore-domain (K2P) potassium leak channels by the
RT tyrosine kinase inhibitor genistein.";
RL Br. J. Pharmacol. 154:1680-1690(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Potassium channel displaying weak inward rectification in
CC symmetrical K(+) solution. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: The current is enhanced by arachidonic acid and
CC inhibited by halothane. {ECO:0000250}.
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; AF287303; AAG32314.1; -; mRNA.
DR EMBL; EU978942; ACH86101.1; -; mRNA.
DR EMBL; CH471061; EAW81417.1; -; Genomic_DNA.
DR EMBL; BC012779; AAH12779.1; -; mRNA.
DR CCDS; CCDS9889.1; -.
DR RefSeq; NP_071337.2; NM_022054.3.
DR AlphaFoldDB; Q9HB14; -.
DR SMR; Q9HB14; -.
DR BioGRID; 121171; 1.
DR STRING; 9606.ENSP00000282146; -.
DR ChEMBL; CHEMBL4523461; -.
DR GlyGen; Q9HB14; 2 sites.
DR iPTMnet; Q9HB14; -.
DR PhosphoSitePlus; Q9HB14; -.
DR BioMuta; KCNK13; -.
DR DMDM; 24636284; -.
DR EPD; Q9HB14; -.
DR jPOST; Q9HB14; -.
DR MassIVE; Q9HB14; -.
DR MaxQB; Q9HB14; -.
DR PaxDb; Q9HB14; -.
DR PeptideAtlas; Q9HB14; -.
DR PRIDE; Q9HB14; -.
DR ProteomicsDB; 81470; -.
DR Antibodypedia; 13480; 130 antibodies from 26 providers.
DR DNASU; 56659; -.
DR Ensembl; ENST00000282146.5; ENSP00000282146.4; ENSG00000152315.5.
DR GeneID; 56659; -.
DR KEGG; hsa:56659; -.
DR MANE-Select; ENST00000282146.5; ENSP00000282146.4; NM_022054.4; NP_071337.2.
DR UCSC; uc001xye.2; human.
DR CTD; 56659; -.
DR DisGeNET; 56659; -.
DR GeneCards; KCNK13; -.
DR HGNC; HGNC:6275; KCNK13.
DR HPA; ENSG00000152315; Tissue enhanced (choroid plexus, parathyroid gland, testis).
DR MIM; 607367; gene.
DR neXtProt; NX_Q9HB14; -.
DR OpenTargets; ENSG00000152315; -.
DR PharmGKB; PA30055; -.
DR VEuPathDB; HostDB:ENSG00000152315; -.
DR eggNOG; KOG4404; Eukaryota.
DR GeneTree; ENSGT00940000157960; -.
DR HOGENOM; CLU_022504_3_1_1; -.
DR InParanoid; Q9HB14; -.
DR OMA; MKSCHER; -.
DR OrthoDB; 645335at2759; -.
DR PhylomeDB; Q9HB14; -.
DR TreeFam; TF313947; -.
DR PathwayCommons; Q9HB14; -.
DR Reactome; R-HSA-1299287; Tandem pore domain halothane-inhibited K+ channel (THIK).
DR Reactome; R-HSA-5576886; Phase 4 - resting membrane potential.
DR BioGRID-ORCS; 56659; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; KCNK13; human.
DR GeneWiki; KCNK13; -.
DR GenomeRNAi; 56659; -.
DR Pharos; Q9HB14; Tbio.
DR PRO; PR:Q9HB14; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9HB14; protein.
DR Bgee; ENSG00000152315; Expressed in right testis and 96 other tissues.
DR Genevisible; Q9HB14; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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 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..408
FT /note="Potassium channel subfamily K member 13"
FT /id="PRO_0000101762"
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..408
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"
FT VARIANT 305
FT /note="G -> R (in dbSNP:rs3814848)"
FT /id="VAR_052429"
FT VARIANT 389
FT /note="G -> A (in dbSNP:rs35909577)"
FT /id="VAR_034052"
FT CONFLICT 288
FT /note="N -> D (in Ref. 1; AAG32314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 45391 MW; B303C01AFD59EE19 CRC64;
MAGRGFSWGP GHLNEDNARF LLLAALIVLY LLGGAAVFSA LELAHERQAK QRWEERLANF
SRGHNLSRDE LRGFLRHYEE ATRAGIRVDN VRPRWDFTGA FYFVGTVVST IGFGMTTPAT
VGGKIFLIFY GLVGCSSTIL FFNLFLERLI TIIAYIMKSC HQRQLRRRGA LPQESLKDAG
QCEVDSLAGW KPSVYYVMLI LCTASILISC CASAMYTPIE GWSYFDSLYF CFVAFSTIGF
GDLVSSQNAH YESQGLYRFA NFVFILMGVC CIYSLFNVIS ILIKQSLNWI LRKMDSGCCP
QCQRGLLRSR RNVVMPGSVR NRCNISIETD GVAESDTDGR RLSGEMISMK DLLAANKASL
AILQKQLSEM ANGCPHQTST LARDNEFSGG VGAFAIMNNR LAETSGDR
