KCNT1_MOUSE
ID KCNT1_MOUSE Reviewed; 1224 AA.
AC Q6ZPR4; B2RUK3; Q8C3E7;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Potassium channel subfamily T member 1;
GN Name=Kcnt1; Synonyms=Kiaa1422;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-297.
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-1224.
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP INTERACTION WITH FMR1.
RX PubMed=20512134; DOI=10.1038/nn.2563;
RA Brown M.R., Kronengold J., Gazula V.R., Chen Y., Strumbos J.G.,
RA Sigworth F.J., Navaratnam D., Kaczmarek L.K.;
RT "Fragile X mental retardation protein controls gating of the sodium-
RT activated potassium channel Slack.";
RL Nat. Neurosci. 13:819-821(2010).
CC -!- FUNCTION: Outwardly rectifying potassium channel subunit that may
CC coassemble with other Slo-type channel subunits. Activated by high
CC intracellular sodium or chloride levels. Activated upon stimulation of
CC G-protein coupled receptors, such as CHRM1 and GRIA1. May be regulated
CC by calcium in the absence of sodium ions (in vitro) (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via C-terminus) with FMR1; this interaction alters
CC gating properties of KCNT1 (By similarity). Interacts with CRBN via its
CC cytoplasmic C-terminus (By similarity). {ECO:0000250|UniProtKB:Q5JUK3,
CC ECO:0000250|UniProtKB:Q9Z258}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Phosphorylated by protein kinase C. Phosphorylation of the C-
CC terminal domain increases channel activity (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC (TC 1.A.1.3) subfamily. KCa4.1/KCNT1 sub-subfamily. {ECO:0000305}.
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DR EMBL; BC141190; AAI41191.1; -; mRNA.
DR EMBL; BC171963; AAI71963.1; -; mRNA.
DR EMBL; AK086119; BAC39614.1; -; mRNA.
DR EMBL; AK129355; BAC98165.1; -; mRNA.
DR CCDS; CCDS79757.1; -.
DR RefSeq; NP_001289280.1; NM_001302351.1.
DR RefSeq; NP_780671.2; NM_175462.4.
DR AlphaFoldDB; Q6ZPR4; -.
DR SMR; Q6ZPR4; -.
DR BioGRID; 230652; 2.
DR IntAct; Q6ZPR4; 3.
DR MINT; Q6ZPR4; -.
DR STRING; 10090.ENSMUSP00000039058; -.
DR BindingDB; Q6ZPR4; -.
DR ChEMBL; CHEMBL4739694; -.
DR GuidetoPHARMACOLOGY; 385; -.
DR GlyGen; Q6ZPR4; 2 sites.
DR iPTMnet; Q6ZPR4; -.
DR PhosphoSitePlus; Q6ZPR4; -.
DR PaxDb; Q6ZPR4; -.
DR PRIDE; Q6ZPR4; -.
DR ProteomicsDB; 268967; -.
DR ABCD; Q6ZPR4; 1 sequenced antibody.
DR Antibodypedia; 32072; 178 antibodies from 26 providers.
DR DNASU; 227632; -.
DR Ensembl; ENSMUST00000114172; ENSMUSP00000109809; ENSMUSG00000058740.
DR GeneID; 227632; -.
DR KEGG; mmu:227632; -.
DR UCSC; uc008itq.2; mouse.
DR CTD; 57582; -.
DR MGI; MGI:1924627; Kcnt1.
DR VEuPathDB; HostDB:ENSMUSG00000058740; -.
DR eggNOG; KOG3193; Eukaryota.
DR GeneTree; ENSGT00940000156880; -.
DR InParanoid; Q6ZPR4; -.
DR OrthoDB; 858812at2759; -.
DR BioGRID-ORCS; 227632; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Kcnt1; mouse.
DR PRO; PR:Q6ZPR4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6ZPR4; protein.
DR Bgee; ENSMUSG00000058740; Expressed in cerebellar cortex and 113 other tissues.
DR ExpressionAtlas; Q6ZPR4; baseline and differential.
DR Genevisible; Q6ZPR4; MM.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005228; F:intracellular sodium activated potassium channel activity; IBA:GO_Central.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR InterPro; IPR003929; K_chnl_BK_asu.
DR InterPro; IPR013099; K_chnl_dom.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1224
FT /note="Potassium channel subfamily T member 1"
FT /id="PRO_0000054091"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..212
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..267
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 268..288
FT /note="Pore-forming"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..1224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 461..582
FT /note="RCK N-terminal"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1224 AA; 138106 MW; 7F343893D70E506B CRC64;
MARAKLPRSP SEGKAGPGDT PAGAAAPEEP HGLSPLLPAR GGGSVGSDVG QRVQVEFYVN
ENTFKERLKL FFIKNQRSSL RIRLFNFSLK LLTCLLYIVR VLLDNPDQGI GCWGCTKYNY
TFNGSSSEFH WAPILWVERK MALWVIQVIV ATISFLETML IIYLSYKGNI WEQIFHVSFV
LEMINTLPFI ITVFWPPLRN LFIPVFLNCW LAKHALENMI NDFHRAILRT QSAMFNQVLI
LFCTLLCLVF TGTCGIQHLE RAGGNLNLLT SFYFCIVTFS TVGFGDVTPK IWPSQLLVVI
LICVTLVVLP LQFEELVYLW MERQKSGGNY SRHRARTEKH VVLCVSSLKI DLLMDFLNEF
YAHPRLQDYY VVILCPSEMD VQVRRVLQIP LWSQRVIYLQ GSALKDQDLM RAKMDNGEAC
FILSSRNEVD RTAADHQTIL RAWAVKDFAP NCPLYVQILK PENKFHVKFA DHVVCEEECK
YAMLALNCIC PATSTLITLL VHTSRGQEGQ ESPEQWQRTY GRCSGNEVYH IRMGDSKFFR
EYEGKSFTYA AFHAHKKYGV CLIGLKREEN KSILLNPGPR HILAASDTCF YINITKEENS
AFIFKQEEKQ KRRGLAGQAL YEGPSRLPVH SIIASMGTVA MDLQNTDCRP SQGGSGGDGT
KLTLPTENGS GSRRPSIAPV LELADSSALL PCDLLSDQSE DEVTPSDDEG LSVVEYVKGY
PPNSPYIGSS PTLCHLLPVK APFCCLRLDK GCKHNSYEDA KAYGFKNKLI IVSAETAGNG
LYNFIVPLRA YYRSRRELNP IVLLLDNKPD HHFLEAICCF PMVYYMEGSV DNLDSLLQCG
IIYADNLVVV DKESTMSAEE DYMADAKTIV NVQTMFRLFP SLSITTELTH PSNMRFMQFR
AKDSYSLALS KLEKQERENG SNLAFMFRLP FAAGRVFSIS MLDTLLYQSF VKDYMITITR
LLLGLDTTPG SGYLCAMKVT EDDLWIRTYG RLFQKLCSSS AEIPIGIYRT ECHVFSEPHD
VRAQSQISVN MEDCEDTREA KGPWGTRAAS GSGSTHGRHG GSADPVEHPL LRRKSLQWAR
KLSRKSTKQA GKAPVATDWI TQQRLSLYRR SERQELSELV KNRMKHLGLP TTGYEDVANL
TASDVMNRVN LGYLQDEMND HHQNTLSYVL INPPPDTRLE PNDIVYLIRS DPLAHVASSS
QSRKSSCSNK LSSCNPETRD ETQL
