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   27-MAR-2024, entry version 150.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyCosmos; Q6ZPR4; 2 sites, No reported glycans.
DR   GlyGen; Q6ZPR4; 2 sites.
DR   iPTMnet; Q6ZPR4; -.
DR   PhosphoSitePlus; Q6ZPR4; -.
DR   PaxDb; 10090-ENSMUSP00000039058; -.
DR   ProteomicsDB; 268967; -.
DR   ABCD; Q6ZPR4; 1 sequenced antibody.
DR   Antibodypedia; 32072; 198 antibodies from 26 providers.
DR   DNASU; 227632; -.
DR   Ensembl; ENSMUST00000114172.6; ENSMUSP00000109809.3; ENSMUSG00000058740.15.
DR   GeneID; 227632; -.
DR   KEGG; mmu:227632; -.
DR   UCSC; uc008itq.2; mouse.
DR   AGR; MGI:1924627; -.
DR   CTD; 57582; -.
DR   MGI; MGI:1924627; Kcnt1.
DR   VEuPathDB; HostDB:ENSMUSG00000058740; -.
DR   eggNOG; KOG3193; Eukaryota.
DR   GeneTree; ENSGT00940000156880; -.
DR   InParanoid; Q6ZPR4; -.
DR   OrthoDB; 2907493at2759; -.
DR   BioGRID-ORCS; 227632; 3 hits in 77 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 115 other cell types or tissues.
DR   ExpressionAtlas; Q6ZPR4; baseline and differential.
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:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR003929; K_chnl_BK_asu.
DR   InterPro; IPR013099; K_chnl_dom.
DR   InterPro; IPR047871; K_chnl_Slo-like.
DR   PANTHER; PTHR10027; CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA CHAIN; 1.
DR   PANTHER; PTHR10027:SF14; POTASSIUM CHANNEL SUBFAMILY T MEMBER 1; 1.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF07885; Ion_trans_2; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   Genevisible; Q6ZPR4; MM.
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
//