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KCNF1_MOUSE
ID   KCNF1_MOUSE             Reviewed;         493 AA.
AC   Q7TSH7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 139.
DE   RecName: Full=Potassium voltage-gated channel subfamily F member 1;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv5.1;
GN   Name=Kcnf1;
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   STRAIN=C57BL/6J; TISSUE=Cerebellum;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Putative voltage-gated potassium channel. {ECO:0000250}.
CC   -!- SUBUNIT: Heteromultimer with KCNG3, KCNG4 and KCNV2. Interacts with
CC       DLG1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at every
CC       third position. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. F (TC 1.A.1.2)
CC       subfamily. Kv5.1/KCNF1 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AK137367; BAE23327.1; -; mRNA.
DR   EMBL; BC053089; AAH53089.1; -; mRNA.
DR   CCDS; CCDS25825.2; -.
DR   RefSeq; NP_963289.2; NM_201531.3.
DR   AlphaFoldDB; Q7TSH7; -.
DR   SMR; Q7TSH7; -.
DR   STRING; 10090.ENSMUSP00000131480; -.
DR   iPTMnet; Q7TSH7; -.
DR   PhosphoSitePlus; Q7TSH7; -.
DR   SwissPalm; Q7TSH7; -.
DR   PaxDb; Q7TSH7; -.
DR   PRIDE; Q7TSH7; -.
DR   ProteomicsDB; 269263; -.
DR   DNASU; 382571; -.
DR   GeneID; 382571; -.
DR   KEGG; mmu:382571; -.
DR   CTD; 3754; -.
DR   MGI; MGI:2687399; Kcnf1.
DR   eggNOG; KOG3713; Eukaryota.
DR   InParanoid; Q7TSH7; -.
DR   OrthoDB; 818306at2759; -.
DR   PhylomeDB; Q7TSH7; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   BioGRID-ORCS; 382571; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Kcnf1; mouse.
DR   PRO; PR:Q7TSH7; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q7TSH7; protein.
DR   GO; GO:0097546; C:ciliary base; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR   GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003971; K_chnl_volt-dep_Kv9.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR028325; VG_K_chnl.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR11537; PTHR11537; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR01494; KV9CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   1: Evidence at protein level;
KW   Ion channel; Ion transport; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..493
FT                   /note="Potassium voltage-gated channel subfamily F member
FT                   1"
FT                   /id="PRO_0000320105"
FT   TOPO_DOM        1..183
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        245..249
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        311..324
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        325..345
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        358..378
FT                   /note="Pore-forming; Name=Segment H5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        407..493
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          434..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           370..375
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   493 AA;  55647 MW;  F5C55969DF79FAD3 CRC64;
     MDASAEQSLP EPGSQDSVAG EDIEIVVNVG GVRQVLYGDL LSQYPETRLA ELINCLAGGY
     DTIFSLCDDY DPGKREFYFD RDPDAFKCVI EVYYFGEVHM KKGICPICFK NEMDFWKVDL
     KFLDDCCKSH LSEKREELEE IARRVQLILD DLGVDAAEGR WRRCQKCVWK FLEKPESSCP
     ARVVAVLSFL LILVSSVVMC MGTIPELQVV DSEGNRVEHP TLENVETACI GWFTLEYLLR
     LFSSPNKLHF ALSFMNIVDV LAILPFYVSL TLTHLGARMM ELTNVQQAVQ ALRIMRIARI
     FKLARHSSGL QTLTYALKRS FKELGLLLMY LAVGIFVFSA LGYTMEQSHP ETLFKSIPQS
     FWWAIITMTT VGYGDIYPKT TLGKLNAAIS FLCGVIAIAL PIHPIINNFV RYYNKQRVLE
     TAAKHELELM ELNSSSAEGK PGGSRSDLDT LPPEPAAREG PSWGSRLKLS HSDTFIPLLT
     EEKHHRTRLQ SCK
 
 
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