KCNN4_MOUSE
ID KCNN4_MOUSE Reviewed; 425 AA.
AC O89109; Q3U1J8; Q9CY39;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Intermediate conductance calcium-activated potassium channel protein 4;
DE Short=SK4;
DE Short=SKCa 4;
DE Short=SKCa4;
DE AltName: Full=IK1;
DE AltName: Full=KCa3.1;
DE AltName: Full=KCa4;
GN Name=Kcnn4;
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 [MRNA], FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=CD-1;
RX PubMed=9705284; DOI=10.1074/jbc.273.34.21542;
RA Vandorpe D.H., Shmukler B.E., Jiang L., Lim B., Maylie J., Adelman J.P.,
RA de Franceschi L., Cappellini M.D., Brugnara C., Alper S.L.;
RT "cDNA cloning and functional characterization of the mouse Ca2+-gated K+
RT channel, mIK1. Roles in regulatory volume decrease and erythroid
RT differentiation.";
RL J. Biol. Chem. 273:21542-21553(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Logsdon N.J., Aiyar J.;
RT "Murine intermediate conductance calcium-activated potassium channel
RT (mKCa4, KCNN4) complete cds.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic liver;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [5]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=20884616; DOI=10.1074/jbc.m110.168070;
RA Di L., Srivastava S., Zhdanova O., Sun Y., Li Z., Skolnik E.Y.;
RT "Nucleoside diphosphate kinase B knock-out mice have impaired activation of
RT the K+ channel KCa3.1, resulting in defective T cell activation.";
RL J. Biol. Chem. 285:38765-38771(2010).
CC -!- FUNCTION: Forms a voltage-independent potassium channel that is
CC activated by intracellular calcium (PubMed:9705284). Activation is
CC followed by membrane hyperpolarization which promotes calcium influx.
CC Required for maximal calcium influx and proliferation during the
CC reactivation of naive T-cells (PubMed:20884616). Plays a role in the
CC late stages of EGF-induced macropinocytosis (By similarity).
CC {ECO:0000250|UniProtKB:O15554, ECO:0000269|PubMed:20884616,
CC ECO:0000269|PubMed:9705284}.
CC -!- ACTIVITY REGULATION: The channel is inhibited by clotrimazole and
CC charybdotoxin but is insensitive to apamin.
CC {ECO:0000269|PubMed:20884616, ECO:0000269|PubMed:9705284}.
CC -!- SUBUNIT: Heterotetramer of potassium channel proteins (Probable).
CC Interacts with MTMR6 (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O15554};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O15554}.
CC -!- PTM: Phosphorylation at His-356 by NDKB activates the channel, and
CC conversely it's dephosphorylation by PHPT1 inhibits the channel.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potassium channel KCNN family. KCa3.1/KCNN4
CC subfamily. {ECO:0000305}.
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DR EMBL; AF042487; AAC32051.1; -; mRNA.
DR EMBL; AF072884; AAC32829.1; -; mRNA.
DR EMBL; AK010943; BAB27283.1; -; mRNA.
DR EMBL; AK155910; BAE33499.1; -; mRNA.
DR EMBL; BC010274; AAH10274.1; -; mRNA.
DR CCDS; CCDS20948.1; -.
DR RefSeq; NP_001156982.1; NM_001163510.1.
DR RefSeq; NP_032459.3; NM_008433.4.
DR RefSeq; XP_006539626.1; XM_006539563.3.
DR AlphaFoldDB; O89109; -.
DR SMR; O89109; -.
DR CORUM; O89109; -.
DR STRING; 10090.ENSMUSP00000133065; -.
DR iPTMnet; O89109; -.
DR PhosphoSitePlus; O89109; -.
DR EPD; O89109; -.
DR MaxQB; O89109; -.
DR PaxDb; O89109; -.
DR PRIDE; O89109; -.
DR ProteomicsDB; 268964; -.
DR Antibodypedia; 31124; 311 antibodies from 33 providers.
DR DNASU; 16534; -.
DR Ensembl; ENSMUST00000171904; ENSMUSP00000133065; ENSMUSG00000054342.
DR Ensembl; ENSMUST00000205428; ENSMUSP00000146012; ENSMUSG00000054342.
DR GeneID; 16534; -.
DR KEGG; mmu:16534; -.
DR UCSC; uc009fpk.2; mouse.
DR CTD; 3783; -.
DR MGI; MGI:1277957; Kcnn4.
DR VEuPathDB; HostDB:ENSMUSG00000054342; -.
DR eggNOG; KOG3684; Eukaryota.
DR GeneTree; ENSGT00950000182904; -.
DR HOGENOM; CLU_014617_5_2_1; -.
DR InParanoid; O89109; -.
DR OMA; PPCVQDL; -.
DR OrthoDB; 907751at2759; -.
DR PhylomeDB; O89109; -.
DR TreeFam; TF315015; -.
DR Reactome; R-MMU-1296052; Ca2+ activated K+ channels.
DR BioGRID-ORCS; 16534; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Kcnn4; mouse.
DR PRO; PR:O89109; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O89109; protein.
DR Bgee; ENSMUSG00000054342; Expressed in parotid gland and 162 other tissues.
DR ExpressionAtlas; O89109; baseline and differential.
DR Genevisible; O89109; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:MGI.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0022894; F:Intermediate conductance calcium-activated potassium channel activity; ISO:MGI.
DR GO; GO:0005267; F:potassium channel activity; IGI:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IEA:InterPro.
DR GO; GO:0006820; P:anion transport; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR GO; GO:0006884; P:cell volume homeostasis; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; IMP:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; IDA:MGI.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; 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 GO; GO:0046541; P:saliva secretion; IGI:MGI.
DR GO; GO:0030322; P:stabilization of membrane potential; ISO:MGI.
DR InterPro; IPR004178; CaM-bd_dom.
DR InterPro; IPR036122; CaM-bd_dom_sf.
DR InterPro; IPR015449; K_chnl_Ca-activ_SK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR10153; PTHR10153; 1.
DR Pfam; PF02888; CaMBD; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR Pfam; PF03530; SK_channel; 1.
DR SMART; SM01053; CaMBD; 1.
DR SUPFAM; SSF81327; SSF81327; 1.
PE 2: Evidence at transcript level;
KW Calmodulin-binding; Cell membrane; Immunity; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..425
FT /note="Intermediate conductance calcium-activated potassium
FT channel protein 4"
FT /id="PRO_0000155018"
FT TRANSMEM 30..50
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..121
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 239..259
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT REGION 284..345
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 356
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:O15554"
FT CONFLICT 181
FT /note="G -> E (in Ref. 3; BAB27283)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 47784 MW; DCD2FC86BDD69A73 CRC64;
MGGELVTGLG ALRRRKRLLE QEKRVAGWAL VLAGTGIGLM VLHAEMLWFL GCKWVLYLLL
VKCLITLSTA FLLCLIVVFH AKEVQLFMTD NGLRDWRVAL TRRQVAQILL ELLVCGVHPV
PLRSPHCALA GEATDAQPWP GFLGEGEALL SLAMLLRLYL VPRAVLLRSG VLLNASYRSI
GALNQVRFRH WFVAKLYMNT HPGRLLLGLT LGLWLTTAWV LSVAERQAVN ATGHLTDTLW
LIPITFLTIG YGDVVPGTMW GKIVCLCTGV MGVCCTALLV AVVARKLEFN KAEKHVHNFM
MDIHYAKEMK ESAARLLQEA WMYYKHTRRK DSRAARRHQR KMLAAIHTFR QVRLKHRKLR
EQVNSMVDIS KMHMILCDLQ LGLSSSHRAL EKRIDGLAGK LDALTELLGT ALQQQQLPEP
SQEAT
