KCNN4_RAT
ID KCNN4_RAT Reviewed; 425 AA.
AC Q9QYW1; Q9R198; Q9WVA5;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 25-MAY-2022, entry version 143.
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; Synonyms=Ik1, Sk4, Smik;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar Kyoto; TISSUE=Aortic smooth muscle;
RX PubMed=10532960; DOI=10.1161/01.res.85.9.e33;
RA Neylon C., Lang R.J., Fu Y., Bobik A., Reinhart P.H.;
RT "Molecular cloning and characterization of the intermediate-conductance
RT Ca(2+)-activated K(+) channel in vascular smooth muscle: relationship
RT between K(Ca) channel diversity and smooth muscle cell function.";
RL Circ. Res. 85:E33-E43(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Colon;
RX PubMed=10519135; DOI=10.1007/s004249900059;
RA Warth R., Hamm K., Bleich M., Kunzelmann K., von Hahn T., Schreiber R.,
RA Ullrich E., Mengel M., Trautmann N., Kindle P., Schwab A., Greger R.;
RT "Molecular and functional characterization of the small Ca2+-regulated K+
RT channel (rSK4) of colonic crypts.";
RL Pflugers Arch. 438:437-444(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Fujiwara Y., Saito T., Sasamura R., Miura M.;
RT "Rat intermediate conductance calcium-activated potassium channel.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Rajendran V.M., Sangan P., Joiner W.J., Binder H.J.;
RT "cDNA cloning of an intermediate conductance Ca2+-activated K+ channel
RT (rIK1) and its regulation by dietary K-depletion in rat distal colon.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms a voltage-independent potassium channel that is
CC activated by intracellular calcium. Activation is followed by membrane
CC hyperpolarization which promotes calcium influx. Required for maximal
CC calcium influx and proliferation during the reactivation of naive T-
CC cells. The channel is blocked by clotrimazole and charybdotoxin but is
CC insensitive to apamin. {ECO:0000250|UniProtKB:O15554,
CC ECO:0000250|UniProtKB:O89109}.
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; AF190458; AAF05602.1; -; mRNA.
DR EMBL; AF149250; AAD38032.1; -; mRNA.
DR EMBL; AJ133438; CAB40141.2; -; mRNA.
DR EMBL; AF156554; AAD38205.1; -; mRNA.
DR AlphaFoldDB; Q9QYW1; -.
DR SMR; Q9QYW1; -.
DR STRING; 10116.ENSRNOP00000026489; -.
DR BindingDB; Q9QYW1; -.
DR iPTMnet; Q9QYW1; -.
DR PhosphoSitePlus; Q9QYW1; -.
DR PaxDb; Q9QYW1; -.
DR UCSC; RGD:621476; rat.
DR RGD; 621476; Kcnn4.
DR eggNOG; KOG3684; Eukaryota.
DR InParanoid; Q9QYW1; -.
DR PhylomeDB; Q9QYW1; -.
DR Reactome; R-RNO-1296052; Ca2+ activated K+ channels.
DR PRO; PR:Q9QYW1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0022894; F:Intermediate conductance calcium-activated potassium channel activity; IDA:RGD.
DR GO; GO:0005267; F:potassium channel activity; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IEA:InterPro.
DR GO; GO:0006820; P:anion transport; IDA:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0006884; P:cell volume homeostasis; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IDA:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IDA:RGD.
DR GO; GO:0046541; P:saliva secretion; ISO:RGD.
DR GO; GO:0030322; P:stabilization of membrane potential; ISO:RGD.
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_0000155019"
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 213
FT /note="L -> F (in Ref. 2; CAB40141)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="V -> L (in Ref. 4; AAD38205)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="D -> H (in Ref. 4; AAD38205)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="G -> R (in Ref. 4; AAD38205)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="T -> S (in Ref. 4; AAD38205)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="Missing (in Ref. 4; AAD38205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 47767 MW; E861DB088D20D8FC CRC64;
MGGELVTGLG ALRRRKRLLE QEKRVAGWAL VLAGTGIGLM VLHAEMLWFL GCKWVLYLLL
VKCLITLSTA FLLCLIVVFH AKEVQLFMTD NGLRDWRVAL TRRQVAQILL ELLVCGVHPV
PLRSPHCTLA GEATDSQAWP GFLGEGEALL SLAMLLRLYL VPRAVLLRSG VLLNASYRSI
GALNQVRFRH WFVAKLYMNT HPGRLLLGLT LGLWLTTAWV LSVAERQAVN ATGHLTDTLW
LIPITFLTIG YGDVVPGTLW GKIVCLCTGV MGVCCTALLV AVVARKLEFN KAEKHVHNFM
MDIHYAKEMK ESAARLLQEA WMYYKHTRRK DSRAARRHQR KMLAAIHTFR QVRLKHRKLR
EQVNSMVDIS KMHMILCDLQ LGLSASHLAL EKRIDGLAGK LDALTELLST ALQQQQPPEP
IQEAT
