KCIP4_RAT
ID KCIP4_RAT Reviewed; 250 AA.
AC Q99MG9; Q99MG8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Kv channel-interacting protein 4;
DE Short=KChIP4;
DE AltName: Full=A-type potassium channel modulatory protein 4;
DE AltName: Full=Potassium channel-interacting protein 4;
GN Name=Kcnip4; Synonyms=Kchip4;
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] (ISOFORMS 1 AND 2).
RX PubMed=11351020; DOI=10.1111/j.1469-7793.2001.0119b.x;
RA Rosati B., Pan Z., Lypen S., Wang H.S., Cohen I., Dixon J.E., McKinnon D.;
RT "Regulation of KChIP2 potassium channel beta subunit gene expression
RT underlies the gradient of transient outward current in canine and human
RT ventricle.";
RL J. Physiol. (Lond.) 533:119-125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH KCND3,
RP AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=11805342; DOI=10.1073/pnas.022509299;
RA Holmqvist M.H., Cao J., Hernandez-Pineda R., Jacobson M.D., Carroll K.I.,
RA Sung M.A., Betty M., Ge P., Gilbride K.J., Brown M.E., Jurman M.E.,
RA Lawson D., Silos-Santiago I., Xie Y., Covarrubias M., Rhodes K.J.,
RA Distefano P.S., An W.F.;
RT "Elimination of fast inactivation in Kv4 A-type potassium channels by an
RT auxiliary subunit domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1035-1040(2002).
RN [3]
RP INTERACTION WITH KCND2.
RX PubMed=11847232; DOI=10.1074/jbc.m200897200;
RA Morohashi Y., Hatano N., Ohya S., Takikawa R., Watabiki T., Takasugi N.,
RA Imaizumi Y., Tomita T., Iwatsubo T.;
RT "Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand
RT protein interacting with presenilin 2 and voltage-gated potassium channel
RT subunit Kv4.";
RL J. Biol. Chem. 277:14965-14975(2002).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=15356203; DOI=10.1523/jneurosci.0776-04.2004;
RA Rhodes K.J., Carroll K.I., Sung M.A., Doliveira L.C., Monaghan M.M.,
RA Burke S.L., Strassle B.W., Buchwalder L., Menegola M., Cao J., An W.F.,
RA Trimmer J.S.;
RT "KChIPs and Kv4 alpha subunits as integral components of A-type potassium
RT channels in mammalian brain.";
RL J. Neurosci. 24:7903-7915(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19441798; DOI=10.1021/bi802316m;
RA Seikel E., Trimmer J.S.;
RT "Convergent modulation of Kv4.2 channel alpha subunits by structurally
RT distinct DPPX and KChIP auxiliary subunits.";
RL Biochemistry 48:5721-5730(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KCND2.
RX PubMed=24811166; DOI=10.1074/jbc.m114.563452;
RA Kitazawa M., Kubo Y., Nakajo K.;
RT "The stoichiometry and biophysical properties of the Kv4 potassium channel
RT complex with K+ channel-interacting protein (KChIP) subunits are variable,
RT depending on the relative expression level.";
RL J. Biol. Chem. 289:17597-17609(2014).
CC -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly
CC inactivating A-type potassium channels, such as KCND2/Kv4.2 and
CC KCND3/Kv4.3. Modulates channel expression at the cell membrane, gating
CC characteristics, inactivation kinetics and rate of recovery from
CC inactivation in a calcium-dependent and isoform-specific manner.
CC {ECO:0000269|PubMed:11805342, ECO:0000269|PubMed:19441798,
CC ECO:0000269|PubMed:24811166}.
CC -!- SUBUNIT: Component of heteromultimeric potassium channels. Identified
CC in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1,
CC KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (By similarity). Interacts with
CC the C-terminus of PSEN2 and probably PSEN1 (By similarity). Interacts
CC with KCND2 and KCND3 (By similarity). {ECO:0000250|UniProtKB:Q6PHZ8,
CC ECO:0000250|UniProtKB:Q6PIL6, ECO:0000269|PubMed:11805342,
CC ECO:0000269|PubMed:11847232}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24811166};
CC Peripheral membrane protein {ECO:0000269|PubMed:24811166}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:19441798}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=KChIP4bl;
CC IsoId=Q99MG9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99MG9-2; Sequence=VSP_015072;
CC -!- TISSUE SPECIFICITY: Expressed in brain. Colocalizes with KCND2 in
CC excitatory neurons including cortical and hippocampal CA1 pyramidal
CC cells. {ECO:0000269|PubMed:11805342, ECO:0000269|PubMed:15356203}.
CC -!- DOMAIN: The KIS (K-channel inactivation suppressor) domain is required
CC for converting A-type Kv4 current to a slowly inactivating delayed
CC rectifier potassium current. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the recoverin family. {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; AF345444; AAK28291.1; -; mRNA.
DR EMBL; AF345445; AAK28292.1; -; mRNA.
DR EMBL; AF453245; AAL86768.1; -; mRNA.
DR RefSeq; NP_852030.1; NM_181365.2. [Q99MG9-1]
DR RefSeq; XP_017454578.1; XM_017599089.1. [Q99MG9-2]
DR AlphaFoldDB; Q99MG9; -.
DR BMRB; Q99MG9; -.
DR SMR; Q99MG9; -.
DR CORUM; Q99MG9; -.
DR STRING; 10116.ENSRNOP00000042016; -.
DR iPTMnet; Q99MG9; -.
DR PhosphoSitePlus; Q99MG9; -.
DR PaxDb; Q99MG9; -.
DR PRIDE; Q99MG9; -.
DR ABCD; Q99MG9; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000049743; ENSRNOP00000042016; ENSRNOG00000032350. [Q99MG9-1]
DR Ensembl; ENSRNOT00000079658; ENSRNOP00000075583; ENSRNOG00000032350. [Q99MG9-2]
DR GeneID; 259243; -.
DR KEGG; rno:259243; -.
DR CTD; 80333; -.
DR RGD; 708539; Kcnip4.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158985; -.
DR InParanoid; Q99MG9; -.
DR OrthoDB; 1513542at2759; -.
DR PhylomeDB; Q99MG9; -.
DR Reactome; R-RNO-5576894; Phase 1 - inactivation of fast Na+ channels.
DR PRO; PR:Q99MG9; -.
DR Proteomes; UP000002494; Chromosome 14.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:UniProtKB.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cytoplasm; Ion channel;
KW Ion transport; Membrane; Metal-binding; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Repeat;
KW Transport; Voltage-gated channel.
FT CHAIN 1..250
FT /note="Kv channel-interacting protein 4"
FT /id="PRO_0000073828"
FT DOMAIN 61..117
FT /note="EF-hand 1; degenerate"
FT /evidence="ECO:0000305"
FT DOMAIN 120..155
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 156..191
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 204..239
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 2..44
FT /note="KIS"
FT /evidence="ECO:0000250"
FT REGION 237..250
FT /note="Interaction with KCND2"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PHZ8"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PHZ8"
FT VAR_SEQ 21..55
FT /note="GFLYAQNNTKRSIKERLMKLLPCSAAKTSSPAIQN -> D (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:11351020"
FT /id="VSP_015072"
SQ SEQUENCE 250 AA; 28756 MW; 56542298021192BF CRC64;
MNVRRVESIS AQLEEASSTG GFLYAQNNTK RSIKERLMKL LPCSAAKTSS PAIQNSVEDE
LEMATVRHRP EALELLEAQS KFTKKELQIL YRGFKNECPS GVVNEETFKE IYSQFFPQGD
STTYAHFLFN AFDTDHNGAV SFEDFIKGLS ILLRGTVQEK LNWAFNLYDI NKDGYITKEE
MLDIMKAIYD MMGKCTYPVL KEDAPRQHVE TFFQKMDKNK DGVVTIDEFI ESCQKDENIM
RSMQLFENVI
