KCIP1_RAT
ID KCIP1_RAT Reviewed; 227 AA.
AC Q8R426; Q793P9; Q8CIR1; Q8R425;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Kv channel-interacting protein 1;
DE Short=KChIP1;
DE AltName: Full=A-type potassium channel modulatory protein 1;
DE AltName: Full=Potassium channel-interacting protein 1;
GN Name=Kcnip1; Synonyms=Kchip1;
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] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11263977; DOI=10.1006/bbrc.2001.4558;
RA Ohya S., Morohashi Y., Muraki K., Tomita T., Watanabe M., Iwatsubo T.,
RA Imaizumi Y.;
RT "Molecular cloning and expression of the novel splice variants of K(+)
RT channel-interacting protein 2.";
RL Biochem. Biophys. Res. Commun. 282:96-102(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Sprague-Dawley;
RA Takimoto K.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12646414; DOI=10.1152/ajpcell.00416.2002;
RA Boland L.M., Jiang M., Lee S.Y., Fahrenkrug S.C., Harnett M.T.,
RA O'Grady S.M.;
RT "Functional properties of a brain-specific NH2-terminally spliced modulator
RT of Kv4 channels.";
RL Am. J. Physiol. 285:C161-C170(2003).
RN [4]
RP INTERACTION WITH KCND2 AND KCND3, AND TISSUE SPECIFICITY.
RX PubMed=10676964; DOI=10.1038/35000592;
RA An W.F., Bowlby M.R., Betty M., Cao J., Ling H.-P., Mendoza G.,
RA Hinson J.W., Mattsson K.I., Strassle B.W., Trimmer J.S., Rhodes K.J.;
RT "Modulation of A-type potassium channels by a family of calcium sensors.";
RL Nature 403:553-556(2000).
RN [5]
RP INTERACTION WITH KCND2.
RX PubMed=11423117; DOI=10.1016/s0014-5793(01)02560-1;
RA Nakamura T.Y., Nandi S., Pountney D.J., Artman M., Rudy B., Coetzee W.A.;
RT "Different effects of the Ca(2+)-binding protein, KChIP1, on two Kv4
RT subfamily members, Kv4.1 and Kv4.2.";
RL FEBS Lett. 499:205-209(2001).
RN [6]
RP TISSUE SPECIFICITY, INTERACTION WITH KCND2, AND SUBCELLULAR LOCATION.
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 45-216 IN COMPLEX WITH CALCIUM
RP IONS AND KCND2, INTERACTION WITH KCND2, CALCIUM-BINDING, FUNCTION,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 214-ASP--MET-227.
RX PubMed=14980206; DOI=10.1016/s0896-6273(04)00045-5;
RA Zhou W., Qian Y., Kunjilwar K., Pfaffinger P.J., Choe S.;
RT "Structural insights into the functional interaction of KChIP1 with Shal-
RT type K(+) channels.";
RL Neuron 41:573-586(2004).
CC -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly
CC inactivating A-type potassium channels (PubMed:14980206). Regulates
CC channel density, inactivation kinetics and rate of recovery from
CC inactivation in a calcium-dependent and isoform-specific manner
CC (PubMed:14980206). Modulates KCND2/Kv4.2 currents (PubMed:14980206). In
CC vitro, modulates KCND1/Kv4.1 currents (By similarity). Increases the
CC presence of KCND2 at the cell surface (PubMed:14980206).
CC {ECO:0000250|UniProtKB:Q9NZI2, ECO:0000269|PubMed:12646414,
CC ECO:0000269|PubMed:14980206}.
CC -!- SUBUNIT: Component of heteromultimeric potassium channels
CC (PubMed:15356203, PubMed:14980206). Identified in potassium channel
CC complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3,
CC KCNIP4, DPP6 and DPP10 (By similarity). Part of a heterooctamer
CC composed of the tetrameric channel and four KCNIP1 chains (By
CC similarity). Interacts with KCND3 and the N-terminal domain of KCND2.
CC Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and
CC KCND2 (PubMed:14980206). Self-associates to form homodimers and
CC homotetramers. Interacts with KCNIP2 isoform 3 in a calcium-dependent
CC manner. {ECO:0000250|UniProtKB:Q9JJ57, ECO:0000250|UniProtKB:Q9NZI2,
CC ECO:0000269|PubMed:10676964, ECO:0000269|PubMed:11423117,
CC ECO:0000269|PubMed:14980206, ECO:0000269|PubMed:15356203}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14980206,
CC ECO:0000269|PubMed:15356203}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14980206}. Cytoplasm {ECO:0000269|PubMed:14980206,
CC ECO:0000269|PubMed:15356203}. Cell projection, dendrite
CC {ECO:0000269|PubMed:15356203}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=KChIP1b;
CC IsoId=Q8R426-1; Sequence=Displayed;
CC Name=2; Synonyms=KChIP1a;
CC IsoId=Q8R426-2; Sequence=VSP_015048;
CC -!- TISSUE SPECIFICITY: Detected in hippocampus and in the molecular layer
CC of the dentate gyrus (at protein level) (PubMed:15356203). Isoform 1
CC and isoform 2 are predominantly expressed at equal levels in brain.
CC Colocalizes with KCND3 in inhibitory interneurons in cortex and
CC hippocampus and in striatal interneurons. {ECO:0000269|PubMed:10676964,
CC ECO:0000269|PubMed:12646414, ECO:0000269|PubMed:15356203}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; AB046443; BAB03308.1; -; mRNA.
DR EMBL; AY082657; AAL92564.1; -; mRNA.
DR EMBL; AY082658; AAL92565.1; -; mRNA.
DR EMBL; AY142709; AAN34942.1; -; mRNA.
DR RefSeq; NP_001248318.1; NM_001261389.1. [Q8R426-1]
DR RefSeq; NP_075218.2; NM_022929.2. [Q8R426-2]
DR PDB; 1S6C; X-ray; 2.00 A; A=45-227.
DR PDBsum; 1S6C; -.
DR AlphaFoldDB; Q8R426; -.
DR SMR; Q8R426; -.
DR BioGRID; 249216; 1.
DR CORUM; Q8R426; -.
DR IntAct; Q8R426; 1.
DR STRING; 10116.ENSRNOP00000007187; -.
DR PaxDb; Q8R426; -.
DR ABCD; Q8R426; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000007187; ENSRNOP00000007187; ENSRNOG00000005365. [Q8R426-1]
DR Ensembl; ENSRNOT00000083090; ENSRNOP00000074006; ENSRNOG00000005365. [Q8R426-2]
DR GeneID; 65023; -.
DR KEGG; rno:65023; -.
DR UCSC; RGD:70886; rat. [Q8R426-1]
DR CTD; 30820; -.
DR RGD; 70886; Kcnip1.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158048; -.
DR InParanoid; Q8R426; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q8R426; -.
DR TreeFam; TF318560; -.
DR Reactome; R-RNO-5576894; Phase 1 - inactivation of fast Na+ channels.
DR ChiTaRS; Kcnip1; rat.
DR EvolutionaryTrace; Q8R426; -.
DR PRO; PR:Q8R426; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Genevisible; Q8R426; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0034705; C:potassium channel complex; IDA:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0045760; P:positive regulation of action potential; IDA:RGD.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISS: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; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane;
KW Cell projection; Cytoplasm; Ion channel; Ion transport; Membrane;
KW Metal-binding; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Repeat; Transport; Voltage-gated channel.
FT CHAIN 1..227
FT /note="Kv channel-interacting protein 1"
FT /id="PRO_0000073820"
FT DOMAIN 38..94
FT /note="EF-hand 1; degenerate"
FT /evidence="ECO:0000305"
FT DOMAIN 97..132
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 133..168
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 181..216
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 214..227
FT /note="Interaction with KCND2"
FT /evidence="ECO:0000269|PubMed:14980206"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:14980206"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:14980206"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:14980206"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:14980206"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:14980206"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:14980206"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:14980206"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:14980206"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:14980206"
FT VAR_SEQ 21..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11263977, ECO:0000303|Ref.2"
FT /id="VSP_015048"
FT MUTAGEN 214..227
FT /note="Missing: Abolishes interaction with KCND2."
FT /evidence="ECO:0000269|PubMed:14980206"
FT CONFLICT 10
FT /note="S -> P (in Ref. 3; AAN34942)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="D -> E (in Ref. 1; BAB03308)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="N -> D (in Ref. 2; AAL92564/AAL92565)"
FT /evidence="ECO:0000305"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:1S6C"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:1S6C"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1S6C"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:1S6C"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:1S6C"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:1S6C"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:1S6C"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:1S6C"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:1S6C"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1S6C"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:1S6C"
FT HELIX 215..227
FT /evidence="ECO:0007829|PDB:1S6C"
SQ SEQUENCE 227 AA; 26817 MW; 92A2F0D72A120197 CRC64;
MGAVMGTFSS LQTKQRRPSK DIAWWYYQYQ RDKIEDDLEM TMVCHRPEGL EQLEAQTNFT
KRELQVLYRG FKNECPSGVV NEETFKQIYA QFFPHGDAST YAHYLFNAFD TTQTGSVKFE
DFVTALSILL RGTVHEKLRW TFNLYDINKD GYINKEEMMD IVKAIYDMMG KYTYPVLKED
TPRQHVDVFF QKMDKNKDGI VTLDEFLESC QEDDNIMRSL QLFQNVM
