KCIP1_MOUSE
ID KCIP1_MOUSE Reviewed; 227 AA.
AC Q9JJ57; Q5SSA3; Q6DTJ1; Q8BGJ4; Q8C4K4; Q8CGL1; Q8K1U1; Q8K3M2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 158.
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 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] (ISOFORMS 1 AND 2), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=BALB/cJ;
RX PubMed=14572458; DOI=10.1016/s1044-7431(03)00174-x;
RA Van Hoorick D., Raes A., Keysers W., Mayeur E., Snyders D.J.;
RT "Differential modulation of Kv4 kinetics by KCHIP1 splice variants.";
RL Mol. Cell. Neurosci. 24:357-366(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Ohya S., Horowitz B.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Swiss Webster;
RA Xia K.U., Fang H.Y., Zhong X.Y., Xia J.H., Zhang Z.H.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=Swiss Webster;
RA Fang H.Y., Xia K., Xia J.H., Zhang Z.H.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Head;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-227 (ISOFORM 2).
RA Franz O., Soloviev M., Roeper J.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=15363885; DOI=10.1016/j.molbrainres.2004.06.024;
RA Xiong H., Kovacs I., Zhang Z.;
RT "Differential distribution of KChIPs mRNAs in adult mouse brain.";
RL Brain Res. Mol. Brain Res. 128:103-111(2004).
RN [10]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19713751; DOI=10.4161/chan.3.4.9553;
RA Marionneau C., LeDuc R.D., Rohrs H.W., Link A.J., Townsend R.R.,
RA Nerbonne J.M.;
RT "Proteomic analyses of native brain K(V)4.2 channel complexes.";
RL Channels 3:284-294(2009).
CC -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly
CC inactivating A-type potassium channels. Regulates channel density,
CC inactivation kinetics and rate of recovery from inactivation in a
CC calcium-dependent and isoform-specific manner. Modulates KCND2/Kv4.2
CC currents (PubMed:14572458). In vitro, modulates KCND1/Kv4.1 currents
CC (By similarity). Increases the presence of KCND2 at the cell surface.
CC {ECO:0000250|UniProtKB:Q9NZI2, ECO:0000269|PubMed:14572458}.
CC -!- SUBUNIT: Component of heteromultimeric potassium channels
CC (PubMed:19713751). Identified in potassium channel complexes containing
CC KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10
CC (PubMed:19713751). Part of a heterooctamer composed of the tetrameric
CC channel and four KCNIP1 chains (By similarity). Interacts with KCND3
CC and the N-terminal domain of KCND2. Probably part of a complex
CC consisting of KCNIP1, KCNIP2 isoform 3 and KCND2. Self-associates to
CC form homodimers and homotetramers. Interacts with KCNIP2 isoform 3 in a
CC calcium-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZI2, ECO:0000269|PubMed:19713751}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14572458};
CC Peripheral membrane protein {ECO:0000269|PubMed:14572458}. Cytoplasm
CC {ECO:0000269|PubMed:14572458}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q8R426}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=A, Kchip1.2, KCHIP1b;
CC IsoId=Q9JJ57-1; Sequence=Displayed;
CC Name=2; Synonyms=Kchip1.1, KCHP1a;
CC IsoId=Q9JJ57-2; Sequence=VSP_015047;
CC Name=3; Synonyms=Kchip1.2;
CC IsoId=Q9JJ57-3; Sequence=VSP_015045;
CC Name=4;
CC IsoId=Q9JJ57-4; Sequence=VSP_015046;
CC -!- TISSUE SPECIFICITY: Expressed in brain. Found in a subpopulation of
CC neurons widely distributed and enriched in Purkinje cells of the
CC cerebellum and in the reticular thalamic and medial habenular nuclei.
CC {ECO:0000269|PubMed:14572458, ECO:0000269|PubMed:15363885}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN77492.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY050525; AAL12488.1; -; mRNA.
DR EMBL; AY050526; AAL12489.1; -; mRNA.
DR EMBL; AB075041; BAB78543.1; -; mRNA.
DR EMBL; AY171234; AAN77492.1; ALT_INIT; mRNA.
DR EMBL; AY647242; AAT68468.1; -; mRNA.
DR EMBL; AK081845; BAC38347.1; -; mRNA.
DR EMBL; AK045948; BAC32543.1; -; mRNA.
DR EMBL; AK046398; BAC32705.1; -; mRNA.
DR EMBL; AL669814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034241; AAH34241.1; -; mRNA.
DR EMBL; AJ278534; CAC82025.1; -; mRNA.
DR CCDS; CCDS24537.1; -. [Q9JJ57-2]
DR CCDS; CCDS56766.1; -. [Q9JJ57-1]
DR CCDS; CCDS70160.1; -. [Q9JJ57-3]
DR RefSeq; NP_001177814.1; NM_001190885.1. [Q9JJ57-1]
DR RefSeq; NP_001177815.1; NM_001190886.1.
DR RefSeq; NP_001277619.1; NM_001290690.1. [Q9JJ57-3]
DR RefSeq; NP_081674.2; NM_027398.3. [Q9JJ57-2]
DR AlphaFoldDB; Q9JJ57; -.
DR SMR; Q9JJ57; -.
DR ComplexPortal; CPX-3262; Kv4.3-KChIP1 channel complex.
DR IntAct; Q9JJ57; 1.
DR MINT; Q9JJ57; -.
DR STRING; 10090.ENSMUSP00000069063; -.
DR PaxDb; Q9JJ57; -.
DR PRIDE; Q9JJ57; -.
DR ProteomicsDB; 269250; -. [Q9JJ57-1]
DR ProteomicsDB; 269251; -. [Q9JJ57-2]
DR ProteomicsDB; 269252; -. [Q9JJ57-3]
DR ProteomicsDB; 269253; -. [Q9JJ57-4]
DR ABCD; Q9JJ57; 1 sequenced antibody.
DR Antibodypedia; 16893; 313 antibodies from 30 providers.
DR DNASU; 70357; -.
DR Ensembl; ENSMUST00000065970; ENSMUSP00000069063; ENSMUSG00000053519. [Q9JJ57-2]
DR Ensembl; ENSMUST00000101368; ENSMUSP00000098919; ENSMUSG00000053519. [Q9JJ57-3]
DR Ensembl; ENSMUST00000109340; ENSMUSP00000104964; ENSMUSG00000053519. [Q9JJ57-1]
DR GeneID; 70357; -.
DR KEGG; mmu:70357; -.
DR UCSC; uc007ikp.2; mouse. [Q9JJ57-1]
DR CTD; 30820; -.
DR MGI; MGI:1917607; Kcnip1.
DR VEuPathDB; HostDB:ENSMUSG00000053519; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158048; -.
DR HOGENOM; CLU_072366_2_2_1; -.
DR InParanoid; Q9JJ57; -.
DR OMA; IHEKLRW; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q9JJ57; -.
DR TreeFam; TF318560; -.
DR Reactome; R-MMU-5576894; Phase 1 - inactivation of fast Na+ channels.
DR BioGRID-ORCS; 70357; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Kcnip1; mouse.
DR PRO; PR:Q9JJ57; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JJ57; protein.
DR Bgee; ENSMUSG00000053519; Expressed in habenula and 137 other tissues.
DR ExpressionAtlas; Q9JJ57; baseline and differential.
DR Genevisible; Q9JJ57; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0034705; C:potassium channel complex; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0045760; P:positive regulation of action potential; ISO:MGI.
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 Alternative splicing; Calcium; Cell membrane; Cell projection; Cytoplasm;
KW Ion channel; Ion transport; Membrane; Metal-binding; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Repeat;
KW Transport; Voltage-gated channel.
FT CHAIN 1..227
FT /note="Kv channel-interacting protein 1"
FT /id="PRO_0000073819"
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:0000250|UniProtKB:Q8R426"
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 BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 VAR_SEQ 1..39
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015045"
FT VAR_SEQ 1..18
FT /note="MGAVMGTFSSLQTKQRRP -> MSSCSKRCRLGFVKFAQTIFKLITGTL
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015046"
FT VAR_SEQ 21..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14572458,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.8"
FT /id="VSP_015047"
FT CONFLICT 147
FT /note="I -> L (in Ref. 1; AAL12488)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="H -> R (in Ref. 3; AAT68468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 26831 MW; 9256B5239A13B126 CRC64;
MGAVMGTFSS LQTKQRRPSK DIAWWYYQYQ RDKIEDELEM TMVCHRPEGL EQLEAQTNFT
KRELQVLYRG FKNECPSGVV NEETFKQIYA QFFPHGDAST YAHYLFNAFD TTQTGSVKFE
DFVTALSILL RGTVHEKLRW TFNLYDINKD GYINKEEMMD IVKAIYDMMG KYTYPVLKED
TPRQHVDVFF QKMDKNKDGI VTLDEFLESC QEDDNIMRSL QLFQNVM
