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 24-JAN-2024, entry version 166. 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}; 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; 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.ENSMUSP00000104964; -. DR PaxDb; 10090-ENSMUSP00000069063; -. 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; 345 antibodies from 30 providers. DR DNASU; 70357; -. DR Ensembl; ENSMUST00000065970.6; ENSMUSP00000069063.6; ENSMUSG00000053519.18. [Q9JJ57-2] DR Ensembl; ENSMUST00000101368.9; ENSMUSP00000098919.3; ENSMUSG00000053519.18. [Q9JJ57-3] DR Ensembl; ENSMUST00000109340.9; ENSMUSP00000104964.3; ENSMUSG00000053519.18. [Q9JJ57-1] DR GeneID; 70357; -. DR KEGG; mmu:70357; -. DR UCSC; uc007ikp.2; mouse. [Q9JJ57-1] DR AGR; MGI:1917607; -. 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; YRGFKNX; -. DR OrthoDB; 339700at2759; -. 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 78 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 138 other cell types or tissues. DR ExpressionAtlas; Q9JJ57; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0043025; C:neuronal cell body; 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:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI. 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 Gene3D; 1.10.238.10; EF-hand; 1. 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; CALCIUM BINDING PROTEINS; 1. DR PANTHER; PTHR23055:SF82; KV CHANNEL-INTERACTING PROTEIN 1; 1. DR Pfam; PF13499; EF-hand_7; 1. DR Pfam; PF13833; EF-hand_8; 1. DR PRINTS; PR00450; RECOVERIN. DR SMART; SM00054; EFh; 3. DR SUPFAM; SSF47473; EF-hand; 1. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 3. DR Genevisible; Q9JJ57; MM. 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 //