ID KCIP1_HUMAN Reviewed; 227 AA. AC Q9NZI2; A0A0C4DFQ7; B7Z7B4; Q3YAD0; Q3YAD1; Q3YAD2; Q3YAD3; Q5U822; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2005, sequence version 2. DT 24-JAN-2024, entry version 184. DE RecName: Full=Kv channel-interacting protein 1; DE Short=KChIP1 {ECO:0000303|PubMed:14572458}; DE AltName: Full=A-type potassium channel modulatory protein 1; DE AltName: Full=Potassium channel-interacting protein 1; DE AltName: Full=Vesicle APC-binding protein; GN Name=KCNIP1; Synonyms=KCHIP1, VABP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH KCND2, RP AND SUBCELLULAR LOCATION. 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain; RA Xia K., Fang H.Y., Zhong X.Y., Xia J.H., Zhang Z.H.; RT "Molecular cloning of human VABP gene."; RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 5), AND ALTERNATIVE RP SPLICING. RX PubMed=16112838; DOI=10.1016/j.ygeno.2005.07.001; RA Pruunsild P., Timmusk T.; RT "Structure, alternative splicing, and expression of the human and mouse RT KCNIP gene family."; RL Genomics 86:581-593(2005). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Zheng L., Jun X.X., Yue F.F., Min L.Y., Ming S.Y., Jun Y.F.; RT "Study on mutations in KCNIP1 gene."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; 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 [9] RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM RP 1), AND TISSUE SPECIFICITY (ISOFORMS 1 AND 2). 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 [10] RP FUNCTION. 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 [11] RP FUNCTION. RX PubMed=12829703; DOI=10.1074/jbc.m306142200; RA Shibata R., Misonou H., Campomanes C.R., Anderson A.E., Schrader L.A., RA Doliveira L.C., Carroll K.I., Sweatt J.D., Rhodes K.J., Trimmer J.S.; RT "A fundamental role for KChIPs in determining the molecular properties and RT trafficking of Kv4.2 potassium channels."; RL J. Biol. Chem. 278:36445-36454(2003). RN [12] RP INTERACTION WITH SNAKE CTX3. RX PubMed=15184042; DOI=10.1016/j.bbrc.2004.05.064; RA Lin Y.-L., Lin S.-R., Wu T.T., Chang L.-S.; RT "Evidence showing an intermolecular interaction between KChIP proteins and RT Taiwan cobra cardiotoxins."; RL Biochem. Biophys. Res. Commun. 319:720-724(2004). RN [13] RP INTERACTION WITH KCNIP2 AND KCDN2, AND HOMOOLIGOMERIZATION. RX PubMed=15358149; DOI=10.1016/j.bbrc.2004.07.006; RA Lin Y.-L., Chen C.Y., Cheng C.P., Chang L.S.; RT "Protein-protein interactions of KChIP proteins and Kv4.2."; RL Biochem. Biophys. Res. Commun. 321:606-610(2004). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) (ISOFORM 2), AND INTERACTION WITH RP KCDN2 AND KCDN3. RX PubMed=14980207; DOI=10.1016/s0896-6273(04)00049-2; RA Scannevin R.H., Wang K., Jow F., Megules J., Kopsco D.C., Edris W., RA Carroll K.C., Lu Q., Xu W., Xu Z., Katz A.H., Olland S., Lin L., Taylor M., RA Stahl M., Malakian K., Somers W., Mosyak L., Bowlby M.R., Chanda P., RA Rhodes K.J.; RT "Two N-terminal domains of Kv4 K(+) channels regulate binding to and RT modulation by KChIP1."; RL Neuron 41:587-598(2004). RN [15] RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 48-227 IN COMPLEX WITH CALCIUM RP IONS AND KCND3, SUBUNIT, AND CALCIUM-BINDING. RX PubMed=17057713; DOI=10.1038/nsmb1164; RA Pioletti M., Findeisen F., Hura G.L., Minor D.L. Jr.; RT "Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a RT cross-shaped octamer."; RL Nat. Struct. Mol. Biol. 13:987-995(2006). RN [16] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 49-227 IN COMPLEX WITH CALCIUM RP IONS AND KCND3, FUNCTION, AND SUBUNIT. RX PubMed=17187064; DOI=10.1038/nn1822; RA Wang H., Yan Y., Liu Q., Huang Y., Shen Y., Chen L., Chen Y., Yang Q., RA Hao Q., Wang K., Chai J.; RT "Structural basis for modulation of Kv4 K+ channels by auxiliary KChIP RT subunits."; RL Nat. Neurosci. 10:32-39(2007). 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. In vitro, modulates CC KCND1/Kv4.1 and KCND2/Kv4.2 currents. Increases the presence of KCND2 CC at the cell surface. {ECO:0000269|PubMed:10676964, CC ECO:0000269|PubMed:11423117, ECO:0000269|PubMed:12829703, CC ECO:0000269|PubMed:17187064}. 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). Part of a CC heterooctamer composed of the tetrameric channel and four KCNIP1 CC chains. 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. Self-associates to form homodimers and homotetramers. Interacts CC with KCNIP2 isoform 3 in a calcium-dependent manner. Interacts with CC Naja atra venom CTX3. {ECO:0000250|UniProtKB:Q9JJ57, CC ECO:0000269|PubMed:10676964, ECO:0000269|PubMed:14980207, CC ECO:0000269|PubMed:15184042, ECO:0000269|PubMed:15358149, CC ECO:0000269|PubMed:17057713, ECO:0000269|PubMed:17187064}. CC -!- INTERACTION: CC Q9NZI2; Q9NZV8: KCND2; NbExp=4; IntAct=EBI-2120635, EBI-1646745; CC Q9NZI2; Q9UK17: KCND3; NbExp=3; IntAct=EBI-2120635, EBI-9825212; CC Q9NZI2; Q9NS61-3: KCNIP2; NbExp=4; IntAct=EBI-2120635, EBI-1053010; CC Q9NZI2; Q62897: Kcnd3; Xeno; NbExp=3; IntAct=EBI-2120635, EBI-7082853; CC Q9NZI2-2; Q01432-4: AMPD3; NbExp=3; IntAct=EBI-22452746, EBI-11955621; CC Q9NZI2-2; Q12797-6: ASPH; NbExp=3; IntAct=EBI-22452746, EBI-12092171; CC Q9NZI2-2; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-22452746, EBI-752069; CC Q9NZI2-2; P40189: IL6ST; NbExp=3; IntAct=EBI-22452746, EBI-1030834; CC Q9NZI2-2; Q99732: LITAF; NbExp=3; IntAct=EBI-22452746, EBI-725647; CC Q9NZI2-2; Q02577: NHLH2; NbExp=3; IntAct=EBI-22452746, EBI-5378683; CC Q9NZI2-2; Q9GZT8: NIF3L1; NbExp=6; IntAct=EBI-22452746, EBI-740897; CC Q9NZI2-2; P08294: SOD3; NbExp=3; IntAct=EBI-22452746, EBI-10195782; CC Q9NZI2-2; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-22452746, EBI-7082156; CC Q9NZI2-2; Q3MII6: TBC1D25; NbExp=3; IntAct=EBI-22452746, EBI-11899977; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10676964}; CC Peripheral membrane protein {ECO:0000305|PubMed:10676964}. Cytoplasm CC {ECO:0000269|PubMed:10676964}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:Q8R426}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=KCHIP1b {ECO:0000303|PubMed:16112838}, KCNIP1-Ib CC {ECO:0000303|PubMed:16112838}; CC IsoId=Q9NZI2-1; Sequence=Displayed; CC Name=2; Synonyms=KCHIP1a {ECO:0000303|PubMed:16112838}, CC KCNIP1-IbdeltaII {ECO:0000303|PubMed:16112838}; CC IsoId=Q9NZI2-2; Sequence=VSP_015044; CC Name=3; CC IsoId=Q9NZI2-3; Sequence=VSP_015043; CC Name=4; Synonyms=KCNIP1-IadeltaII {ECO:0000303|PubMed:16112838}; CC IsoId=Q9NZI2-4; Sequence=VSP_041511; CC Name=5; CC IsoId=Q9NZI2-5; Sequence=VSP_015044, VSP_047687; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in brain and CC kidney. Isoform 1 is also expressed in liver, pancreas, skeletal CC muscle, small intestine and testis. Isoform 2 is also expressed in CC lung, pancreas, leukocytes, prostate and thymus. 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; AF199597; AAF33682.1; -; mRNA. DR EMBL; AY170821; AAN77491.1; -; mRNA. DR EMBL; DQ148476; AAZ77793.1; -; mRNA. DR EMBL; DQ148477; AAZ77794.1; -; mRNA. DR EMBL; DQ148478; AAZ77795.1; -; mRNA. DR EMBL; DQ148479; AAZ77796.1; -; mRNA. DR EMBL; AY780424; AAV51968.1; -; mRNA. DR EMBL; AK301775; BAH13550.1; -; mRNA. DR EMBL; AC008619; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC008719; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027306; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027312; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC034199; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC113432; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC134820; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF458055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW61470.1; -; Genomic_DNA. DR EMBL; BC050375; AAH50375.1; -; mRNA. DR CCDS; CCDS34285.1; -. [Q9NZI2-4] DR CCDS; CCDS34286.1; -. [Q9NZI2-1] DR CCDS; CCDS4374.1; -. [Q9NZI2-2] DR CCDS; CCDS64312.1; -. [Q9NZI2-5] DR CCDS; CCDS64313.1; -. [Q9NZI2-3] DR RefSeq; NP_001030009.1; NM_001034837.2. [Q9NZI2-1] DR RefSeq; NP_001030010.1; NM_001034838.2. [Q9NZI2-4] DR RefSeq; NP_001265268.1; NM_001278339.1. [Q9NZI2-5] DR RefSeq; NP_001265269.1; NM_001278340.1. [Q9NZI2-3] DR RefSeq; NP_055407.1; NM_014592.3. [Q9NZI2-2] DR RefSeq; XP_016864896.1; XM_017009407.1. [Q9NZI2-4] DR PDB; 1S1E; X-ray; 2.30 A; A=1-227. DR PDB; 2I2R; X-ray; 3.35 A; E/F/G/H/M/N/O/P=48-227. DR PDB; 2NZ0; X-ray; 3.20 A; A/C=49-227. DR PDB; 7E83; EM; 3.10 A; B/E/F/H=47-227. DR PDB; 7E84; EM; 3.10 A; E/H/J/L=47-227. DR PDB; 7F3F; EM; 3.10 A; E/H/J/L=1-227. DR PDB; 7W6N; EM; 3.40 A; A/C/E/G=1-227. DR PDB; 7W6T; EM; 3.85 A; A/C/E/G=1-227. DR PDBsum; 1S1E; -. DR PDBsum; 2I2R; -. DR PDBsum; 2NZ0; -. DR PDBsum; 7E83; -. DR PDBsum; 7E84; -. DR PDBsum; 7F3F; -. DR PDBsum; 7W6N; -. DR PDBsum; 7W6T; -. DR AlphaFoldDB; Q9NZI2; -. DR EMDB; EMD-31009; -. DR EMDB; EMD-31010; -. DR EMDB; EMD-31016; -. DR EMDB; EMD-31019; -. DR EMDB; EMD-31433; -. DR EMDB; EMD-32330; -. DR EMDB; EMD-32335; -. DR SMR; Q9NZI2; -. DR BioGRID; 119044; 25. DR ComplexPortal; CPX-3256; Kv4.3-KChIP1 channel complex. DR DIP; DIP-29246N; -. DR IntAct; Q9NZI2; 18. DR MINT; Q9NZI2; -. DR STRING; 9606.ENSP00000414886; -. DR TCDB; 8.A.82.2.6; the calmodulin calcium binding protein (calmodulin) family. DR BioMuta; KCNIP1; -. DR DMDM; 73621122; -. DR EPD; Q9NZI2; -. DR MassIVE; Q9NZI2; -. DR PeptideAtlas; Q9NZI2; -. DR ProteomicsDB; 61890; -. DR ProteomicsDB; 83400; -. [Q9NZI2-1] DR ProteomicsDB; 83401; -. [Q9NZI2-2] DR ProteomicsDB; 83402; -. [Q9NZI2-3] DR ProteomicsDB; 83403; -. [Q9NZI2-4] DR ABCD; Q9NZI2; 1 sequenced antibody. DR Antibodypedia; 16893; 345 antibodies from 30 providers. DR DNASU; 30820; -. DR Ensembl; ENST00000328939.9; ENSP00000329686.4; ENSG00000182132.15. [Q9NZI2-2] DR Ensembl; ENST00000377360.8; ENSP00000366577.4; ENSG00000182132.15. [Q9NZI2-4] DR Ensembl; ENST00000411494.5; ENSP00000395323.1; ENSG00000182132.15. [Q9NZI2-1] DR Ensembl; ENST00000434108.5; ENSP00000414886.1; ENSG00000182132.15. [Q9NZI2-5] DR Ensembl; ENST00000520740.5; ENSP00000431102.1; ENSG00000182132.15. [Q9NZI2-3] DR GeneID; 30820; -. DR KEGG; hsa:30820; -. DR MANE-Select; ENST00000328939.9; ENSP00000329686.4; NM_014592.4; NP_055407.1. [Q9NZI2-2] DR UCSC; uc003map.5; human. [Q9NZI2-1] DR AGR; HGNC:15521; -. DR CTD; 30820; -. DR DisGeNET; 30820; -. DR GeneCards; KCNIP1; -. DR HGNC; HGNC:15521; KCNIP1. DR HPA; ENSG00000182132; Group enriched (brain, epididymis). DR MalaCards; KCNIP1; -. DR MIM; 604660; gene. DR neXtProt; NX_Q9NZI2; -. DR OpenTargets; ENSG00000182132; -. DR PharmGKB; PA30041; -. DR VEuPathDB; HostDB:ENSG00000182132; -. DR GeneTree; ENSGT00940000158048; -. DR HOGENOM; CLU_072366_2_2_1; -. DR InParanoid; Q9NZI2; -. DR OMA; YRGFKNX; -. DR OrthoDB; 339700at2759; -. DR PhylomeDB; Q9NZI2; -. DR TreeFam; TF318560; -. DR PathwayCommons; Q9NZI2; -. DR Reactome; R-HSA-5576894; Phase 1 - inactivation of fast Na+ channels. DR SignaLink; Q9NZI2; -. DR BioGRID-ORCS; 30820; 10 hits in 1150 CRISPR screens. DR ChiTaRS; KCNIP1; human. DR EvolutionaryTrace; Q9NZI2; -. DR GeneWiki; KCNIP1; -. DR GenomeRNAi; 30820; -. DR Pharos; Q9NZI2; Tbio. DR PRO; PR:Q9NZI2; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q9NZI2; Protein. DR Bgee; ENSG00000182132; Expressed in nucleus accumbens and 102 other cell types or tissues. DR ExpressionAtlas; Q9NZI2; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IDA: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:0044325; F:transmembrane transporter binding; IBA:GO_Central. DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA: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; Q9NZI2; HS. 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_0000073818" 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 ECO:0000269|PubMed:17057713, ECO:0000269|PubMed:17187064" 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:17057713, ECO:0000269|PubMed:17187064" 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:17057713, ECO:0000269|PubMed:17187064" 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:17057713, ECO:0000269|PubMed:17187064" 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:17057713, ECO:0000269|PubMed:17187064" 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:17057713, ECO:0000269|PubMed:17187064" 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:17057713, ECO:0000269|PubMed:17187064" 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:17057713, ECO:0000269|PubMed:17187064" 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:17057713, ECO:0000269|PubMed:17187064" FT VAR_SEQ 1..39 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_015043" FT VAR_SEQ 1..31 FT /note="MGAVMGTFSSLQTKQRRPSKDIAWWYYQYQR -> MSGCSKRCKLGFVKFAQ FT TIFKLITGTLSK (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:16112838" FT /id="VSP_041511" FT VAR_SEQ 21..31 FT /note="Missing (in isoform 2 and isoform 5)" FT /evidence="ECO:0000303|PubMed:10676964, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16112838, FT ECO:0000303|Ref.2" FT /id="VSP_015044" FT VAR_SEQ 96 FT /note="G -> GALPCLEGSPCVEFLPPSPALLFCLV (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16112838" FT /id="VSP_047687" FT CONFLICT 116 FT /note="S -> P (in Ref. 5; BAH13550)" FT /evidence="ECO:0000305" FT HELIX 50..56 FT /evidence="ECO:0007829|PDB:1S1E" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:2NZ0" FT HELIX 61..74 FT /evidence="ECO:0007829|PDB:1S1E" FT STRAND 78..81 FT /evidence="ECO:0007829|PDB:7E83" FT HELIX 82..90 FT /evidence="ECO:0007829|PDB:1S1E" FT STRAND 93..96 FT /evidence="ECO:0007829|PDB:2NZ0" FT HELIX 99..109 FT /evidence="ECO:0007829|PDB:1S1E" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:7E83" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:7E83" FT HELIX 119..131 FT /evidence="ECO:0007829|PDB:1S1E" FT HELIX 134..145 FT /evidence="ECO:0007829|PDB:1S1E" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:7E83" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:1S1E" FT HELIX 155..169 FT /evidence="ECO:0007829|PDB:1S1E" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:1S1E" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:1S1E" FT HELIX 182..193 FT /evidence="ECO:0007829|PDB:1S1E" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:2NZ0" FT HELIX 203..211 FT /evidence="ECO:0007829|PDB:1S1E" FT HELIX 214..225 FT /evidence="ECO:0007829|PDB:1S1E" SQ SEQUENCE 227 AA; 26817 MW; D39DD5F8EA13B0FD CRC64; MGAVMGTFSS LQTKQRRPSK DIAWWYYQYQ RDKIEDELEM TMVCHRPEGL EQLEAQTNFT KRELQVLYRG FKNECPSGVV NEDTFKQIYA QFFPHGDAST YAHYLFNAFD TTQTGSVKFE DFVTALSILL RGTVHEKLRW TFNLYDINKD GYINKEEMMD IVKAIYDMMG KYTYPVLKED TPRQHVDVFF QKMDKNKDGI VTLDEFLESC QEDDNIMRSL QLFQNVM //