KCIP1_HUMAN
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 03-AUG-2022, entry version 176.
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}.
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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 PDBsum; 1S1E; -.
DR PDBsum; 2I2R; -.
DR PDBsum; 2NZ0; -.
DR PDBsum; 7E83; -.
DR PDBsum; 7E84; -.
DR PDBsum; 7F3F; -.
DR AlphaFoldDB; Q9NZI2; -.
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 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 PaxDb; Q9NZI2; -.
DR PeptideAtlas; Q9NZI2; -.
DR PRIDE; 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; 313 antibodies from 30 providers.
DR DNASU; 30820; -.
DR Ensembl; ENST00000328939.9; ENSP00000329686.4; ENSG00000182132.14. [Q9NZI2-2]
DR Ensembl; ENST00000377360.8; ENSP00000366577.4; ENSG00000182132.14. [Q9NZI2-4]
DR Ensembl; ENST00000411494.5; ENSP00000395323.1; ENSG00000182132.14. [Q9NZI2-1]
DR Ensembl; ENST00000434108.5; ENSP00000414886.1; ENSG00000182132.14. [Q9NZI2-5]
DR Ensembl; ENST00000520740.5; ENSP00000431102.1; ENSG00000182132.14. [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 CTD; 30820; -.
DR DisGeNET; 30820; -.
DR GeneCards; KCNIP1; -.
DR HGNC; HGNC:15521; KCNIP1.
DR HPA; ENSG00000182132; Tissue enhanced (brain, choroid plexus, epididymis).
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; IHEKLRW; -.
DR OrthoDB; 1271942at2759; -.
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; 9 hits in 1072 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 100 other tissues.
DR ExpressionAtlas; Q9NZI2; baseline and differential.
DR Genevisible; Q9NZI2; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
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:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
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; 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_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
