ID KCIP4_HUMAN Reviewed; 250 AA. AC Q6PIL6; Q3YAB8; Q3YAB9; Q3YAC0; Q3YAC1; Q3YAC2; Q4W5G8; Q8NEU0; Q9BWT2; AC Q9H294; Q9H2A4; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 162. DE RecName: Full=Kv channel-interacting protein 4; DE Short=KChIP4 {ECO:0000303|PubMed:11847232}; DE AltName: Full=A-type potassium channel modulatory protein 4; DE AltName: Full=Calsenilin-like protein {ECO:0000303|PubMed:11847232}; DE AltName: Full=Potassium channel-interacting protein 4; GN Name=KCNIP4; Synonyms=CALP, KCHIP4; 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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, INTERACTION WITH KCND2; PSEN1 AND PSEN2, AND RP CALCIUM-BINDING. RX PubMed=11847232; DOI=10.1074/jbc.m200897200; RA Morohashi Y., Hatano N., Ohya S., Takikawa R., Watabiki T., Takasugi N., RA Imaizumi Y., Tomita T., Iwatsubo T.; RT "Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand RT protein interacting with presenilin 2 and voltage-gated potassium channel RT subunit Kv4."; RL J. Biol. Chem. 277:14965-14975(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX PubMed=11805342; DOI=10.1073/pnas.022509299; RA Holmqvist M.H., Cao J., Hernandez-Pineda R., Jacobson M.D., Carroll K.I., RA Sung M.A., Betty M., Ge P., Gilbride K.J., Brown M.E., Jurman M.E., RA Lawson D., Silos-Santiago I., Xie Y., Covarrubias M., Rhodes K.J., RA Distefano P.S., An W.F.; RT "Elimination of fast inactivation in Kv4 A-type potassium channels by an RT auxiliary subunit domain."; RL Proc. Natl. Acad. Sci. U.S.A. 99:1035-1040(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4). RA Isbrandt D., Pongs O.; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hippocampus; 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=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [9] RP FUNCTION (ISOFORM 4), AND INTERACTION WITH KCND2. RX PubMed=18957440; DOI=10.1074/jbc.m806852200; RA Jerng H.H., Pfaffinger P.J.; RT "Multiple Kv channel-interacting proteins contain an N-terminal RT transmembrane domain that regulates Kv4 channel trafficking and gating."; RL J. Biol. Chem. 283:36046-36059(2008). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=22057399; DOI=10.1074/jbc.m111.301853; RA Kunze M., Neuberger G., Maurer-Stroh S., Ma J., Eck T., Braverman N., RA Schmid J.A., Eisenhaber F., Berger J.; RT "Structural requirements for interaction of peroxisomal targeting signal 2 RT and its receptor PEX7."; RL J. Biol. Chem. 286:45048-45062(2011). RN [11] RP FUNCTION (ISOFORM 4), AND SUBUNIT. RX PubMed=23576435; DOI=10.1074/jbc.m113.466052; RA Tang Y.Q., Liang P., Zhou J., Lu Y., Lei L., Bian X., Wang K.; RT "Auxiliary KChIP4a suppresses A-type K+ current through endoplasmic RT reticulum (ER) retention and promoting closed-state inactivation of Kv4 RT channels."; RL J. Biol. Chem. 288:14727-14741(2013). RN [12] RP INTERACTION WITH KCND2. RX PubMed=24811166; DOI=10.1074/jbc.m114.563452; RA Kitazawa M., Kubo Y., Nakajo K.; RT "The stoichiometry and biophysical properties of the Kv4 potassium channel RT complex with K+ channel-interacting protein (KChIP) subunits are variable, RT depending on the relative expression level."; RL J. Biol. Chem. 289:17597-17609(2014). CC -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly CC inactivating A-type potassium channels. Modulates KCND2 channel CC density, inactivation kinetics and rate of recovery from inactivation CC in a calcium-dependent and isoform-specific manner (PubMed:11847232, CC PubMed:18957440, PubMed:23576435). Modulates KCND3/Kv4.3 currents CC (PubMed:23576435). Isoform 4 does not increase KCND2 expression at the CC cell membrane (PubMed:18957440). Isoform 4 retains KCND3 in the CC endoplasmic reticulum and negatively regulates its expression at the CC cell membrane. {ECO:0000250|UniProtKB:Q6PHZ8, CC ECO:0000269|PubMed:11847232, ECO:0000269|PubMed:18957440, CC ECO:0000269|PubMed:23576435}. CC -!- SUBUNIT: Component of heteromultimeric potassium channels CC (PubMed:23576435). Identified in potassium channel complexes containing CC KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (By CC similarity). Interacts with KCND2 (PubMed:11847232, PubMed:18957440). CC Interacts with KCND3 (By similarity). Interacts with the C-terminus of CC PSEN2 and probably PSEN1 (PubMed:11847232). CC {ECO:0000250|UniProtKB:Q6PHZ8, ECO:0000269|PubMed:11847232, CC ECO:0000269|PubMed:18957440, ECO:0000269|PubMed:23576435, CC ECO:0000269|PubMed:24811166}. CC -!- INTERACTION: CC Q6PIL6; Q12797-6: ASPH; NbExp=3; IntAct=EBI-1051469, EBI-12092171; CC Q6PIL6; P08123: COL1A2; NbExp=9; IntAct=EBI-1051469, EBI-983038; CC Q6PIL6; Q7Z5G4: GOLGA7; NbExp=3; IntAct=EBI-1051469, EBI-4403685; CC Q6PIL6; Q16552: IL17A; NbExp=3; IntAct=EBI-1051469, EBI-10237926; CC Q6PIL6; Q99732: LITAF; NbExp=3; IntAct=EBI-1051469, EBI-725647; CC Q6PIL6; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1051469, EBI-16439278; CC Q6PIL6; P20396: TRH; NbExp=3; IntAct=EBI-1051469, EBI-12813975; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11847232}; CC Peripheral membrane protein {ECO:0000305|PubMed:11847232}. Cytoplasm CC {ECO:0000269|PubMed:11847232, ECO:0000269|PubMed:23576435}. Peroxisome CC {ECO:0000269|PubMed:22057399}. CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Endoplasmic reticulum CC {ECO:0000269|PubMed:23576435}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=KChIP4.1; CC IsoId=Q6PIL6-1; Sequence=Displayed; CC Name=2; Synonyms=KChIP4.2; CC IsoId=Q6PIL6-2; Sequence=VSP_015068; CC Name=3; Synonyms=KChIP4bs, KCHIP4.2; CC IsoId=Q6PIL6-3; Sequence=VSP_015066; CC Name=4; Synonyms=KChIP4a, KChIP4.4; CC IsoId=Q6PIL6-4; Sequence=VSP_015067; CC Name=5; CC IsoId=Q6PIL6-5; Sequence=VSP_043321; CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain. CC {ECO:0000269|PubMed:11847232}. CC -!- DOMAIN: The KIS (K-channel inactivation suppressor) domain is required CC for converting A-type Kv4 current to a slowly inactivating delayed CC rectifier potassium current. {ECO:0000250|UniProtKB:Q6PHZ8}. 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; AF302044; AAG36974.1; -; mRNA. DR EMBL; AF305072; AAG36977.1; -; mRNA. DR EMBL; AF453246; AAL86769.1; -; mRNA. DR EMBL; AF367023; AAK53712.1; -; mRNA. DR EMBL; AF367024; AAK53713.1; -; mRNA. DR EMBL; AY029176; AAK31594.1; -; mRNA. DR EMBL; AY118170; AAM81578.1; -; mRNA. DR EMBL; DQ148487; AAZ77804.1; -; mRNA. DR EMBL; DQ148488; AAZ77805.1; -; mRNA. DR EMBL; DQ148489; AAZ77806.1; -; mRNA. DR EMBL; DQ148490; AAZ77807.1; -; mRNA. DR EMBL; DQ148491; AAZ77808.1; -; mRNA. DR EMBL; AK289922; BAF82611.1; -; mRNA. DR EMBL; AC096576; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC097505; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC098597; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104065; AAY40911.1; -; Genomic_DNA. DR EMBL; AC107462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC108147; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC109360; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC109636; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC110296; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC110612; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC113606; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC116641; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471069; EAW92798.1; -; Genomic_DNA. DR EMBL; BC032520; AAH32520.1; -; mRNA. DR CCDS; CCDS3428.1; -. [Q6PIL6-4] DR CCDS; CCDS43215.1; -. [Q6PIL6-2] DR CCDS; CCDS43216.1; -. [Q6PIL6-1] DR CCDS; CCDS43217.1; -. [Q6PIL6-5] DR CCDS; CCDS47035.1; -. [Q6PIL6-3] DR RefSeq; NP_001030175.1; NM_001035003.1. [Q6PIL6-5] DR RefSeq; NP_001030176.1; NM_001035004.1. [Q6PIL6-3] DR RefSeq; NP_079497.2; NM_025221.5. [Q6PIL6-1] DR RefSeq; NP_671710.1; NM_147181.3. [Q6PIL6-2] DR RefSeq; NP_671711.1; NM_147182.3. [Q6PIL6-3] DR RefSeq; NP_671712.1; NM_147183.3. [Q6PIL6-4] DR RefSeq; XP_016864142.1; XM_017008653.1. DR AlphaFoldDB; Q6PIL6; -. DR BMRB; Q6PIL6; -. DR SMR; Q6PIL6; -. DR BioGRID; 123244; 24. DR CORUM; Q6PIL6; -. DR IntAct; Q6PIL6; 17. DR STRING; 9606.ENSP00000371587; -. DR TCDB; 8.A.82.2.2; the calmodulin calcium binding protein (calmodulin) family. DR iPTMnet; Q6PIL6; -. DR PhosphoSitePlus; Q6PIL6; -. DR BioMuta; KCNIP4; -. DR DMDM; 73621129; -. DR EPD; Q6PIL6; -. DR MassIVE; Q6PIL6; -. DR PaxDb; 9606-ENSP00000371587; -. DR PeptideAtlas; Q6PIL6; -. DR ProteomicsDB; 67166; -. [Q6PIL6-1] DR ProteomicsDB; 67167; -. [Q6PIL6-2] DR ProteomicsDB; 67168; -. [Q6PIL6-3] DR ProteomicsDB; 67169; -. [Q6PIL6-4] DR ProteomicsDB; 67170; -. [Q6PIL6-5] DR ABCD; Q6PIL6; 2 sequenced antibodies. DR Antibodypedia; 10064; 224 antibodies from 25 providers. DR DNASU; 80333; -. DR Ensembl; ENST00000382148.7; ENSP00000371583.3; ENSG00000185774.17. [Q6PIL6-5] DR Ensembl; ENST00000382150.8; ENSP00000371585.4; ENSG00000185774.17. [Q6PIL6-4] DR Ensembl; ENST00000382152.7; ENSP00000371587.2; ENSG00000185774.17. [Q6PIL6-1] DR Ensembl; ENST00000447367.6; ENSP00000399080.2; ENSG00000185774.17. [Q6PIL6-2] DR Ensembl; ENST00000509207.1; ENSP00000423257.1; ENSG00000185774.17. [Q6PIL6-3] DR GeneID; 80333; -. DR KEGG; hsa:80333; -. DR MANE-Select; ENST00000382152.7; ENSP00000371587.2; NM_025221.6; NP_079497.2. DR UCSC; uc003gqf.2; human. [Q6PIL6-1] DR AGR; HGNC:30083; -. DR CTD; 80333; -. DR DisGeNET; 80333; -. DR GeneCards; KCNIP4; -. DR HGNC; HGNC:30083; KCNIP4. DR HPA; ENSG00000185774; Tissue enhanced (brain, retina). DR MIM; 608182; gene. DR neXtProt; NX_Q6PIL6; -. DR OpenTargets; ENSG00000185774; -. DR PharmGKB; PA134893552; -. DR VEuPathDB; HostDB:ENSG00000185774; -. DR eggNOG; KOG0044; Eukaryota. DR GeneTree; ENSGT00940000158985; -. DR HOGENOM; CLU_072366_5_0_1; -. DR InParanoid; Q6PIL6; -. DR OMA; GXDFIKG; -. DR OrthoDB; 339700at2759; -. DR PhylomeDB; Q6PIL6; -. DR TreeFam; TF318560; -. DR PathwayCommons; Q6PIL6; -. DR Reactome; R-HSA-5576894; Phase 1 - inactivation of fast Na+ channels. DR SignaLink; Q6PIL6; -. DR SIGNOR; Q6PIL6; -. DR BioGRID-ORCS; 80333; 20 hits in 1150 CRISPR screens. DR ChiTaRS; KCNIP4; human. DR GenomeRNAi; 80333; -. DR Pharos; Q6PIL6; Tbio. DR PRO; PR:Q6PIL6; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q6PIL6; Protein. DR Bgee; ENSG00000185774; Expressed in lateral nuclear group of thalamus and 154 other cell types or tissues. DR ExpressionAtlas; Q6PIL6; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS: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; ISS:UniProtKB. DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB. 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:SF30; KV CHANNEL-INTERACTING PROTEIN 4; 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; 3. DR PROSITE; PS50222; EF_HAND_2; 3. DR Genevisible; Q6PIL6; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cell membrane; Cytoplasm; KW Endoplasmic reticulum; Ion channel; Ion transport; Membrane; Metal-binding; KW Peroxisome; Phosphoprotein; Potassium; Potassium channel; KW Potassium transport; Reference proteome; Repeat; Transport; KW Voltage-gated channel. FT CHAIN 1..250 FT /note="Kv channel-interacting protein 4" FT /id="PRO_0000073825" FT DOMAIN 61..117 FT /note="EF-hand 1; degenerate" FT /evidence="ECO:0000305" FT DOMAIN 120..155 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 156..191 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 204..239 FT /note="EF-hand 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REGION 2..44 FT /note="KIS" FT /evidence="ECO:0000250|UniProtKB:Q6PHZ8" FT REGION 237..250 FT /note="Interaction with KCND2" FT /evidence="ECO:0000250|UniProtKB:Q8R426" FT BINDING 133 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 135 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 137 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 144 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 169 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 171 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 173 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 175 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 180 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 217 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 219 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 221 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 228 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PHZ8" FT MOD_RES 56 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PHZ8" FT VAR_SEQ 1..62 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11805342, FT ECO:0000303|PubMed:16112838, ECO:0000303|Ref.3" FT /id="VSP_015066" FT VAR_SEQ 1..55 FT /note="MNVRRVESISAQLEEASSTGGFLYAQNSTKRSIKERLMKLLPCSAAKTSSPA FT IQN -> MNLEGLEMIAVLIVIVLFVKLLEQFGLIEAGLED (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16112838, ECO:0000303|Ref.3" FT /id="VSP_015067" FT VAR_SEQ 1..55 FT /note="MNVRRVESISAQLEEASSTGGFLYAQNSTKRSIKERLMKLLPCSAAKTSSPA FT IQN -> MSGCRKRCKREILKFAQYLLRLLTGSLHTD (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16112838" FT /id="VSP_043321" FT VAR_SEQ 21..55 FT /note="GFLYAQNSTKRSIKERLMKLLPCSAAKTSSPAIQN -> D (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:11847232, FT ECO:0000303|PubMed:16112838, ECO:0000303|Ref.3" FT /id="VSP_015068" FT CONFLICT 29 FT /note="T -> I (in Ref. 1; AAG36974 and 3; AAK53713)" FT /evidence="ECO:0000305" FT CONFLICT 32 FT /note="S -> N (in Ref. 1; AAG36974 and 3; AAK53713)" FT /evidence="ECO:0000305" SQ SEQUENCE 250 AA; 28729 MW; DC6C758D73468092 CRC64; MNVRRVESIS AQLEEASSTG GFLYAQNSTK RSIKERLMKL LPCSAAKTSS PAIQNSVEDE LEMATVRHRP EALELLEAQS KFTKKELQIL YRGFKNECPS GVVNEETFKE IYSQFFPQGD STTYAHFLFN AFDTDHNGAV SFEDFIKGLS ILLRGTVQEK LNWAFNLYDI NKDGYITKEE MLDIMKAIYD MMGKCTYPVL KEDAPRQHVE TFFQKMDKNK DGVVTIDEFI ESCQKDENIM RSMQLFENVI //