KCIP4_HUMAN
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 03-AUG-2022, entry version 154.
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 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 [11]
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}.
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}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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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. [Q6PIL6-3]
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; Q6PIL6; -.
DR PeptideAtlas; Q6PIL6; -.
DR PRIDE; 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; 199 antibodies from 25 providers.
DR DNASU; 80333; -.
DR Ensembl; ENST00000359001.9; ENSP00000351892.5; ENSG00000185774.16. [Q6PIL6-3]
DR Ensembl; ENST00000382148.7; ENSP00000371583.3; ENSG00000185774.16. [Q6PIL6-5]
DR Ensembl; ENST00000382150.8; ENSP00000371585.4; ENSG00000185774.16. [Q6PIL6-4]
DR Ensembl; ENST00000382152.7; ENSP00000371587.2; ENSG00000185774.16. [Q6PIL6-1]
DR Ensembl; ENST00000447367.6; ENSP00000399080.2; ENSG00000185774.16. [Q6PIL6-2]
DR Ensembl; ENST00000509207.1; ENSP00000423257.1; ENSG00000185774.16. [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 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; GMNLADD; -.
DR OrthoDB; 1513542at2759; -.
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 BioGRID-ORCS; 80333; 18 hits in 1072 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 153 other tissues.
DR ExpressionAtlas; Q6PIL6; baseline and differential.
DR Genevisible; Q6PIL6; HS.
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: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:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
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 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; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Endoplasmic reticulum; Ion channel; Ion transport; Membrane; Metal-binding;
KW Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Repeat; Transport; 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"
FT REGION 237..250
FT /note="Interaction with KCND2"
FT /evidence="ECO:0000250"
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
