ID KCIP4_MOUSE Reviewed; 250 AA. AC Q6PHZ8; Q6DTJ3; Q8CAD0; Q8R4I2; Q9EQ01; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 16-SEP-2015, entry version 99. DE RecName: Full=Kv channel-interacting protein 4; DE Short=KChIP4; DE AltName: Full=A-type potassium channel modulatory protein 4; DE AltName: Full=Calsenilin-like protein; DE AltName: Full=Potassium channel-interacting protein 4; GN Name=Kcnip4; Synonyms=Calp, Kchip4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=11847232; DOI=10.1074/jbc.M200897200; RA Morohashi Y., Hatano N., Ohya S., Takikawa R., Watabiki T., RA Takasugi N., Imaizumi Y., Tomita T., Iwatsubo T.; RT "Molecular cloning and characterization of CALP/KChIP4, a novel EF- RT hand protein interacting with presenilin 2 and voltage-gated potassium RT channel subunit Kv4."; RL J. Biol. Chem. 277:14965-14975(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY, RP DOMAIN, AND INTERACTION WITH KCND2. RC STRAIN=C57BL/6J; RX PubMed=11805342; DOI=10.1073/pnas.022509299; RA Holmqvist M.H., Cao J., Hernandez-Pineda R., Jacobson M.D., RA Carroll K.I., Sung M.A., Betty M., Ge P., Gilbride K.J., Brown M.E., RA Jurman M.E., Lawson D., Silos-Santiago I., Xie Y., Covarrubias M., RA Rhodes K.J., Distefano P.S., An W.F.; RT "Elimination of fast inactivation in Kv4 A-type potassium channels by RT an auxiliary subunit domain."; RL Proc. Natl. Acad. Sci. U.S.A. 99:1035-1040(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). 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 [LARGE SCALE MRNA] (ISOFORM 4). RC STRAIN=C57BL/6J; TISSUE=Hypothalamus; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-192 (ISOFORM 2). RC TISSUE=Retina; RA Ida H., Boylan S., Weigel A., Smit-McBride Z., Chao A., Gao J., RA Buchoff P., Wistow G., Hjelmeland L.; RT "Expressed sequence tag analysis of mouse retina."; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] 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). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-56, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [10] RP INTERACTION WITH KCND2, AND FUNCTION. RX PubMed=20943905; DOI=10.1523/JNEUROSCI.2487-10.2010; RA Norris A.J., Foeger N.C., Nerbonne J.M.; RT "Interdependent roles for accessory KChIP2, KChIP3, and KChIP4 RT subunits in the generation of Kv4-encoded IA channels in cortical RT pyramidal neurons."; RL J. Neurosci. 30:13644-13655(2010). RN [11] RP FUNCTION, AND INTERACTION WITH KCND2. RX PubMed=20045463; DOI=10.1016/j.mcn.2009.12.005; RA Lin L., Sun W., Wikenheiser A.M., Kung F., Hoffman D.A.; RT "KChIP4a regulates Kv4.2 channel trafficking through PKA RT phosphorylation."; RL Mol. Cell. Neurosci. 43:315-325(2010). RN [12] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 56-250 IN COMPLEX WITH RP CALCIUM IONS, INTERACTION WITH KCND3/KV4.3, AND FUNCTION. RX PubMed=19109250; DOI=10.1074/jbc.M807704200; RA Liang P., Wang H., Chen H., Cui Y., Gu L., Chai J., Wang K.; RT "Structural insights into KChIP4a modulation of Kv4.3 inactivation."; RL J. Biol. Chem. 284:4960-4967(2009). CC -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated CC rapidly inactivating A-type potassium channels, such as CC KCND2/Kv4.2 and KCND3/Kv4.3 (PubMed:19109250). Modulates channel CC expression at the cell membrane, gating characteristics, CC inactivation kinetics and rate of recovery from inactivation in a CC calcium-dependent and isoform-specific manner. CC {ECO:0000269|PubMed:19109250, ECO:0000269|PubMed:20045463, CC ECO:0000269|PubMed:20943905}. CC -!- SUBUNIT: Component of heteromultimeric potassium channels CC (PubMed:19713751, PubMed:20943905). Identified in potassium CC channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, CC KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:19713751). Interacts with CC the C-terminus of PSEN2 and probably PSEN1 (By similarity). CC Interacts with KCND2 and KCND3. {ECO:0000250|UniProtKB:Q6PIL6, CC ECO:0000269|PubMed:11805342, ECO:0000269|PubMed:19109250, CC ECO:0000269|PubMed:20045463, ECO:0000269|PubMed:20943905}. CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000250|UniProtKB:Q6PIL6}; Peripheral membrane protein CC {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q6PIL6}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q6PHZ8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6PHZ8-2; Sequence=VSP_015071; CC Note=Derived from EST data. No experimental confirmation CC available.; CC Name=3; CC IsoId=Q6PHZ8-3; Sequence=VSP_015069; CC Name=4; Synonyms=KChIPa; CC IsoId=Q6PHZ8-4; Sequence=VSP_015070; CC -!- TISSUE SPECIFICITY: Expressed in brain. Highly expressed by CC neurons in layers II-IV of cortex and in hippocampus, thalamus and CC the Purkinje cell layer of the cerebellum. CC {ECO:0000269|PubMed:11805342, ECO:0000269|PubMed:11847232, CC ECO:0000269|PubMed:15363885}. CC -!- DOMAIN: The KIS (K-channel inactivation suppressor) domain is CC required for converting A-type Kv4 current to a slowly CC inactivating delayed rectifier potassium current. CC {ECO:0000269|PubMed:11805342}. CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 4 EF-hand domains. {ECO:0000255|PROSITE- CC ProRule:PRU00448}. 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; AF305071; AAG36976.1; -; mRNA. DR EMBL; AF453243; AAL86766.1; -; mRNA. DR EMBL; AY647240; AAT68466.1; -; mRNA. DR EMBL; AK039048; BAC30218.1; -; mRNA. DR EMBL; BC051130; AAH51130.1; -; mRNA. DR EMBL; CK618709; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS39084.1; -. [Q6PHZ8-4] DR CCDS; CCDS57341.1; -. [Q6PHZ8-2] DR CCDS; CCDS57342.1; -. [Q6PHZ8-1] DR RefSeq; NP_001186171.1; NM_001199242.1. [Q6PHZ8-1] DR RefSeq; NP_001186172.1; NM_001199243.1. [Q6PHZ8-2] DR RefSeq; NP_084541.3; NM_030265.3. [Q6PHZ8-4] DR UniGene; Mm.160172; -. DR PDB; 3DD4; X-ray; 3.00 A; A=56-250. DR PDBsum; 3DD4; -. DR ProteinModelPortal; Q6PHZ8; -. DR SMR; Q6PHZ8; 53-250. DR IntAct; Q6PHZ8; 1. DR MINT; MINT-4128953; -. DR STRING; 10090.ENSMUSP00000084656; -. DR MaxQB; Q6PHZ8; -. DR PaxDb; Q6PHZ8; -. DR PRIDE; Q6PHZ8; -. DR Ensembl; ENSMUST00000087395; ENSMUSP00000084656; ENSMUSG00000029088. [Q6PHZ8-1] DR Ensembl; ENSMUST00000176191; ENSMUSP00000135071; ENSMUSG00000029088. [Q6PHZ8-2] DR Ensembl; ENSMUST00000176978; ENSMUSP00000134758; ENSMUSG00000029088. [Q6PHZ8-4] DR GeneID; 80334; -. DR KEGG; mmu:80334; -. DR UCSC; uc033ijo.1; mouse. [Q6PHZ8-1] DR CTD; 80333; -. DR MGI; MGI:1933131; Kcnip4. DR eggNOG; COG5126; -. DR GeneTree; ENSGT00760000118820; -. DR HOGENOM; HOG000233019; -. DR HOVERGEN; HBG108179; -. DR InParanoid; Q6PHZ8; -. DR OrthoDB; EOG7GJ6F3; -. DR PhylomeDB; Q6PHZ8; -. DR TreeFam; TF318560; -. DR ChiTaRS; Kcnip4; mouse. DR EvolutionaryTrace; Q6PHZ8; -. DR NextBio; 350021; -. DR PRO; PR:Q6PHZ8; -. DR Proteomes; UP000000589; Chromosome 5. DR Bgee; Q6PHZ8; -. DR CleanEx; MM_KCNIP4; -. DR ExpressionAtlas; Q6PHZ8; baseline and differential. DR Genevisible; Q6PHZ8; MM. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. 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; IMP: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; IMP:UniProtKB. DR Gene3D; 1.10.238.10; -; 3. 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 SMART; SM00054; EFh; 3. DR PROSITE; PS00018; EF_HAND_1; 3. DR PROSITE; PS50222; EF_HAND_2; 3. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell membrane; KW Complete proteome; Cytoplasm; Ion channel; Ion transport; Membrane; KW Metal-binding; Phosphoprotein; Potassium; Potassium channel; KW Potassium transport; Reference proteome; Repeat; Transport; KW Voltage-gated channel. FT CHAIN 1 250 Kv channel-interacting protein 4. FT /FTId=PRO_0000073827. FT DOMAIN 61 117 EF-hand 1; degenerate. FT {ECO:0000255|PROSITE-ProRule:PRU00448}. FT DOMAIN 120 155 EF-hand 2. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 156 191 EF-hand 3. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 204 239 EF-hand 4. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT CA_BIND 133 144 1. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT CA_BIND 169 180 2. {ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:19109250}. FT CA_BIND 217 228 3. {ECO:0000255|PROSITE-ProRule:PRU00448, FT ECO:0000269|PubMed:19109250}. FT REGION 2 44 KIS. FT REGION 237 250 Interaction with KCND2. {ECO:0000250}. FT MOD_RES 17 17 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 56 56 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT VAR_SEQ 1 62 Missing (in isoform 3). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_015069. FT VAR_SEQ 1 55 MNVRRVESISAQLEEASSTGGFLYAQNNTKRSIKERLMKLL FT PCSAAKTSSPAIQN -> MNLEGLEMIAVLIVIVLFVKLLE FT QFGLIEAGLED (in isoform 4). FT {ECO:0000303|PubMed:11805342, FT ECO:0000303|PubMed:16141072}. FT /FTId=VSP_015070. FT VAR_SEQ 21 55 GFLYAQNNTKRSIKERLMKLLPCSAAKTSSPAIQN -> D FT (in isoform 2). {ECO:0000303|Ref.6}. FT /FTId=VSP_015071. FT CONFLICT 32 32 S -> T (in Ref. 1; AAG36976). FT {ECO:0000305}. FT CONFLICT 67 67 R -> K (in Ref. 4; BAC30218). FT {ECO:0000305}. FT HELIX 57 61 {ECO:0000244|PDB:3DD4}. FT HELIX 69 95 {ECO:0000244|PDB:3DD4}. FT HELIX 105 115 {ECO:0000244|PDB:3DD4}. FT STRAND 118 120 {ECO:0000244|PDB:3DD4}. FT HELIX 121 130 {ECO:0000244|PDB:3DD4}. FT HELIX 142 154 {ECO:0000244|PDB:3DD4}. FT HELIX 157 168 {ECO:0000244|PDB:3DD4}. FT HELIX 178 191 {ECO:0000244|PDB:3DD4}. FT HELIX 208 216 {ECO:0000244|PDB:3DD4}. FT STRAND 221 223 {ECO:0000244|PDB:3DD4}. FT HELIX 226 234 {ECO:0000244|PDB:3DD4}. FT HELIX 237 246 {ECO:0000244|PDB:3DD4}. SQ SEQUENCE 250 AA; 28756 MW; 56542298021192BF CRC64; MNVRRVESIS AQLEEASSTG GFLYAQNNTK RSIKERLMKL LPCSAAKTSS PAIQNSVEDE LEMATVRHRP EALELLEAQS KFTKKELQIL YRGFKNECPS GVVNEETFKE IYSQFFPQGD STTYAHFLFN AFDTDHNGAV SFEDFIKGLS ILLRGTVQEK LNWAFNLYDI NKDGYITKEE MLDIMKAIYD MMGKCTYPVL KEDAPRQHVE TFFQKMDKNK DGVVTIDEFI ESCQKDENIM RSMQLFENVI //