CSEN_HUMAN
ID CSEN_HUMAN Reviewed; 256 AA.
AC Q9Y2W7; H7BY46; Q3YAC3; Q3YAC4; Q53TJ5; Q96T40; Q9UJ84; Q9UJ85;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Calsenilin;
DE AltName: Full=A-type potassium channel modulatory protein 3;
DE AltName: Full=DRE-antagonist modulator;
DE Short=DREAM;
DE AltName: Full=Kv channel-interacting protein 3;
DE Short=KChIP3;
GN Name=KCNIP3; Synonyms=CSEN, DREAM, KCHIP3;
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 1), AND FUNCTION IN PRESENILIN
RP REGULATION.
RX PubMed=9771752; DOI=10.1038/2673;
RA Buxbaum J.D., Choi E.K., Luo Y., Lilliehook C., Crowley A.C., Merriam D.E.,
RA Wasco W.;
RT "Calsenilin: a calcium-binding protein that interacts with the presenilins
RT and regulates the levels of a presenilin fragment.";
RL Nat. Med. 4:1177-1181(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION IN TRANSCRIPTION
RP REGULATION.
RC TISSUE=Caudate nucleus;
RX PubMed=10078534; DOI=10.1038/18044;
RA Carrion A.M., Link W.A., Ledo F., Mellstrom B., Naranjo J.R.;
RT "DREAM is a Ca2+-regulated transcriptional repressor.";
RL Nature 398:80-84(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION IN POTASSIUM
RP TRANSPORT.
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND ALTERNATIVE 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 [MRNA] (ISOFORM 2).
RA Isbrandt D., Pongs O.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [8]
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 [9]
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 [10]
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP INTERACTION WITH PSEN2, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND
RP MUTAGENESIS OF ASP-61 AND ASP-64.
RX PubMed=11278424; DOI=10.1074/jbc.m008597200;
RA Choi E.K., Zaidi N.F., Miller J.S., Crowley A.C., Merriam D.E.,
RA Lilliehook C., Buxbaum J.D., Wasco W.;
RT "Calsenilin is a substrate for caspase-3 that preferentially interacts with
RT the familial Alzheimer's disease-associated C-terminal fragment of
RT presenilin 2.";
RL J. Biol. Chem. 276:19197-19204(2001).
RN [12]
RP FUNCTION IN APOPTOSIS.
RX PubMed=11259376; DOI=10.1096/fj.00-0541fje;
RA Jo D.G., Kim M.J., Choi Y.H., Kim I.K., Song Y.H., Woo H.N., Chung C.W.,
RA Jung Y.K.;
RT "Pro-apoptotic function of calsenilin/DREAM/KChIP3.";
RL FASEB J. 15:589-591(2001).
RN [13]
RP FUNCTION IN APOPTOSIS.
RX PubMed=11988022; DOI=10.1006/mcne.2001.1096;
RA Lilliehook C., Chan S., Choi E.K., Zaidi N.F., Wasco W., Mattson M.P.,
RA Buxbaum J.D.;
RT "Calsenilin enhances apoptosis by altering endoplasmic reticulum calcium
RT signaling.";
RL Mol. Cell. Neurosci. 19:552-559(2002).
RN [14]
RP FUNCTION IN POTASSIUM TRANSPORT.
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 [15]
RP PHOSPHORYLATION AT SER-63.
RX PubMed=12837631; DOI=10.1016/s1044-7431(03)00072-1;
RA Choi E.K., Miller J.S., Zaidi N.F., Salih E., Buxbaum J.D., Wasco W.;
RT "Phosphorylation of calsenilin at Ser63 regulates its cleavage by caspase-
RT 3.";
RL Mol. Cell. Neurosci. 23:495-506(2003).
RN [16]
RP INTERACTION WITH KCND2, FUNCTION IN POTASSIUM TRANSPORT, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15485870; DOI=10.1074/jbc.m409721200;
RA Kunjilwar K., Strang C., DeRubeis D., Pfaffinger P.J.;
RT "KChIP3 rescues the functional expression of Shal channel tetramerization
RT mutants.";
RL J. Biol. Chem. 279:54542-54551(2004).
RN [17]
RP TISSUE SPECIFICITY.
RX PubMed=14720210; DOI=10.1111/j.1471-4159.2004.02159.x;
RA Jo D.G., Lee J.Y., Hong Y.M., Song S., Mook-Jung I., Koh J.Y., Jung Y.K.;
RT "Induction of pro-apoptotic calsenilin/DREAM/KChIP3 in Alzheimer's disease
RT and cultured neurons after amyloid-beta exposure.";
RL J. Neurochem. 88:604-611(2004).
RN [18]
RP FUNCTION IN POTASSIUM TRANSPORT.
RX PubMed=16123112; DOI=10.1113/jphysiol.2005.087858;
RA Jerng H.H., Kunjilwar K., Pfaffinger P.J.;
RT "Multiprotein assembly of Kv4.2, KChIP3 and DPP10 produces ternary channel
RT complexes with ISA-like properties.";
RL J. Physiol. (Lond.) 568:767-788(2005).
RN [19]
RP FUNCTION IN POTASSIUM TRANSPORT, INTERACTION WITH KCND2, AND SUBCELLULAR
RP LOCATION.
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 [20]
RP SUMOYLATION AT LYS-26 AND LYS-90, AND SUBCELLULAR LOCATION.
RX PubMed=21070824; DOI=10.1016/j.bbamcr.2010.11.001;
RA Palczewska M., Casafont I., Ghimire K., Rojas A.M., Valencia A.,
RA Lafarga M., Mellstrom B., Naranjo J.R.;
RT "Sumoylation regulates nuclear localization of repressor DREAM.";
RL Biochim. Biophys. Acta 1813:1050-1058(2011).
RN [21]
RP STRUCTURE BY NMR OF 161-256, SUBUNIT, AND CALCIUM-BINDING.
RX PubMed=17962406; DOI=10.1110/ps.072928007;
RA Yu L., Sun C., Mendoza R., Wang J., Matayoshi E.D., Hebert E.,
RA Pereda-Lopez A., Hajduk P.J., Olejniczak E.T.;
RT "Solution structure and calcium-binding properties of EF-hands 3 and 4 of
RT calsenilin.";
RL Protein Sci. 16:2502-2509(2007).
RN [22]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-170 AND TYR-179.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Calcium-dependent transcriptional repressor that binds to the
CC DRE element of genes including PDYN and FOS. Affinity for DNA is
CC reduced upon binding to calcium and enhanced by binding to magnesium.
CC Seems to be involved in nociception (By similarity).
CC {ECO:0000250|UniProtKB:Q9QXT8}.
CC -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly
CC inactivating A-type potassium channels, such as KCND2/Kv4.2 and
CC KCND3/Kv4.3. Modulates channel expression at the cell membrane, gating
CC characteristics, inactivation kinetics and rate of recovery from
CC inactivation in a calcium-dependent and isoform-specific manner.
CC {ECO:0000269|PubMed:10676964, ECO:0000269|PubMed:12829703,
CC ECO:0000269|PubMed:15485870, ECO:0000269|PubMed:16123112,
CC ECO:0000269|PubMed:18957440}.
CC -!- FUNCTION: May play a role in the regulation of PSEN2 proteolytic
CC processing and apoptosis. Together with PSEN2 involved in modulation of
CC amyloid-beta formation. {ECO:0000269|PubMed:11259376,
CC ECO:0000269|PubMed:11988022, ECO:0000269|PubMed:9771752}.
CC -!- SUBUNIT: Binds to DNA as a homomultimer. Dimerization is induced by
CC binding to calcium (PubMed:17962406). Interacts with the C-terminus of
CC PSEN1 and PSEN2 and with PSEN2 CTF subunit. Associates with KCN1.
CC Component of heteromultimeric potassium channels. Identified in
CC potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1,
CC KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (By similarity). Interacts with
CC KCND2 and KCND3. {ECO:0000250|UniProtKB:Q9QXT8,
CC ECO:0000269|PubMed:11278424, ECO:0000269|PubMed:15485870,
CC ECO:0000269|PubMed:17962406, ECO:0000269|PubMed:18957440}.
CC -!- INTERACTION:
CC Q9Y2W7; P05067: APP; NbExp=3; IntAct=EBI-751501, EBI-77613;
CC Q9Y2W7; Q12797-6: ASPH; NbExp=3; IntAct=EBI-751501, EBI-12092171;
CC Q9Y2W7; Q9BXJ5: C1QTNF2; NbExp=3; IntAct=EBI-751501, EBI-2817707;
CC Q9Y2W7; Q8N6Q3: CD177; NbExp=9; IntAct=EBI-751501, EBI-747170;
CC Q9Y2W7; O14843: FFAR3; NbExp=3; IntAct=EBI-751501, EBI-17762181;
CC Q9Y2W7; Q7Z5G4: GOLGA7; NbExp=3; IntAct=EBI-751501, EBI-4403685;
CC Q9Y2W7; P08069: IGF1R; NbExp=6; IntAct=EBI-751501, EBI-475981;
CC Q9Y2W7; P40189: IL6ST; NbExp=7; IntAct=EBI-751501, EBI-1030834;
CC Q9Y2W7; Q17RA0: IL6ST; NbExp=3; IntAct=EBI-751501, EBI-10238517;
CC Q9Y2W7; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-751501, EBI-9089060;
CC Q9Y2W7; P57682: KLF3; NbExp=3; IntAct=EBI-751501, EBI-8472267;
CC Q9Y2W7; Q7Z434: MAVS; NbExp=3; IntAct=EBI-751501, EBI-995373;
CC Q9Y2W7; Q8WZ73-3: RFFL; NbExp=3; IntAct=EBI-751501, EBI-25839575;
CC Q9Y2W7; P08865: RPSA; NbExp=3; IntAct=EBI-751501, EBI-354112;
CC Q9Y2W7; P08294: SOD3; NbExp=6; IntAct=EBI-751501, EBI-10195782;
CC Q9Y2W7; Q86TD4-2: SRL; NbExp=3; IntAct=EBI-751501, EBI-12304565;
CC Q9Y2W7; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-751501, EBI-12090309;
CC Q9Y2W7; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-751501, EBI-9089156;
CC Q9Y2W7; O60844: ZG16; NbExp=3; IntAct=EBI-751501, EBI-746479;
CC Q9Y2W7; A0A1U9X8X8; NbExp=3; IntAct=EBI-751501, EBI-17234977;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18957440}. Cell
CC membrane {ECO:0000269|PubMed:15485870, ECO:0000269|PubMed:18957440};
CC Lipid-anchor {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:11278424, ECO:0000269|PubMed:18957440}. Golgi
CC apparatus {ECO:0000269|PubMed:11278424}. Nucleus
CC {ECO:0000269|PubMed:21070824}. Note=Also membrane-bound, associated
CC with the plasma membrane (PubMed:15485870). In the presence of PSEN2
CC associated with the endoplasmic reticulum and Golgi. The sumoylated
CC form is present only in the nucleus. {ECO:0000269|PubMed:11278424,
CC ECO:0000269|PubMed:15485870, ECO:0000269|PubMed:21070824}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=KChIP3.1;
CC IsoId=Q9Y2W7-1; Sequence=Displayed;
CC Name=2; Synonyms=KChIP3.2, KChIP4.2;
CC IsoId=Q9Y2W7-2; Sequence=VSP_015040;
CC Name=3; Synonyms=KChip3.x;
CC IsoId=Q9Y2W7-3; Sequence=VSP_040982, VSP_040983;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Widely expressed at
CC lower levels. Expression levels are elevated in brain cortex regions
CC affected by Alzheimer disease. {ECO:0000269|PubMed:14720210}.
CC -!- PTM: Palmitoylated. Palmitoylation enhances association with the plasma
CC membrane (By similarity). {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved by caspase-3.
CC {ECO:0000269|PubMed:11278424}.
CC -!- PTM: Phosphorylation at Ser-63 inhibits cleavage by CASP3.
CC {ECO:0000269|PubMed:11278424, ECO:0000269|PubMed:12837631}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; AF120102; AAD20350.1; -; mRNA.
DR EMBL; AJ131730; CAB56836.1; -; mRNA.
DR EMBL; AJ131730; CAB56835.1; -; mRNA.
DR EMBL; AF199599; AAF33684.1; -; mRNA.
DR EMBL; DQ148485; AAZ77802.1; -; mRNA.
DR EMBL; DQ148486; AAZ77803.1; -; mRNA.
DR EMBL; AF367022; AAK53711.1; -; mRNA.
DR EMBL; BT020075; AAV38878.1; -; mRNA.
DR EMBL; AK315437; BAG37825.1; -; mRNA.
DR EMBL; AC009238; AAY14752.1; -; Genomic_DNA.
DR EMBL; CH471219; EAX10724.1; -; Genomic_DNA.
DR EMBL; BC012850; AAH12850.1; -; mRNA.
DR CCDS; CCDS2013.1; -. [Q9Y2W7-1]
DR CCDS; CCDS33245.1; -. [Q9Y2W7-3]
DR RefSeq; NP_001030086.1; NM_001034914.1. [Q9Y2W7-3]
DR RefSeq; NP_038462.1; NM_013434.4. [Q9Y2W7-1]
DR PDB; 2E6W; NMR; -; A=161-256.
DR PDBsum; 2E6W; -.
DR AlphaFoldDB; Q9Y2W7; -.
DR SMR; Q9Y2W7; -.
DR BioGRID; 119042; 33.
DR IntAct; Q9Y2W7; 24.
DR STRING; 9606.ENSP00000295225; -.
DR TCDB; 8.A.82.2.5; the calmodulin calcium binding protein (calmodulin) family.
DR iPTMnet; Q9Y2W7; -.
DR PhosphoSitePlus; Q9Y2W7; -.
DR BioMuta; KCNIP3; -.
DR DMDM; 13431428; -.
DR MassIVE; Q9Y2W7; -.
DR PaxDb; Q9Y2W7; -.
DR PeptideAtlas; Q9Y2W7; -.
DR PRIDE; Q9Y2W7; -.
DR ProteomicsDB; 43500; -.
DR ProteomicsDB; 85919; -. [Q9Y2W7-1]
DR ProteomicsDB; 85920; -. [Q9Y2W7-2]
DR ProteomicsDB; 85921; -. [Q9Y2W7-3]
DR ABCD; Q9Y2W7; 2 sequenced antibodies.
DR Antibodypedia; 4181; 546 antibodies from 41 providers.
DR DNASU; 30818; -.
DR Ensembl; ENST00000295225.10; ENSP00000295225.5; ENSG00000115041.13. [Q9Y2W7-1]
DR Ensembl; ENST00000468529.1; ENSP00000417499.1; ENSG00000115041.13. [Q9Y2W7-3]
DR GeneID; 30818; -.
DR KEGG; hsa:30818; -.
DR MANE-Select; ENST00000295225.10; ENSP00000295225.5; NM_013434.5; NP_038462.1.
DR UCSC; uc002sup.4; human. [Q9Y2W7-1]
DR CTD; 30818; -.
DR DisGeNET; 30818; -.
DR GeneCards; KCNIP3; -.
DR HGNC; HGNC:15523; KCNIP3.
DR HPA; ENSG00000115041; Low tissue specificity.
DR MIM; 604662; gene.
DR neXtProt; NX_Q9Y2W7; -.
DR OpenTargets; ENSG00000115041; -.
DR PharmGKB; PA26934; -.
DR VEuPathDB; HostDB:ENSG00000115041; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158782; -.
DR HOGENOM; CLU_072366_2_2_1; -.
DR InParanoid; Q9Y2W7; -.
DR OMA; NIFHPET; -.
DR PhylomeDB; Q9Y2W7; -.
DR TreeFam; TF318560; -.
DR PathwayCommons; Q9Y2W7; -.
DR Reactome; R-HSA-5576894; Phase 1 - inactivation of fast Na+ channels.
DR SignaLink; Q9Y2W7; -.
DR SIGNOR; Q9Y2W7; -.
DR BioGRID-ORCS; 30818; 22 hits in 1077 CRISPR screens.
DR ChiTaRS; KCNIP3; human.
DR EvolutionaryTrace; Q9Y2W7; -.
DR GeneWiki; Calsenilin; -.
DR GenomeRNAi; 30818; -.
DR Pharos; Q9Y2W7; Tbio.
DR PRO; PR:Q9Y2W7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y2W7; protein.
DR Bgee; ENSG00000115041; Expressed in right frontal lobe and 108 other tissues.
DR ExpressionAtlas; Q9Y2W7; baseline and differential.
DR Genevisible; Q9Y2W7; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL.
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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
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 GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; Apoptosis; Calcium; Cell membrane;
KW Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Ion channel;
KW Ion transport; Isopeptide bond; Lipoprotein; Membrane; Metal-binding;
KW Nucleus; Palmitate; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transport; Ubl conjugation;
KW Voltage-gated channel.
FT CHAIN 1..256
FT /note="Calsenilin"
FT /id="PRO_0000073814"
FT DOMAIN 67..123
FT /note="EF-hand 1; degenerate"
FT /evidence="ECO:0000305"
FT DOMAIN 126..161
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 162..197
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 210..245
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..256
FT /note="Interaction with KCND2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM47"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXT8"
FT MOD_RES 63
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:12837631"
FT LIPID 45
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 46
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:21070824"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:21070824"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16112838"
FT /id="VSP_040982"
FT VAR_SEQ 27..60
FT /note="KEGIKWQRPRLSRQALMRCCLVKWILSSTAPQGS -> MGIQGMELCAMAVV
FT VLLFIAVLKQFGILEPISME (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16112838"
FT /id="VSP_040983"
FT VAR_SEQ 103..124
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_015040"
FT VARIANT 119
FT /note="A -> V (in dbSNP:rs35658670)"
FT /id="VAR_048663"
FT VARIANT 170
FT /note="A -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035463"
FT VARIANT 179
FT /note="D -> Y (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035464"
FT MUTAGEN 61
FT /note="D->A: Abolishes cleavage by caspase-3."
FT /evidence="ECO:0000269|PubMed:11278424"
FT MUTAGEN 64
FT /note="D->A: Abolishes cleavage by caspase-3."
FT /evidence="ECO:0000269|PubMed:11278424"
FT CONFLICT 182
FT /note="I -> V (in Ref. 2; CAB56836/CAB56835)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="R -> Q (in Ref. 2; CAB56836/CAB56835)"
FT /evidence="ECO:0000305"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:2E6W"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:2E6W"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:2E6W"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:2E6W"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:2E6W"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:2E6W"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:2E6W"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:2E6W"
SQ SEQUENCE 256 AA; 29231 MW; 635C3EDF8B91E1C5 CRC64;
MQPAKEVTKA SDGSLLGDLG HTPLSKKEGI KWQRPRLSRQ ALMRCCLVKW ILSSTAPQGS
DSSDSELELS TVRHQPEGLD QLQAQTKFTK KELQSLYRGF KNECPTGLVD EDTFKLIYAQ
FFPQGDATTY AHFLFNAFDA DGNGAIHFED FVVGLSILLR GTVHEKLKWA FNLYDINKDG
YITKEEMLAI MKSIYDMMGR HTYPILREDA PAEHVERFFE KMDRNQDGVV TIEEFLEACQ
KDENIMSSMQ LFENVI
