ID CSEN_MOUSE Reviewed; 256 AA. AC Q9QXT8; Q924L0; Q99PH9; Q99PI0; Q99PI2; Q99PI3; Q9JHZ5; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2005, sequence version 2. DT 24-JAN-2024, entry version 178. 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 Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3), NUCLEOTIDE SEQUENCE [GENOMIC RP DNA], TISSUE SPECIFICITY, AND VARIANT SER-14. RC STRAIN=129/Ola, and C57BL/6J; RX PubMed=11161465; DOI=10.1006/mcne.2000.0913; RA Spreafico F., Barski J.J., Farina C., Meyer M.; RT "Mouse DREAM/calsenilin/KChIP3: gene structure, coding potential and RT expression."; RL Mol. Cell. Neurosci. 17:1-16(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Jo D.G., Kim M., Jung Y.K.; RT "Cloning and characterization of mouse calsenilin/DREAM."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-14. RC STRAIN=FVB/NJ; TISSUE=Brain; RA Deng L., Reid R.E., Leavitt B., Hayden M.R.; RT "Allele of Mus musculus Dream/calsenilin gene."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-14. RC STRAIN=BALB/cJ; RA Lee H.G., Choi J.K., Choi E.K., Wasco W., Buxbaum J.D., Beier D.R., RA Kim Y.S.; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Brain, Eye, and Olfactory epithelium; 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 [6] RP TISSUE SPECIFICITY. 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 [7] RP INTERACTION WITH KCND3. RX PubMed=11598014; DOI=10.1093/emboj/20.20.5715; RA Liss B., Franz O., Sewing S., Bruns R., Neuhoff H., Roeper J.; RT "Tuning pacemaker frequency of individual dopaminergic neurons by Kv4.3L RT and KChip3.1 transcription."; RL EMBO J. 20:5715-5724(2001). RN [8] RP FUNCTION. RX PubMed=11792319; DOI=10.1016/s0092-8674(01)00629-8; RA Cheng H.Y., Pitcher G.M., Laviolette S.R., Whishaw I.Q., Tong K.I., RA Kockeritz L.K., Wada T., Joza N.A., Crackower M., Goncalves J., Sarosi I., RA Woodgett J.R., Oliveira-dos-Santos A.J., Ikura M., van der Kooy D., RA Salter M.W., Penninger J.M.; RT "DREAM is a critical transcriptional repressor for pain modulation."; RL Cell 108:31-43(2002). RN [9] RP INTERACTION WITH KCND2. RX PubMed=12451113; DOI=10.1523/jneurosci.22-23-10123.2002; RA Schrader L.A., Anderson A.E., Mayne A., Pfaffinger P.J., Sweatt J.D.; RT "PKA modulation of Kv4.2-encoded A-type potassium channels requires RT formation of a supramolecular complex."; RL J. Neurosci. 22:10123-10133(2002). RN [10] RP TISSUE SPECIFICITY. RX PubMed=12646414; DOI=10.1152/ajpcell.00416.2002; RA Boland L.M., Jiang M., Lee S.Y., Fahrenkrug S.C., Harnett M.T., RA O'Grady S.M.; RT "Functional properties of a brain-specific NH2-terminally spliced modulator RT of Kv4 channels."; RL Am. J. Physiol. 285:C161-C170(2003). RN [11] RP FUNCTION. RX PubMed=14534243; DOI=10.1523/jneurosci.23-27-09097.2003; RA Lilliehook C., Bozdagi O., Yao J., Gomez-Ramirez M., Zaidi N.F., Wasco W., RA Gandy S., Santucci A.C., Haroutunian V., Huntley G.W., Buxbaum J.D.; RT "Altered Abeta formation and long-term potentiation in a calsenilin knock- RT out."; RL J. Neurosci. 23:9097-9106(2003). RN [12] 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 [13] RP DNA-BINDING, CALCIUM-BINDING, SUBUNIT, AND MUTAGENESIS OF GLU-186 AND RP GLU-234. RX PubMed=15746104; DOI=10.1074/jbc.m500338200; RA Osawa M., Dace A., Tong K.I., Valiveti A., Ikura M., Ames J.B.; RT "Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of RT DREAM."; RL J. Biol. Chem. 280:18008-18014(2005). RN [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY RP 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 expression."; RL Cell 143:1174-1189(2010). RN [16] RP FUNCTION IN POTASSIUM TRANSPORT, AND INTERACTION WITH KCND2. 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 subunits in RT the generation of Kv4-encoded IA channels in cortical pyramidal neurons."; RL J. Neurosci. 30:13644-13655(2010). RN [17] RP FUNCTION IN POTASSIUM TRANSPORT, AND SUBCELLULAR LOCATION. RX PubMed=22311982; DOI=10.1074/jbc.m111.324574; RA Foeger N.C., Norris A.J., Wren L.M., Nerbonne J.M.; RT "Augmentation of Kv4.2-encoded currents by accessory dipeptidyl peptidase 6 RT and 10 subunits reflects selective cell surface Kv4.2 protein RT stabilization."; RL J. Biol. Chem. 287:9640-9650(2012). RN [18] RP STRUCTURE BY NMR, SUBUNIT, DNA-BINDING, AND CALCIUM-BINDING. RX PubMed=18201103; DOI=10.1021/bi7017267; RA Lusin J.D., Vanarotti M., Li C., Valiveti A., Ames J.B.; RT "NMR structure of DREAM: implications for Ca(2+)-dependent DNA binding and RT protein dimerization."; RL Biochemistry 47:2252-2264(2008). 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. {ECO:0000269|PubMed:11792319, CC ECO:0000269|PubMed:14534243}. 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:20943905, ECO:0000269|PubMed:22311982}. 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 (By similarity). {ECO:0000250|UniProtKB:Q9Y2W7}. CC -!- SUBUNIT: Binds to DNA as a homomultimer. Dimerization is induced by CC binding to calcium (PubMed:18201103). Interacts with the C-terminus of CC PSEN1 and PSEN2 and with PSEN2 CTF subunit. Associates with KCN1. CC Component of heteromultimeric potassium channels (PubMed:19713751). CC Identified in potassium channel complexes containing KCND1, KCND2, CC KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 CC (PubMed:19713751). Interacts with KCND2 and KCND3 (PubMed:11598014, CC PubMed:12451113, PubMed:20943905). {ECO:0000269|PubMed:11598014, CC ECO:0000269|PubMed:12451113, ECO:0000269|PubMed:15746104, CC ECO:0000269|PubMed:18201103, ECO:0000269|PubMed:20943905, ECO:0000305}. CC -!- INTERACTION: CC Q9QXT8; Q61144: Psen2; NbExp=3; IntAct=EBI-11720427, EBI-21309044; CC Q9QXT8; PRO_0000025608 [Q61144]: Psen2; NbExp=3; IntAct=EBI-11720427, EBI-21396390; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22311982}. Cell CC membrane {ECO:0000250|UniProtKB:Q9Y2W7}; Lipid-anchor. Endoplasmic CC reticulum {ECO:0000250|UniProtKB:Q9Y2W7}. Golgi apparatus CC {ECO:0000250|UniProtKB:Q9Y2W7}. Nucleus {ECO:0000250|UniProtKB:Q9Y2W7}. CC Note=The sumoylated form is present only in the nucleus. In the CC presence of PSEN2, associated with the endoplasmic reticulum and Golgi. CC {ECO:0000250|UniProtKB:Q9Y2W7}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Calsenilin/KChIP3 T+; CC IsoId=Q9QXT8-1; Sequence=Displayed; CC Name=2; Synonyms=Calsenilin/KChIP3 T-; CC IsoId=Q9QXT8-2; Sequence=VSP_015042; CC Name=3; Synonyms=DREAM T-; CC IsoId=Q9QXT8-3; Sequence=VSP_015041; CC Name=4; Synonyms=DREAM T+; CC IsoId=P0C092-1; Sequence=External; CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Isoform 1 or isoform 4 CC (T+ forms) are expressed at equal levels with isoform 2 or isoform 3 CC (T- forms). Primarily detected in the layer V and deep layer VI of the CC cerebral cortex, the hippocampus, and the entire cerebellum. Expressed CC at low levels in testis. Also expressed in heart. CC {ECO:0000269|PubMed:10676964, ECO:0000269|PubMed:11161465, CC ECO:0000269|PubMed:12646414, ECO:0000269|PubMed:15363885}. CC -!- PTM: Palmitoylated. Palmitoylation enhances association with the plasma CC membrane (By similarity). {ECO:0000250}. CC -!- PTM: Proteolytically cleaved by caspase-3. {ECO:0000250}. CC -!- MISCELLANEOUS: Mice deficient for Csen show a significant decrease of CC amyloid-beta protein 40 and beta-amyloid protein 42, and display CC markedly reduced responses in models of acute thermal, mechanical, and CC visceral pain. CC -!- MISCELLANEOUS: [Isoform 2]: Lacks EF-hand domains. {ECO:0000305}. 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; AF287732; AAK08175.1; -; mRNA. DR EMBL; AF287733; AAK08180.1; -; mRNA. DR EMBL; AF287737; AAK08176.1; -; Genomic_DNA. DR EMBL; AF287734; AAK08176.1; JOINED; Genomic_DNA. DR EMBL; AF287735; AAK08176.1; JOINED; Genomic_DNA. DR EMBL; AF287736; AAK08176.1; JOINED; Genomic_DNA. DR EMBL; AF287737; AAK08177.1; -; Genomic_DNA. DR EMBL; AF287734; AAK08177.1; JOINED; Genomic_DNA. DR EMBL; AF287735; AAK08177.1; JOINED; Genomic_DNA. DR EMBL; AF287736; AAK08177.1; JOINED; Genomic_DNA. DR EMBL; AF287737; AAK08179.1; -; Genomic_DNA. DR EMBL; AF287734; AAK08179.1; JOINED; Genomic_DNA. DR EMBL; AF287735; AAK08179.1; JOINED; Genomic_DNA. DR EMBL; AF287736; AAK08179.1; JOINED; Genomic_DNA. DR EMBL; AF184624; AAF14576.1; -; mRNA. DR EMBL; AF274050; AAF74784.1; -; mRNA. DR EMBL; AF300870; AAG17450.1; -; mRNA. DR EMBL; BC026980; AAH26980.1; -; mRNA. DR EMBL; BC047139; AAH47139.1; -; mRNA. DR EMBL; BC057329; AAH57329.1; -; mRNA. DR CCDS; CCDS16703.1; -. [Q9QXT8-1] DR CCDS; CCDS71139.1; -. [Q9QXT8-3] DR RefSeq; NP_001104801.1; NM_001111331.1. DR RefSeq; NP_001277934.1; NM_001291005.1. DR RefSeq; NP_062763.2; NM_019789.4. [Q9QXT8-1] DR PDB; 2JUL; NMR; -; A=1-256. DR PDBsum; 2JUL; -. DR AlphaFoldDB; Q9QXT8; -. DR BMRB; Q9QXT8; -. DR SMR; Q9QXT8; -. DR BioGRID; 208000; 2. DR IntAct; Q9QXT8; 2. DR MINT; Q9QXT8; -. DR STRING; 10090.ENSMUSP00000028850; -. DR iPTMnet; Q9QXT8; -. DR PhosphoSitePlus; Q9QXT8; -. DR SwissPalm; Q9QXT8; -. DR jPOST; Q9QXT8; -. DR MaxQB; Q9QXT8; -. DR PaxDb; 10090-ENSMUSP00000099504; -. DR ProteomicsDB; 284031; -. [Q9QXT8-1] DR ProteomicsDB; 284032; -. [Q9QXT8-2] DR ProteomicsDB; 284033; -. [Q9QXT8-3] DR ABCD; Q9QXT8; 2 sequenced antibodies. DR Antibodypedia; 4181; 600 antibodies from 41 providers. DR DNASU; 56461; -. DR Ensembl; ENSMUST00000103215.11; ENSMUSP00000099504.5; ENSMUSG00000079056.13. [Q9QXT8-1] DR GeneID; 56461; -. DR KEGG; mmu:56461; -. DR UCSC; uc008mfm.2; mouse. [Q9QXT8-1] DR AGR; MGI:1929258; -. DR CTD; 30818; -. DR MGI; MGI:1929258; Kcnip3. DR VEuPathDB; HostDB:ENSMUSG00000079056; -. DR eggNOG; KOG0044; Eukaryota. DR GeneTree; ENSGT00940000158782; -. DR InParanoid; Q9QXT8; -. DR OrthoDB; 339700at2759; -. DR TreeFam; TF318560; -. DR Reactome; R-MMU-5576894; Phase 1 - inactivation of fast Na+ channels. DR BioGRID-ORCS; 56461; 2 hits in 77 CRISPR screens. DR ChiTaRS; Kcnip3; mouse. DR EvolutionaryTrace; Q9QXT8; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q9QXT8; Protein. DR Bgee; ENSMUSG00000079056; Expressed in lumbar dorsal root ganglion and 158 other cell types or tissues. DR ExpressionAtlas; Q9QXT8; baseline and differential. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0043679; C:axon terminus; ISO:MGI. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0030425; C:dendrite; ISO:MGI. 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; IDA:MGI. DR GO; GO:0032993; C:protein-DNA complex; IMP:CAFA. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IMP:CAFA. DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:CAFA. DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IMP:CAFA. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0043167; F:ion binding; EXP:DisProt. DR GO; GO:0000287; F:magnesium ion binding; IMP:CAFA. DR GO; GO:0140677; F:molecular function activator activity; EXP:DisProt. 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI. DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0048266; P:behavioral response to pain; IMP:MGI. DR GO; GO:0006886; P:intracellular protein transport; ISO:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; TAS:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI. DR GO; GO:0006813; P:potassium ion transport; TAS:MGI. DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB. DR GO; GO:0043523; P:regulation of neuron apoptotic process; IDA:MGI. DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IMP:UniProtKB. DR GO; GO:0032026; P:response to magnesium ion; IMP:UniProtKB. DR GO; GO:0048265; P:response to pain; IMP:MGI. DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI. DR CDD; cd00051; EFh; 2. DR DisProt; DP00291; -. 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:SF165; CALSENILIN; 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; 2. DR PROSITE; PS50222; EF_HAND_2; 3. DR Genevisible; Q9QXT8; MM. 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_0000073815" 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..22 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 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 63 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y2W7" 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:0000250|UniProtKB:Q9Y2W7" FT CROSSLNK 90 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000250|UniProtKB:Q9Y2W7" FT VAR_SEQ 1..61 FT /note="MQRTKEAVKASDGNLLGDPGRIPLSKRESIKWQRPRFTRQALMRCCLIKWIL FT SSAAPQGSD -> MRQLPAGPSSLACSGCKAGRLVTVPFSSRDAEDQGSREGIGWQPPG FT RSWAHTTEQEGKHQVAKATVHPPGPDALLLNQVDPVQCCPTRL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11161465" FT /id="VSP_015041" FT VAR_SEQ 61..256 FT /note="DSSDSELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFKNECPTGLVDED FT TFKLIYSQFFPQGDATTYAHFLFNAFDADGNGAIHFEDFVVGLSILLRGTVHEKLKWAF FT NLYDINKDGCITKEEMLAIMKSIYDMMGRHTYPILREDAPLEHVERFFQKMDRNQDGVV FT TIDEFLETCQKDENIMNSMQLFENVI -> AVTVNWSYPRCAISQRAWTSYKLRPSSPR FT RSCSPFTEASRMSVPQAWWMKTPSNSFIPSSSLREMPPPMHTSSSMPSMLMGTGPSTLR FT TLWLGSPSCFEGRSMRSSSGPSISMTLTRMVASPRRRCWPS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11161465" FT /id="VSP_015042" FT VARIANT 14 FT /note="N -> S (in strain: 129/Ola, BALB/c and FVB/NJ)" FT /evidence="ECO:0000269|PubMed:11161465, ECO:0000269|Ref.3, FT ECO:0000269|Ref.4" FT MUTAGEN 186 FT /note="E->Q: Abolishes calcium-binding." FT /evidence="ECO:0000269|PubMed:15746104" FT MUTAGEN 234 FT /note="E->Q: Abolishes calcium-binding." FT /evidence="ECO:0000269|PubMed:15746104" FT CONFLICT 246 FT /note="M -> T (in Ref. 2; AAF14576)" FT /evidence="ECO:0000305" FT HELIX 78..85 FT /evidence="ECO:0007829|PDB:2JUL" FT HELIX 90..103 FT /evidence="ECO:0007829|PDB:2JUL" FT STRAND 107..110 FT /evidence="ECO:0007829|PDB:2JUL" FT HELIX 111..121 FT /evidence="ECO:0007829|PDB:2JUL" FT HELIX 128..137 FT /evidence="ECO:0007829|PDB:2JUL" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:2JUL" FT HELIX 149..159 FT /evidence="ECO:0007829|PDB:2JUL" FT HELIX 163..173 FT /evidence="ECO:0007829|PDB:2JUL" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:2JUL" FT HELIX 184..197 FT /evidence="ECO:0007829|PDB:2JUL" FT HELIX 211..221 FT /evidence="ECO:0007829|PDB:2JUL" FT HELIX 232..241 FT /evidence="ECO:0007829|PDB:2JUL" FT HELIX 245..255 FT /evidence="ECO:0007829|PDB:2JUL" SQ SEQUENCE 256 AA; 29463 MW; 0F43D5F239D6378C CRC64; MQRTKEAVKA SDGNLLGDPG RIPLSKRESI KWQRPRFTRQ ALMRCCLIKW ILSSAAPQGS DSSDSELELS TVRHQPEGLD QLQAQTKFTK KELQSLYRGF KNECPTGLVD EDTFKLIYSQ FFPQGDATTY AHFLFNAFDA DGNGAIHFED FVVGLSILLR GTVHEKLKWA FNLYDINKDG CITKEEMLAI MKSIYDMMGR HTYPILREDA PLEHVERFFQ KMDRNQDGVV TIDEFLETCQ KDENIMNSMQ LFENVI //