CSEN_MOUSE
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 03-AUG-2022, entry version 170.
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 -!- 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}.
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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; 1.
DR MINT; Q9QXT8; -.
DR STRING; 10090.ENSMUSP00000099504; -.
DR iPTMnet; Q9QXT8; -.
DR PhosphoSitePlus; Q9QXT8; -.
DR jPOST; Q9QXT8; -.
DR MaxQB; Q9QXT8; -.
DR PaxDb; Q9QXT8; -.
DR PRIDE; Q9QXT8; -.
DR ProteomicsDB; 284031; -. [Q9QXT8-1]
DR ProteomicsDB; 284032; -. [Q9QXT8-2]
DR ProteomicsDB; 284033; -. [Q9QXT8-3]
DR ABCD; Q9QXT8; 2 sequenced antibodies.
DR Antibodypedia; 4181; 546 antibodies from 41 providers.
DR DNASU; 56461; -.
DR Ensembl; ENSMUST00000103215; ENSMUSP00000099504; ENSMUSG00000079056. [Q9QXT8-1]
DR GeneID; 56461; -.
DR KEGG; mmu:56461; -.
DR UCSC; uc008mfm.2; mouse. [Q9QXT8-1]
DR CTD; 30818; -.
DR MGI; MGI:1929258; Kcnip3.
DR VEuPathDB; HostDB:ENSMUSG00000079056; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158782; -.
DR InParanoid; Q9QXT8; -.
DR OrthoDB; 1271942at2759; -.
DR TreeFam; TF318560; -.
DR Reactome; R-MMU-5576894; Phase 1 - inactivation of fast Na+ channels.
DR BioGRID-ORCS; 56461; 1 hit in 72 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 155 other tissues.
DR ExpressionAtlas; Q9QXT8; baseline and differential.
DR Genevisible; Q9QXT8; MM.
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:0000287; F:magnesium ion binding; IMP:CAFA.
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:0008022; F:protein C-terminus binding; IPI:MGI.
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:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS: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 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_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
