CSEN_BOVIN
ID CSEN_BOVIN Reviewed; 256 AA.
AC Q17QD9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Calsenilin;
DE AltName: Full=A-type potassium channel modulatory protein 3;
DE AltName: Full=Kv channel-interacting protein 3;
DE Short=KChIP3;
GN Name=KCNIP3; Synonyms=CSEN;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9Y2W7}.
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 -!- 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 -!- SUBUNIT: Binds to DNA as a homomultimer. Dimerization is induced by
CC binding to calcium. Interacts with the C-terminus of PSEN1 and PSEN2
CC and with PSEN2 CTF subunit. Associates with KCN1. Component of
CC heteromultimeric potassium channels. Identified in potassium channel
CC complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3,
CC KCNIP4, DPP6 and DPP10. Interacts with KCND2 and KCND3.
CC {ECO:0000250|UniProtKB:Q9QXT8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2W7}. Cell
CC membrane {ECO:0000250|UniProtKB:Q9Y2W7}; Lipid-anchor {ECO:0000250}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y2W7}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9Y2W7}. Nucleus {ECO:0000250|UniProtKB:Q9Y2W7}.
CC Note=Also membrane-bound, associated with the plasma membrane. In the
CC presence of PSEN2 associated with the endoplasmic reticulum and Golgi.
CC The sumoylated form is present only in the nucleus.
CC {ECO:0000250|UniProtKB:Q9Y2W7}.
CC -!- PTM: Palmitoylated. Palmitoylation enhances association with the plasma
CC membrane (By similarity). {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved by caspase-3.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; BC118417; AAI18418.1; -; mRNA.
DR RefSeq; NP_001069080.1; NM_001075612.1.
DR AlphaFoldDB; Q17QD9; -.
DR BMRB; Q17QD9; -.
DR SMR; Q17QD9; -.
DR STRING; 9913.ENSBTAP00000023873; -.
DR PaxDb; Q17QD9; -.
DR PRIDE; Q17QD9; -.
DR GeneID; 513316; -.
DR KEGG; bta:513316; -.
DR CTD; 30818; -.
DR eggNOG; KOG0044; Eukaryota.
DR InParanoid; Q17QD9; -.
DR OrthoDB; 1271942at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
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; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 2: Evidence at transcript level;
KW Apoptosis; Calcium; Cell membrane; Cytoplasm; Endoplasmic reticulum;
KW Golgi apparatus; Ion channel; Ion transport; Isopeptide bond; Lipoprotein;
KW Membrane; Metal-binding; Nucleus; Palmitate; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Transport;
KW Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..256
FT /note="Calsenilin"
FT /id="PRO_0000285577"
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..30
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"
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"
SQ SEQUENCE 256 AA; 29446 MW; 9C0BFC4B96406513 CRC64;
MQRAKEVMKV SDGSLLGEPG RTPLSKKEGV KWQRPRLTRQ ALMRCCLVKW ILSSAAPQGS
YSSDSELELS AVRHQPEGLD QLQAQTKFTK KELQSLYRGF KNECPTGLVD EDTFKLIYSQ
FFPQGDATTY AHFLFNAFDA DGNGAIRFED FVVGLSILLR GTVHEKLKWA FNLYDINKDG
YITKEEMLAI MKSIYDMMGR HTYPILREDA PLEHVERFFQ KMDRNQDGVV TIDEFLETCQ
KDENIMSSMQ LFENVI
