NCS1_BOVIN
ID NCS1_BOVIN Reviewed; 190 AA.
AC Q2V8Y7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Neuronal calcium sensor 1;
DE Short=NCS-1;
DE AltName: Full=Frequenin homolog;
GN Name=NCS1; Synonyms=FREQ;
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 [MRNA].
RA Fik-Rymarkiewicz E., Duda T., Sharma R.K.;
RT "Novel Ca2+-modulated frequenin-ROS-GC transduction machinery in bovine
RT hippocampus.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH PI4KB, AND SUBCELLULAR LOCATION.
RX PubMed=11526106; DOI=10.1074/jbc.m104048200;
RA Zhao X., Varnai P., Tuymetova G., Balla A., Toth Z.E., Oker-Blom C.,
RA Roder J., Jeromin A., Balla T.;
RT "Interaction of neuronal calcium sensor-1 (NCS-1) with phosphatidylinositol
RT 4-kinase beta stimulates lipid kinase activity and affects membrane
RT trafficking in COS-7 cells.";
RL J. Biol. Chem. 276:40183-40189(2001).
CC -!- FUNCTION: Neuronal calcium sensor, regulator of G protein-coupled
CC receptor phosphorylation in a calcium dependent manner. Directly
CC regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for
CC calmodulin (By similarity). Stimulates PI4KB kinase activity (By
CC similarity). Involved in long-term synaptic plasticity through its
CC interaction with PICK1 (By similarity). May also play a role in neuron
CC differentiation through inhibition of the activity of N-type voltage-
CC gated calcium channel (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with KCND2 (By similarity).
CC Interacts in a calcium-independent manner with PI4KB, but only if
CC myristoylated (PubMed:11526106). This binding competes with CALN2/CABP7
CC binding to PI4KB (PubMed:11526106). Interacts in a calcium-dependent
CC manner with PICK1 (via AH domain) (By similarity). Interacts with ARF1,
CC ARF3, ARF5 and ARF6 (By similarity). Interacts with IL1RAPL1 (By
CC similarity). {ECO:0000250|UniProtKB:P62166,
CC ECO:0000250|UniProtKB:P62168, ECO:0000269|PubMed:11526106}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P62166}.
CC Postsynaptic density {ECO:0000250|UniProtKB:P62166}. Cytoplasm,
CC perinuclear region {ECO:0000250|UniProtKB:P62166}. Cytoplasm
CC {ECO:0000250|UniProtKB:P62168}. Cell membrane
CC {ECO:0000250|UniProtKB:P62166}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P62166}. Membrane
CC {ECO:0000250|UniProtKB:P62168}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62166}. Note=Associated with Golgi stacks.
CC Post-synaptic densities of dendrites, and in the pre-synaptic nerve
CC terminal at neuromuscular junctions. {ECO:0000250|UniProtKB:P62166}.
CC -!- MISCELLANEOUS: Binds 3 calcium ions via the second, third and fourth
CC EF-hand. {ECO:0000250}.
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; DQ284984; ABB88851.1; -; mRNA.
DR RefSeq; NP_001035637.1; NM_001040547.1.
DR AlphaFoldDB; Q2V8Y7; -.
DR BMRB; Q2V8Y7; -.
DR SMR; Q2V8Y7; -.
DR STRING; 9913.ENSBTAP00000011496; -.
DR PaxDb; Q2V8Y7; -.
DR PRIDE; Q2V8Y7; -.
DR GeneID; 526544; -.
DR CTD; 23413; -.
DR eggNOG; KOG0044; Eukaryota.
DR InParanoid; Q2V8Y7; -.
DR OrthoDB; 1369072at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008048; F:calcium sensitive guanylate cyclase activator activity; IBA:GO_Central.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; 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; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cytoplasm; Golgi apparatus; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Reference proteome; Repeat; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62166"
FT CHAIN 2..190
FT /note="Neuronal calcium sensor 1"
FT /id="PRO_0000269462"
FT DOMAIN 24..59
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 60..95
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 96..131
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 144..179
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 174..190
FT /note="Interaction with IL1RAPL1"
FT /evidence="ECO:0000250|UniProtKB:P62166"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62168"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P62166"
SQ SEQUENCE 190 AA; 21833 MW; 7BB8F67F23E317FE CRC64;
MGKSNSKLKP EVVEELTRKT YFTEKEVQQW YKGFIKDCPS GQLDAAGFQK IYKQFFPFGD
PTKFATFVFN VFDENKDGRI EFSEFIQALS VTSRGTLDEK LRWASKLYDL DNDGYITRNE
MLDIVDAIYQ MVGNTVELPE EENTPEKRVD RIFAMMDKNA DGKLTLQEFQ EGTKADPSIV
QALSLYDGLV
