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Neuronal calcium sensor 1 (NCS-1) (Frequenin homolog) (Frequenin-like protein) (Frequenin-like ubiquitous protein)

 NCS1_RAT                Reviewed;         190 AA.
P62168; P36610; Q9UK26;
21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 127.
RecName: Full=Neuronal calcium sensor 1;
Short=NCS-1;
AltName: Full=Frequenin homolog;
AltName: Full=Frequenin-like protein;
AltName: Full=Frequenin-like ubiquitous protein;
Name=Ncs1; Synonyms=Flup, Freq;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7488079; DOI=10.1006/bbrc.1995.2601;
de Castro E., Nef S., Fiumelli H., Lenz S.E., Kawamura S., Nef P.;
"Regulation of rhodopsin phosphorylation by a family of neuronal
calcium sensors.";
Biochem. Biophys. Res. Commun. 216:133-140(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Lindemeier J.;
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
[3]
MYRISTOYLATION AT GLY-2, CALCIUM-BINDING, AND SUBCELLULAR LOCATION.
PubMed=10514519; DOI=10.1074/jbc.274.42.30258;
McFerran B.W., Weiss J.L., Burgoyne R.D.;
"Neuronal Ca(2+) sensor 1. Characterization of the myristoylated
protein, its cellular effects in permeabilized adrenal chromaffin
cells, Ca(2+)-independent membrane association, and interaction with
binding proteins, suggesting a role in rapid Ca(2+) signal
transduction.";
J. Biol. Chem. 274:30258-30265(1999).
[4]
INTERACTION WITH PI4KB, AND SUBCELLULAR LOCATION.
PubMed=11526106; DOI=10.1074/jbc.M104048200;
Zhao X., Varnai P., Tuymetova G., Balla A., Toth Z.E., Oker-Blom C.,
Roder J., Jeromin A., Balla T.;
"Interaction of neuronal calcium sensor-1 (NCS-1) with
phosphatidylinositol 4-kinase beta stimulates lipid kinase activity
and affects membrane trafficking in COS-7 cells.";
J. Biol. Chem. 276:40183-40189(2001).
[5]
FUNCTION.
PubMed=17502602; DOI=10.1073/pnas.0701133104;
Gambino F., Pavlowsky A., Begle A., Dupont J.-L., Bahi N.,
Courjaret R., Gardette R., Hadjkacem H., Skala H., Poulain B.,
Chelly J., Vitale N., Humeau Y.;
"IL1-receptor accessory protein-like 1 (IL1RAPL1), a protein involved
in cognitive functions, regulates N-type Ca2+-channel and neurite
elongation.";
Proc. Natl. Acad. Sci. U.S.A. 104:9063-9068(2007).
[6]
MUTAGENESIS OF ASP-73; GLU-84; ASP-109 AND GLU-120, CALCIUM-BINDING,
AND MAGNESIUM-BINDING.
PubMed=18199453; DOI=10.1016/j.jmb.2007.12.033;
Aravind P., Chandra K., Reddy P.P., Jeromin A., Chary K.V.R.,
Sharma Y.;
"Regulatory and structural EF-hand motifs of neuronal calcium sensor-
1: Mg 2+ modulates Ca 2+ binding, Ca 2+ -induced conformational
changes, and equilibrium unfolding transitions.";
J. Mol. Biol. 376:1100-1115(2008).
[7]
INTERACTION WITH PICK1.
PubMed=19109914; DOI=10.1016/j.neuron.2008.10.050;
Jo J., Heon S., Kim M.J., Son G.H., Park Y., Henley J.M., Weiss J.L.,
Sheng M., Collingridge G.L., Cho K.;
"Metabotropic glutamate receptor-mediated LTD involves two interacting
Ca(2+) sensors, NCS-1 and PICK1.";
Neuron 60:1095-1111(2008).
-!- FUNCTION: Neuronal calcium sensor, regulator of G protein-coupled
receptor phosphorylation in a calcium dependent manner. Directly
regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for
calmodulin. Stimulates PI4KB kinase activity. Involved in long-
term synaptic plasticity through its interaction with PICK1. May
also play a role in neuron differentiation through inhibition of
the activity of N-type voltage-gated calcium channel.
{ECO:0000269|PubMed:17502602}.
-!- SUBUNIT: Interacts in a calcium-independent manner with PI4KB, but
only if myristoylated. This binding competes with CALN2/CABP7
binding to PI4KB. Interacts in a calcium-dependent manner with
PICK1 (via AH domain). Interacts with KCND2, ARF1, ARF3, ARF5 and
ARF6 (By similarity). Interacts with IL1RAPL1 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
P84080:ARF1 (xeno); NbExp=2; IntAct=EBI-907774, EBI-449051;
P14100:PDE1A (xeno); NbExp=2; IntAct=EBI-907774, EBI-907809;
-!- SUBCELLULAR LOCATION: Golgi apparatus
{ECO:0000269|PubMed:11526106}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density {ECO:0000305}.
Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P62166}.
Cytoplasm {ECO:0000269|PubMed:11526106}. Cell membrane
{ECO:0000269|PubMed:11526106}. Membrane
{ECO:0000250|UniProtKB:P62166, ECO:0000269|PubMed:10514519};
Lipid-anchor {ECO:0000250|UniProtKB:P62166}. Note=Associated with
Golgi stacks. Post-synaptic densities of dendrites, and in the
pre-synaptic nerve terminal at neuromuscular junctions.
{ECO:0000250|UniProtKB:P62166, ECO:0000269|PubMed:11526106,
ECO:0000305}.
-!- DOMAIN: Binds 3 calcium ions via the second, third and fourth EF-
hand. EF-2 and EF-3 bind both magnesium and calcium, while EF-4
binds only calcium. At the resting state, magnesium is bound to
EF-2 and EF-3 and upon activation, both sites bind calcium
simultaneously while EF-4 is the last one to be occupied.
-!- MISCELLANEOUS: Fourfold reduction in calcium affinity for
NCS1/FREQ in the presence of magnesium.
-!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L27421; AAA88510.1; -; mRNA.
EMBL; X82188; CAA57678.1; -; mRNA.
RefSeq; NP_077342.1; NM_024366.1.
UniGene; Rn.62653; -.
PDB; 4OV2; X-ray; 2.60 A; A/B/C/D=1-177.
PDB; 4YRU; X-ray; 2.80 A; A/B/C/D=1-177.
PDB; 5AEQ; X-ray; 1.95 A; A/B=1-190.
PDB; 5AER; X-ray; 2.19 A; A=1-190.
PDB; 5AFP; X-ray; 2.30 A; A/B=1-190.
PDBsum; 4OV2; -.
PDBsum; 4YRU; -.
PDBsum; 5AEQ; -.
PDBsum; 5AER; -.
PDBsum; 5AFP; -.
ProteinModelPortal; P62168; -.
SMR; P62168; -.
IntAct; P62168; 7.
STRING; 10116.ENSRNOP00000011648; -.
iPTMnet; P62168; -.
PaxDb; P62168; -.
PRIDE; P62168; -.
Ensembl; ENSRNOT00000011648; ENSRNOP00000011648; ENSRNOG00000008761.
GeneID; 65153; -.
KEGG; rno:65153; -.
UCSC; RGD:68417; rat.
CTD; 23413; -.
RGD; 68417; Ncs1.
eggNOG; KOG0044; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00760000118820; -.
HOGENOM; HOG000233019; -.
HOVERGEN; HBG108179; -.
InParanoid; P62168; -.
KO; K19932; -.
OMA; KRELQQW; -.
OrthoDB; EOG091G11T4; -.
PhylomeDB; P62168; -.
TreeFam; TF300009; -.
PRO; PR:P62168; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000008761; -.
Genevisible; P62168; RN.
GO; GO:0030424; C:axon; ISO:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IDA:RGD.
GO; GO:0008427; F:calcium-dependent protein kinase inhibitor activity; TAS:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:RGD.
GO; GO:0045921; P:positive regulation of exocytosis; IDA:RGD.
GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
CDD; cd00051; EFh; 2.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF00036; EF-hand_1; 1.
Pfam; PF13499; EF-hand_7; 1.
SMART; SM00054; EFh; 3.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 3.
PROSITE; PS50222; EF_HAND_2; 3.
1: Evidence at protein level;
3D-structure; Calcium; Cell junction; Cell membrane;
Complete proteome; Cytoplasm; Golgi apparatus; Lipoprotein; Membrane;
Metal-binding; Myristate; Postsynaptic cell membrane;
Reference proteome; Repeat; Synapse.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10514519}.
CHAIN 2 190 Neuronal calcium sensor 1.
/FTId=PRO_0000073790.
DOMAIN 24 59 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 60 95 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 96 131 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 144 179 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 73 84 1.
CA_BIND 109 120 2.
CA_BIND 157 168 3.
REGION 36 47 Ancestral calcium site 1.
REGION 174 190 Interaction with IL1RAPL1. {ECO:0000250}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:10514519}.
MUTAGEN 73 73 D->A: Loss of magnesium-binding; when
associated with Q-84, A-109 and Q-120.
{ECO:0000269|PubMed:18199453}.
MUTAGEN 84 84 E->Q: Loss of magnesium-binding; when
associated with A-73, A-109 and Q-120.
{ECO:0000269|PubMed:18199453}.
MUTAGEN 109 109 D->A: Loss of magnesium-binding; when
associated with A-73, Q-84 and Q-120.
{ECO:0000269|PubMed:18199453}.
MUTAGEN 120 120 E->Q: Loss of magnesium-binding; when
associated with A-73, Q-84 and A-109.
{ECO:0000269|PubMed:18199453}.
HELIX 10 18 {ECO:0000244|PDB:5AEQ}.
STRAND 20 22 {ECO:0000244|PDB:5AER}.
HELIX 24 37 {ECO:0000244|PDB:5AEQ}.
STRAND 41 43 {ECO:0000244|PDB:5AEQ}.
HELIX 45 49 {ECO:0000244|PDB:5AEQ}.
HELIX 51 55 {ECO:0000244|PDB:5AEQ}.
HELIX 62 72 {ECO:0000244|PDB:5AEQ}.
STRAND 77 81 {ECO:0000244|PDB:5AER}.
HELIX 82 94 {ECO:0000244|PDB:5AEQ}.
HELIX 97 108 {ECO:0000244|PDB:5AEQ}.
STRAND 113 117 {ECO:0000244|PDB:5AEQ}.
HELIX 118 130 {ECO:0000244|PDB:5AEQ}.
HELIX 133 135 {ECO:0000244|PDB:5AER}.
HELIX 140 142 {ECO:0000244|PDB:5AEQ}.
HELIX 145 156 {ECO:0000244|PDB:5AEQ}.
STRAND 161 165 {ECO:0000244|PDB:5AEQ}.
HELIX 166 175 {ECO:0000244|PDB:5AEQ}.
HELIX 177 183 {ECO:0000244|PDB:5AEQ}.
HELIX 186 189 {ECO:0000244|PDB:5AER}.
SEQUENCE 190 AA; 21879 MW; 9AF8E26A23F80D4F CRC64;
MGKSNSKLKP EVVEELTRKT YFTEKEVQQW YKGFIKDCPS GQLDAAGFQK IYKQFFPFGD
PTKFATFVFN VFDENKDGRI EFSEFIQALS VTSRGTLDEK LRWAFKLYDL DNDGYITRNE
MLDIVDAIYQ MVGNTVELPE EENTPEKRVD RIFAMMDKNA DGKLTLQEFQ EGSKADPSIV
QALSLYDGLV


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