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

 NCS1_HUMAN              Reviewed;         190 AA.
P62166; E9PAY3; P36610; Q9UK26;
21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 146.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Lindemeier J.R., Hauenschild A., Pongs O.;
"Frequenin-like Ca2+-binding protein (flup) modulates fast
inactivation of mammalian presynaptic A-type K-channel.";
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Bao X.G., Yu L., Zhao S.Y.;
"Cloning of a new human cDNA homologous to Rattus norvegicus neuronal
calcium sensor (NCS-1).";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Nef S.;
Submitted (JUN-1999) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Pongs O., Hauenschild A., Dannenberg J.;
"Sequence of human frequenin.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Ovary, and Spinal ganglion;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH KCND2.
PubMed=11606724; DOI=10.1073/pnas.221168498;
Nakamura T.Y., Pountney D.J., Ozaita A., Nandi S., Ueda S., Rudy B.,
Coetzee W.A.;
"A role for frequenin, a Ca2+-binding protein, as a regulator of Kv4
K+-currents.";
Proc. Natl. Acad. Sci. U.S.A. 98:12808-12813(2001).
[8]
INTERACTION WITH IL1RAPL1.
PubMed=12783849; DOI=10.1093/hmg/ddg147;
Bahi N., Friocourt G., Carrie A., Graham M.E., Weiss J.L., Chafey P.,
Fauchereau F., Burgoyne R.D., Chelly J.;
"IL1 receptor accessory protein like, a protein involved in X-linked
mental retardation, interacts with Neuronal Calcium Sensor-1 and
regulates exocytosis.";
Hum. Mol. Genet. 12:1415-1425(2003).
[9]
INTERACTION WITH ARF1; ARF3; ARF5 AND ARF6, AND SUBCELLULAR LOCATION.
PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x;
Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.;
"Specificity, promiscuity and localization of ARF protein interactions
with NCS-1 and phosphatidylinositol-4 kinase-III beta.";
Traffic 8:1080-1092(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[12]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS OF GLU-81; THR-117
AND THR-165, CALCIUM-BINDING, AND SUBCELLULAR LOCATION.
PubMed=11092894; DOI=10.1074/jbc.M009373200;
Bourne Y., Dannenberg J., Pollmann V., Marchot P., Pongs O.;
"Immunocytochemical localization and crystal structure of human
frequenin (neuronal calcium sensor 1).";
J. Biol. Chem. 276:11949-11955(2001).
-!- 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 (By similarity). Stimulates PI4KB kinase activity (By
similarity). Involved in long-term synaptic plasticity through its
interaction with PICK1 (By similarity). May also play a role in
neuron differentiation through inhibition of the activity of N-
type voltage-gated calcium channel (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with KCND2. Interacts in a calcium-independent
manner with PI4KB. This binding competes with CALN2/CABP7 binding
to PI4KB (By similarity). Interacts with ARF1, ARF3, ARF5 and
ARF6. Interacts in a calcium-dependent manner with PICK1 (via AH
domain) (By similarity). Interacts with IL1RAPL1. {ECO:0000250,
ECO:0000269|PubMed:11606724, ECO:0000269|PubMed:12783849,
ECO:0000269|PubMed:17555535}.
-!- INTERACTION:
Q86UW9:DTX2; NbExp=12; IntAct=EBI-746987, EBI-740376;
P41271:NBL1; NbExp=3; IntAct=EBI-746987, EBI-10208650;
-!- SUBCELLULAR LOCATION: Golgi apparatus
{ECO:0000269|PubMed:17555535}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density {ECO:0000305}.
Cytoplasm, perinuclear region {ECO:0000269|PubMed:11092894,
ECO:0000269|PubMed:17555535}. Cytoplasm
{ECO:0000250|UniProtKB:P62168}. Cell membrane
{ECO:0000269|PubMed:17555535}; Peripheral membrane protein.
Membrane {ECO:0000250|UniProtKB:P62168}; Lipid-anchor
{ECO:0000305}. Note=Associated with Golgi stacks. Post-synaptic
densities of dendrites, and in the pre-synaptic nerve terminal at
neuromuscular junctions. {ECO:0000305,
ECO:0000305|PubMed:17555535}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P62166-1; Sequence=Displayed;
Name=2;
IsoId=P62166-2; Sequence=VSP_046312;
Note=No experimental confirmation available.;
-!- MISCELLANEOUS: Binds 3 calcium ions via the second, third and
fourth EF-hand.
-!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X84048; CAA58867.1; -; mRNA.
EMBL; AF134479; AAP97256.1; -; mRNA.
EMBL; AF186409; AAF01804.1; -; mRNA.
EMBL; AL360004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004856; AAH04856.1; -; mRNA.
EMBL; BQ880305; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS6932.1; -. [P62166-1]
CCDS; CCDS78448.1; -. [P62166-2]
RefSeq; NP_001122298.1; NM_001128826.1. [P62166-2]
RefSeq; NP_055101.2; NM_014286.3. [P62166-1]
UniGene; Hs.642946; -.
UniGene; Hs.714951; -.
PDB; 1G8I; X-ray; 1.90 A; A/B=1-190.
PDB; 2LCP; NMR; -; A=1-190.
PDB; 4GUK; X-ray; 1.75 A; A/B/C/D=6-188.
PDBsum; 1G8I; -.
PDBsum; 2LCP; -.
PDBsum; 4GUK; -.
ProteinModelPortal; P62166; -.
SMR; P62166; -.
BioGrid; 116985; 32.
IntAct; P62166; 13.
MINT; MINT-1436213; -.
STRING; 9606.ENSP00000361475; -.
iPTMnet; P62166; -.
PhosphoSitePlus; P62166; -.
BioMuta; NCS1; -.
DMDM; 49065666; -.
EPD; P62166; -.
MaxQB; P62166; -.
PaxDb; P62166; -.
PeptideAtlas; P62166; -.
PRIDE; P62166; -.
TopDownProteomics; P62166-1; -. [P62166-1]
DNASU; 23413; -.
Ensembl; ENST00000372398; ENSP00000361475; ENSG00000107130. [P62166-1]
Ensembl; ENST00000630865; ENSP00000486695; ENSG00000107130. [P62166-2]
GeneID; 23413; -.
KEGG; hsa:23413; -.
UCSC; uc004bzi.2; human. [P62166-1]
CTD; 23413; -.
DisGeNET; 23413; -.
GeneCards; NCS1; -.
HGNC; HGNC:3953; NCS1.
HPA; CAB018587; -.
HPA; HPA019713; -.
MIM; 603315; gene.
neXtProt; NX_P62166; -.
OpenTargets; ENSG00000107130; -.
PharmGKB; PA28371; -.
eggNOG; KOG0044; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00760000118820; -.
HOGENOM; HOG000233019; -.
HOVERGEN; HBG108179; -.
InParanoid; P62166; -.
KO; K19932; -.
OMA; KRELQQW; -.
OrthoDB; EOG091G11T4; -.
PhylomeDB; P62166; -.
TreeFam; TF300009; -.
ChiTaRS; NCS1; human.
EvolutionaryTrace; P62166; -.
GeneWiki; Neuronal_calcium_sensor-1; -.
GenomeRNAi; 23413; -.
PRO; PR:P62166; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000107130; -.
CleanEx; HS_FREQ; -.
ExpressionAtlas; P62166; baseline and differential.
Genevisible; P62166; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0031045; C:dense core granule; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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; TAS:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:Ensembl.
GO; GO:0045921; P:positive regulation of exocytosis; IEA:Ensembl.
GO; GO:0010975; P:regulation of neuron projection development; ISS: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; Alternative splicing; 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:25255805}.
CHAIN 2 190 Neuronal calcium sensor 1.
/FTId=PRO_0000073788.
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. {ECO:0000269|PubMed:11092894}.
CA_BIND 109 120 2. {ECO:0000269|PubMed:11092894}.
CA_BIND 157 168 3. {ECO:0000269|PubMed:11092894}.
REGION 174 190 Interaction with IL1RAPL1.
{ECO:0000269|PubMed:12783849}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25255805}.
VAR_SEQ 1 22 MGKSNSKLKPEVVEELTRKTYF -> MATI (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046312.
MUTAGEN 81 81 E->T: Reduces calcium binding; when
associated with A-117 or A-165. Abolishes
calcium binding; when associated with A-
117 and A-165.
{ECO:0000269|PubMed:11092894}.
MUTAGEN 117 117 T->A: Reduces calcium binding; when
associated with T-81. Abolishes calcium
binding; when associated with T-81 and A-
165. {ECO:0000269|PubMed:11092894}.
MUTAGEN 165 165 T->A: Reduces calcium binding; when
associated with A-117. Abolishes calcium
binding; when associated with T-81 and A-
117. {ECO:0000269|PubMed:11092894}.
CONFLICT 90 90 S -> P (in Ref. 4; AAF01804).
{ECO:0000305}.
CONFLICT 178 178 S -> P (in Ref. 4; AAF01804).
{ECO:0000305}.
HELIX 3 5 {ECO:0000244|PDB:2LCP}.
HELIX 10 18 {ECO:0000244|PDB:4GUK}.
STRAND 20 22 {ECO:0000244|PDB:1G8I}.
HELIX 24 37 {ECO:0000244|PDB:4GUK}.
STRAND 41 43 {ECO:0000244|PDB:4GUK}.
HELIX 45 55 {ECO:0000244|PDB:4GUK}.
HELIX 62 72 {ECO:0000244|PDB:4GUK}.
STRAND 77 81 {ECO:0000244|PDB:4GUK}.
HELIX 82 94 {ECO:0000244|PDB:4GUK}.
HELIX 97 108 {ECO:0000244|PDB:4GUK}.
STRAND 109 111 {ECO:0000244|PDB:2LCP}.
STRAND 113 117 {ECO:0000244|PDB:1G8I}.
HELIX 118 132 {ECO:0000244|PDB:4GUK}.
STRAND 134 136 {ECO:0000244|PDB:1G8I}.
STRAND 142 144 {ECO:0000244|PDB:4GUK}.
HELIX 145 156 {ECO:0000244|PDB:4GUK}.
HELIX 157 159 {ECO:0000244|PDB:2LCP}.
STRAND 161 164 {ECO:0000244|PDB:4GUK}.
HELIX 166 175 {ECO:0000244|PDB:4GUK}.
HELIX 177 183 {ECO:0000244|PDB:4GUK}.
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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