NCS1_MOUSE
ID NCS1_MOUSE Reviewed; 190 AA.
AC Q8BNY6; A2AJ84;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Neuronal calcium sensor 1;
DE Short=NCS-1;
DE AltName: Full=Frequenin homolog;
GN Name=Ncs1; Synonyms=Freq;
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].
RC STRAIN=C57BL/6J;
RA Mount D.B.;
RT "Intra-renal expression of mNCS-1.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-190.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP IDENTIFICATION BY 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).
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 (By similarity).
CC This binding competes with CALN2/CABP7 binding to PI4KB (By
CC similarity). Interacts in a calcium-dependent manner with PICK1 (via AH
CC domain) (By similarity). Interacts with ARF1, ARF3, ARF5 and ARF6 (By
CC similarity). Interacts with IL1RAPL1 (By similarity).
CC {ECO:0000250|UniProtKB:P62166, ECO:0000250|UniProtKB:P62168}.
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 {ECO:0000250|UniProtKB:P62166,
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}.
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DR EMBL; AF020184; AAD01642.1; -; mRNA.
DR EMBL; AL732572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059825; AAH59825.1; -; mRNA.
DR EMBL; AK079136; BAC37557.1; -; mRNA.
DR CCDS; CCDS15896.1; -.
DR RefSeq; NP_062655.1; NM_019681.3.
DR AlphaFoldDB; Q8BNY6; -.
DR SMR; Q8BNY6; -.
DR BioGRID; 199742; 3.
DR DIP; DIP-61316N; -.
DR IntAct; Q8BNY6; 3.
DR MINT; Q8BNY6; -.
DR STRING; 10090.ENSMUSP00000000199; -.
DR iPTMnet; Q8BNY6; -.
DR PhosphoSitePlus; Q8BNY6; -.
DR EPD; Q8BNY6; -.
DR MaxQB; Q8BNY6; -.
DR PaxDb; Q8BNY6; -.
DR PeptideAtlas; Q8BNY6; -.
DR PRIDE; Q8BNY6; -.
DR ProteomicsDB; 293636; -.
DR Antibodypedia; 4347; 372 antibodies from 38 providers.
DR DNASU; 14299; -.
DR Ensembl; ENSMUST00000000199; ENSMUSP00000000199; ENSMUSG00000062661.
DR GeneID; 14299; -.
DR KEGG; mmu:14299; -.
DR UCSC; uc008jdq.1; mouse.
DR CTD; 23413; -.
DR MGI; MGI:109166; Ncs1.
DR VEuPathDB; HostDB:ENSMUSG00000062661; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000154645; -.
DR HOGENOM; CLU_072366_1_2_1; -.
DR InParanoid; Q8BNY6; -.
DR OMA; EYVFNVF; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; Q8BNY6; -.
DR TreeFam; TF300009; -.
DR BioGRID-ORCS; 14299; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ncs1; mouse.
DR PRO; PR:Q8BNY6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BNY6; protein.
DR Bgee; ENSMUSG00000062661; Expressed in dentate gyrus of hippocampal formation granule cell and 203 other tissues.
DR ExpressionAtlas; Q8BNY6; baseline and differential.
DR Genevisible; Q8BNY6; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0044305; C:calyx of Held; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0031045; C:dense core granule; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0008048; F:calcium sensitive guanylate cyclase activator activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; ISO:MGI.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; TAS:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
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_0000073789"
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"
FT CONFLICT 63
FT /note="K -> E (in Ref. 4; BAC37557)"
FT /evidence="ECO:0000305"
SQ 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
