NCAH_DROME
ID NCAH_DROME Reviewed; 190 AA.
AC P42325; Q9VW67;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Neurocalcin homolog;
DE Short=DrosNCa;
GN Name=Nca; ORFNames=CG7641;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Canton-S;
RX PubMed=7989365; DOI=10.1016/s0021-9258(18)31780-0;
RA Teng D.H.-F., Chen C.-K., Hurley J.B.;
RT "A highly conserved homologue of bovine neurocalcin in Drosophila
RT melanogaster is a Ca(2+)-binding protein expressed in neuronal tissues.";
RL J. Biol. Chem. 269:31900-31907(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, MASS SPECTROMETRY, AND MYRISTOYLATION AT GLY-2.
RX PubMed=8626592; DOI=10.1074/jbc.271.17.10256;
RA Faurobert E., Chen C.-K., Hurley J.B., Teng D.H.-F.;
RT "Drosophila neurocalcin, a fatty acylated, Ca2+-binding protein that
RT associates with membranes and inhibits in vitro phosphorylation of bovine
RT rhodopsin.";
RL J. Biol. Chem. 271:10256-10262(1996).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30865587; DOI=10.7554/elife.38114;
RA Chen K.F., Lowe S., Lamaze A., Kraetschmer P., Jepson J.;
RT "Neurocalcin regulates nighttime sleep and arousal in Drosophila.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Calcium-binding protein that is essential for promoting
CC night-time sleep and inhibiting nocturnal hyperactivity
CC (PubMed:7989365, PubMed:30865587). During the night-time it promotes
CC sleep by limiting synaptic output from arousal- and wake-promoting
CC neurons within the C01- and A05- domains that include the mushroom
CC body, and the antennal mechanosensory and motor center
CC (PubMed:30865587). Regulated by the circadian clock network and light-
CC sensing circuits that include the CRY photoreceptor; it is likely that
CC both of these internal and external cues are required to define the
CC temporal window (the night-time) during which this protein functions
CC (PubMed:30865587). Inhibits the phosphorylation of rhodopsin in a
CC calcium-dependent manner (PubMed:8626592).
CC {ECO:0000269|PubMed:30865587, ECO:0000269|PubMed:7989365,
CC ECO:0000269|PubMed:8626592}.
CC -!- INTERACTION:
CC P42325; Q4V3Y0: CG15149; NbExp=4; IntAct=EBI-149848, EBI-15122292;
CC P42325; Q9W221: Dmel\CG13510; NbExp=4; IntAct=EBI-149848, EBI-130463;
CC P42325; P54192: Obp19d; NbExp=4; IntAct=EBI-149848, EBI-26770067;
CC -!- TISSUE SPECIFICITY: Expressed in neuronal tissues. High level
CC expression seen in the cortical regions of the central brain and lower
CC levels in the lamina, the first optic lobe of the brain. It is also
CC found in the thoracic ganglia. {ECO:0000269|PubMed:7989365}.
CC -!- DEVELOPMENTAL STAGE: Found in the embryos, larvae and pupae. Expression
CC in the adult heads is higher than in the bodies.
CC {ECO:0000269|PubMed:7989365}.
CC -!- MASS SPECTROMETRY: Mass=21975.51; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8626592};
CC -!- DISRUPTION PHENOTYPE: Viable. Adults exhibit reduced night-time sleep
CC but daytime sleep appears normal. RNAi-mediated knockdown in the whole
CC organism or simultaneously knockdown in the C01 and A05 neurons,
CC results in a similar phenotype to the genetic knockout. As demonstrated
CC in adults undergoing RNAi-mediated knockdown in the C01 and A05
CC neurons, the reduction in night-time sleep and increase in night-time
CC arousal is likely the result of enhanced neurotransmitter release in
CC the mushroom body alpha-beta lobes, and the antennal mechanosensory and
CC motor center, which occurs only during the dark period of different
CC light-dark conditions. RNAi-mediated knockdown in a tim mutant
CC background, also results in sleep loss during the dark period of
CC different light-dark conditions but under constant light conditions
CC sleep loss is completely suppressed. RNAi-mediated knockdown in a cry
CC mutant background, results in a small but significant reduction in
CC sleep under LL conditions. {ECO:0000269|PubMed:30865587}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; U15735; AAA62152.1; -; mRNA.
DR EMBL; AE014296; AAF49082.1; -; Genomic_DNA.
DR EMBL; AY071612; AAL49234.1; -; mRNA.
DR PIR; A55666; A55666.
DR RefSeq; NP_788543.1; NM_176365.3.
DR AlphaFoldDB; P42325; -.
DR SMR; P42325; -.
DR BioGRID; 65453; 16.
DR DIP; DIP-19235N; -.
DR IntAct; P42325; 44.
DR STRING; 7227.FBpp0074671; -.
DR iPTMnet; P42325; -.
DR PaxDb; P42325; -.
DR PRIDE; P42325; -.
DR DNASU; 40186; -.
DR EnsemblMetazoa; FBtr0074902; FBpp0074671; FBgn0013303.
DR GeneID; 40186; -.
DR KEGG; dme:Dmel_CG7641; -.
DR UCSC; CG7641-RA; d. melanogaster.
DR CTD; 40186; -.
DR FlyBase; FBgn0013303; Nca.
DR VEuPathDB; VectorBase:FBgn0013303; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158862; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; P42325; -.
DR OMA; MGCVCMK; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; P42325; -.
DR Reactome; R-DME-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-DME-451308; Activation of Ca-permeable Kainate Receptor.
DR SignaLink; P42325; -.
DR BioGRID-ORCS; 40186; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 40186; -.
DR PRO; PR:P42325; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0013303; Expressed in head capsule and 25 other tissues.
DR Genevisible; P42325; DM.
DR GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
DR GO; GO:1902848; P:negative regulation of neuronal signal transduction; IMP:UniProtKB.
DR GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IMP: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; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Lipoprotein; Metal-binding; Myristate; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..190
FT /note="Neurocalcin homolog"
FT /id="PRO_0000073801"
FT DOMAIN 40..58
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 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 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:0000269|PubMed:8626592"
SQ SEQUENCE 190 AA; 21894 MW; F1158FEB8CF13F64 CRC64;
MGKQNSKLKP EVLEDLKQNT EFTDAEIQEW YKGFLKDCPS GHLSVEEFKK IYGNFFPYGD
ASKFAEHVFR TFDANGDGTI DFREFLCALS VTSRGKLEQK LKWAFSMYDL DGNGYISRQE
MLEIVTAIYK MVGSVMKMPE DESTPEKRTD KIFRQMDRNK DGKLSLEEFI EGAKSDPSIV
RLLQCDPQSH
