NCS1_CHICK
ID NCS1_CHICK Reviewed; 190 AA.
AC P62167; P36610; Q9UK26;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Neuronal calcium sensor 1;
DE Short=NCS-1;
DE AltName: Full=Frequenin homolog;
DE AltName: Full=Frequenin-like protein;
DE AltName: Full=Frequenin-like ubiquitous protein;
GN Name=NCS1; Synonyms=FLUP, FREQ;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7488079; DOI=10.1006/bbrc.1995.2601;
RA de Castro E., Nef S., Fiumelli H., Lenz S.E., Kawamura S., Nef P.;
RT "Regulation of rhodopsin phosphorylation by a family of neuronal calcium
RT sensors.";
RL Biochem. Biophys. Res. Commun. 216:133-140(1995).
RN [2]
RP CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=8903951; DOI=10.3109/10799899509045227;
RA Nef S., Fiumelli H., de Castro E., Raes M.-B., Nef P.;
RT "Identification of neuronal calcium sensor (NCS-1) possibly involved in the
RT regulation of receptor phosphorylation.";
RL J. Recept. Signal Transduct. 15:365-378(1995).
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.
CC -!- SUBUNIT: Interacts with KCND2. {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Post-mitotic neurons in the central and peripheral
CC nervous system.
CC -!- DEVELOPMENTAL STAGE: Found in embryo from embryonic day E3 to adult
CC stages.
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; L27420; AAA85633.1; -; mRNA.
DR RefSeq; NP_990708.1; NM_205377.1.
DR RefSeq; XP_015134825.1; XM_015279339.1.
DR AlphaFoldDB; P62167; -.
DR BMRB; P62167; -.
DR SMR; P62167; -.
DR STRING; 9031.ENSGALP00000020720; -.
DR PaxDb; P62167; -.
DR Ensembl; ENSGALT00000020749; ENSGALP00000020720; ENSGALG00000012710.
DR GeneID; 396336; -.
DR KEGG; gga:396336; -.
DR CTD; 23413; -.
DR VEuPathDB; HostDB:geneid_396336; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000154645; -.
DR HOGENOM; CLU_072366_1_2_1; -.
DR InParanoid; P62167; -.
DR OMA; EYVFNVF; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; P62167; -.
DR PRO; PR:P62167; -.
DR Proteomes; UP000000539; Chromosome 17.
DR Bgee; ENSGALG00000012710; Expressed in brain and 10 other tissues.
DR ExpressionAtlas; P62167; baseline and differential.
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; TAS:UniProtKB.
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"
FT CHAIN 2..190
FT /note="Neuronal calcium sensor 1"
FT /id="PRO_0000073791"
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 36..47
FT /note="Ancestral calcium site 1"
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:0000250"
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
