NCS1_LYMST
ID NCS1_LYMST Reviewed; 191 AA.
AC Q3YLA4;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Neuronal calcium sensor 1 {ECO:0000312|EMBL:AAZ66779.2};
DE Short=NCS-1 {ECO:0000303|PubMed:18039973};
OS Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Lymnaeidae; Lymnaea.
OX NCBI_TaxID=6523;
RN [1] {ECO:0000305|PubMed:18039973, ECO:0000312|EMBL:AAZ66779.2}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=CNS {ECO:0000312|EMBL:AAZ66779.2};
RX PubMed=18039973; DOI=10.1242/dev.008979;
RA Hui K., Fei G.H., Saab B.J., Su J., Roder J.C., Feng Z.P.;
RT "Neuronal calcium sensor-1 modulation of optimal calcium level for neurite
RT outgrowth.";
RL Development 134:4479-4489(2007).
CC -!- FUNCTION: Neuronal calcium sensor, regulator of G protein-coupled
CC receptor phosphorylation in a calcium dependent manner (By similarity).
CC Regulates neurite extension and branching by activity-dependent Ca(2+)
CC influx in growth cones. {ECO:0000250|UniProtKB:P62166,
CC ECO:0000269|PubMed:18039973}.
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:18039973}. Cell
CC projection {ECO:0000269|PubMed:18039973}. Cell projection, growth cone
CC {ECO:0000269|PubMed:18039973}. Note=In pedal neurons, higher expression
CC in secondary neurites, perikarya, growth cones and branch points than
CC in primary neurites. {ECO:0000269|PubMed:18039973}.
CC -!- MISCELLANEOUS: Binds 3 calcium ions via the second, third and fourth
CC EF-hand. {ECO:0000250|UniProtKB:P62166}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000255}.
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DR EMBL; DQ099793; AAZ66779.2; -; mRNA.
DR AlphaFoldDB; Q3YLA4; -.
DR SMR; Q3YLA4; -.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Calcium; Cell projection; Lipoprotein; Metal-binding; Myristate;
KW Neurogenesis; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..191
FT /note="Neuronal calcium sensor 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000423516"
FT DOMAIN 24..59
FT /note="EF-hand 1"
FT /evidence="ECO:0000250|UniProtKB:P62166"
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 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:0000255"
SQ SEQUENCE 191 AA; 22182 MW; 2C2E467D0EFBB4A8 CRC64;
MGKRASKLRP EEVDELKAHT YFTESEIKQW HKGFRKDCPD GKLTLEGFTK IYQQFFPFGD
PSKFANFVFN VFDENKDGFI SFSEFLQALS VTSRGTVEEK LKWAFRLYDL DNDGYITRDE
LLDIVDAIYR MVGESVTLPE EENTPEKRVN RIFQVMDKNK DDQLTFEEFL EGSKEDPTII
QALTLCDSGQ A
