NCS1_HUMAN
ID NCS1_HUMAN Reviewed; 190 AA.
AC P62166; E9PAY3; P36610; Q9UK26;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lindemeier J.R., Hauenschild A., Pongs O.;
RT "Frequenin-like Ca2+-binding protein (flup) modulates fast inactivation of
RT mammalian presynaptic A-type K-channel.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Bao X.G., Yu L., Zhao S.Y.;
RT "Cloning of a new human cDNA homologous to Rattus norvegicus neuronal
RT calcium sensor (NCS-1).";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Nef S.;
RL Submitted (JUN-1999) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Pongs O., Hauenschild A., Dannenberg J.;
RT "Sequence of human frequenin.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ovary, and Spinal ganglion;
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 [7]
RP INTERACTION WITH KCND2.
RX PubMed=11606724; DOI=10.1073/pnas.221168498;
RA Nakamura T.Y., Pountney D.J., Ozaita A., Nandi S., Ueda S., Rudy B.,
RA Coetzee W.A.;
RT "A role for frequenin, a Ca2+-binding protein, as a regulator of Kv4 K+-
RT currents.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12808-12813(2001).
RN [8]
RP INTERACTION WITH IL1RAPL1.
RX PubMed=12783849; DOI=10.1093/hmg/ddg147;
RA Bahi N., Friocourt G., Carrie A., Graham M.E., Weiss J.L., Chafey P.,
RA Fauchereau F., Burgoyne R.D., Chelly J.;
RT "IL1 receptor accessory protein like, a protein involved in X-linked mental
RT retardation, interacts with Neuronal Calcium Sensor-1 and regulates
RT exocytosis.";
RL Hum. Mol. Genet. 12:1415-1425(2003).
RN [9]
RP INTERACTION WITH ARF1; ARF3; ARF5 AND ARF6, AND SUBCELLULAR LOCATION.
RX PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x;
RA Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.;
RT "Specificity, promiscuity and localization of ARF protein interactions with
RT NCS-1 and phosphatidylinositol-4 kinase-III beta.";
RL Traffic 8:1080-1092(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), MUTAGENESIS OF GLU-81; THR-117 AND
RP THR-165, CALCIUM-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=11092894; DOI=10.1074/jbc.m009373200;
RA Bourne Y., Dannenberg J., Pollmann V., Marchot P., Pongs O.;
RT "Immunocytochemical localization and crystal structure of human frequenin
RT (neuronal calcium sensor 1).";
RL J. Biol. Chem. 276:11949-11955(2001).
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
CC (PubMed:11606724). Interacts in a calcium-independent manner with PI4KB
CC (By similarity). This binding competes with CALN2/CABP7 binding to
CC PI4KB (By similarity). Interacts in a calcium-dependent manner with
CC PICK1 (via AH domain) (By similarity). Interacts with ARF1, ARF3, ARF5
CC and ARF6 (PubMed:17555535). Interacts with IL1RAPL1 (PubMed:12783849).
CC {ECO:0000250|UniProtKB:P62168, ECO:0000269|PubMed:11606724,
CC ECO:0000269|PubMed:12783849, ECO:0000269|PubMed:17555535}.
CC -!- INTERACTION:
CC P62166; Q9BXJ5: C1QTNF2; NbExp=3; IntAct=EBI-746987, EBI-2817707;
CC P62166; Q96ST8-3: CEP89; NbExp=4; IntAct=EBI-746987, EBI-11144046;
CC P62166; Q03060-25: CREM; NbExp=3; IntAct=EBI-746987, EBI-12884642;
CC P62166; P78358: CTAG1B; NbExp=3; IntAct=EBI-746987, EBI-1188472;
CC P62166; Q86UW9: DTX2; NbExp=13; IntAct=EBI-746987, EBI-740376;
CC P62166; O75084: FZD7; NbExp=5; IntAct=EBI-746987, EBI-746917;
CC P62166; O95868: LY6G6D; NbExp=3; IntAct=EBI-746987, EBI-12382527;
CC P62166; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-746987, EBI-16439278;
CC P62166; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-746987, EBI-11988931;
CC P62166; P41271: NBL1; NbExp=3; IntAct=EBI-746987, EBI-10208650;
CC P62166; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-746987, EBI-12813389;
CC P62166; Q9UKN5: PRDM4; NbExp=3; IntAct=EBI-746987, EBI-2803427;
CC P62166; O60930: RNASEH1; NbExp=3; IntAct=EBI-746987, EBI-2372399;
CC P62166; Q8IWL1: SFTPA2; NbExp=3; IntAct=EBI-746987, EBI-12350685;
CC P62166; Q9Y336: SIGLEC9; NbExp=3; IntAct=EBI-746987, EBI-12857926;
CC P62166; P10451: SPP1; NbExp=3; IntAct=EBI-746987, EBI-723648;
CC P62166; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-746987, EBI-7082156;
CC P62166; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-746987, EBI-742550;
CC P62166; A0A1U9X8X8; NbExp=3; IntAct=EBI-746987, EBI-17234977;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:17555535}.
CC Postsynaptic density {ECO:0000305}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:11092894, ECO:0000269|PubMed:17555535}. Cytoplasm
CC {ECO:0000250|UniProtKB:P62168}. Cell membrane
CC {ECO:0000269|PubMed:17555535}; Peripheral membrane protein. Membrane
CC {ECO:0000250|UniProtKB:P62168}; Lipid-anchor {ECO:0000305}.
CC Note=Associated with Golgi stacks. Post-synaptic densities of
CC dendrites, and in the pre-synaptic nerve terminal at neuromuscular
CC junctions. {ECO:0000305, ECO:0000305|PubMed:17555535}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62166-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62166-2; Sequence=VSP_046312;
CC -!- MISCELLANEOUS: Binds 3 calcium ions via the second, third and fourth
CC EF-hand.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; X84048; CAA58867.1; -; mRNA.
DR EMBL; AF134479; AAP97256.1; -; mRNA.
DR EMBL; AF186409; AAF01804.1; -; mRNA.
DR EMBL; AL360004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004856; AAH04856.1; -; mRNA.
DR EMBL; BQ880305; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS6932.1; -. [P62166-1]
DR CCDS; CCDS78448.1; -. [P62166-2]
DR RefSeq; NP_001122298.1; NM_001128826.1. [P62166-2]
DR RefSeq; NP_055101.2; NM_014286.3. [P62166-1]
DR PDB; 1G8I; X-ray; 1.90 A; A/B=1-190.
DR PDB; 2LCP; NMR; -; A=1-190.
DR PDB; 4GUK; X-ray; 1.75 A; A/B/C/D=6-188.
DR PDB; 5O9S; X-ray; 2.70 A; C/D=2-9.
DR PDB; 6QI4; X-ray; 1.78 A; B/C=1-190.
DR PDBsum; 1G8I; -.
DR PDBsum; 2LCP; -.
DR PDBsum; 4GUK; -.
DR PDBsum; 5O9S; -.
DR PDBsum; 6QI4; -.
DR AlphaFoldDB; P62166; -.
DR BMRB; P62166; -.
DR SMR; P62166; -.
DR BioGRID; 116985; 74.
DR IntAct; P62166; 41.
DR MINT; P62166; -.
DR STRING; 9606.ENSP00000361475; -.
DR BindingDB; P62166; -.
DR ChEMBL; CHEMBL4295788; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR iPTMnet; P62166; -.
DR PhosphoSitePlus; P62166; -.
DR BioMuta; NCS1; -.
DR DMDM; 49065666; -.
DR EPD; P62166; -.
DR jPOST; P62166; -.
DR MassIVE; P62166; -.
DR MaxQB; P62166; -.
DR PaxDb; P62166; -.
DR PeptideAtlas; P62166; -.
DR PRIDE; P62166; -.
DR ProteomicsDB; 19104; -.
DR ProteomicsDB; 57369; -. [P62166-1]
DR TopDownProteomics; P62166-1; -. [P62166-1]
DR Antibodypedia; 4347; 372 antibodies from 38 providers.
DR DNASU; 23413; -.
DR Ensembl; ENST00000372398.6; ENSP00000361475.3; ENSG00000107130.10. [P62166-1]
DR Ensembl; ENST00000630865.1; ENSP00000486695.1; ENSG00000107130.10. [P62166-2]
DR GeneID; 23413; -.
DR KEGG; hsa:23413; -.
DR MANE-Select; ENST00000372398.6; ENSP00000361475.3; NM_014286.4; NP_055101.2.
DR UCSC; uc004bzi.2; human. [P62166-1]
DR CTD; 23413; -.
DR DisGeNET; 23413; -.
DR GeneCards; NCS1; -.
DR HGNC; HGNC:3953; NCS1.
DR HPA; ENSG00000107130; Tissue enhanced (brain).
DR MIM; 603315; gene.
DR neXtProt; NX_P62166; -.
DR OpenTargets; ENSG00000107130; -.
DR PharmGKB; PA28371; -.
DR VEuPathDB; HostDB:ENSG00000107130; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000154645; -.
DR HOGENOM; CLU_072366_1_2_1; -.
DR InParanoid; P62166; -.
DR OMA; EYVFNVF; -.
DR PhylomeDB; P62166; -.
DR TreeFam; TF300009; -.
DR PathwayCommons; P62166; -.
DR SignaLink; P62166; -.
DR SIGNOR; P62166; -.
DR BioGRID-ORCS; 23413; 8 hits in 1071 CRISPR screens.
DR ChiTaRS; NCS1; human.
DR EvolutionaryTrace; P62166; -.
DR GeneWiki; Neuronal_calcium_sensor-1; -.
DR GenomeRNAi; 23413; -.
DR Pharos; P62166; Tbio.
DR PRO; PR:P62166; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P62166; protein.
DR Bgee; ENSG00000107130; Expressed in right frontal lobe and 155 other tissues.
DR ExpressionAtlas; P62166; baseline and differential.
DR Genevisible; P62166; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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 3D-structure; Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Golgi apparatus; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Reference proteome; Repeat; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..190
FT /note="Neuronal calcium sensor 1"
FT /id="PRO_0000073788"
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:0000269|PubMed:12783849"
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:0000269|PubMed:25255805"
FT VAR_SEQ 1..22
FT /note="MGKSNSKLKPEVVEELTRKTYF -> MATI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046312"
FT MUTAGEN 81
FT /note="E->T: Reduces calcium binding; when associated with
FT A-117 or A-165. Abolishes calcium binding; when associated
FT with A-117 and A-165."
FT /evidence="ECO:0000269|PubMed:11092894"
FT MUTAGEN 117
FT /note="T->A: Reduces calcium binding; when associated with
FT T-81. Abolishes calcium binding; when associated with T-81
FT and A-165."
FT /evidence="ECO:0000269|PubMed:11092894"
FT MUTAGEN 165
FT /note="T->A: Reduces calcium binding; when associated with
FT A-117. Abolishes calcium binding; when associated with T-81
FT and A-117."
FT /evidence="ECO:0000269|PubMed:11092894"
FT CONFLICT 90
FT /note="S -> P (in Ref. 4; AAF01804)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="S -> P (in Ref. 4; AAF01804)"
FT /evidence="ECO:0000305"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2LCP"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:4GUK"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1G8I"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:4GUK"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4GUK"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:4GUK"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:4GUK"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:4GUK"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:4GUK"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:4GUK"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2LCP"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:6QI4"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:4GUK"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6QI4"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:4GUK"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:4GUK"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2LCP"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:4GUK"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:4GUK"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:4GUK"
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
