NCS1_SCHPO
ID NCS1_SCHPO Reviewed; 190 AA.
AC Q09711;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Calcium-binding protein NCS-1;
GN Name=ncs1; ORFNames=SPAC18B11.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], STRUCTURE BY NMR, FUNCTION, SUBCELLULAR
RP LOCATION, MYRISTOYLATION AT GLY-2, CALCIUM-BINDING, AND MUTAGENESIS OF
RP GLY-2; GLU-84; GLU-120 AND GLU-168.
RC STRAIN=972 / ATCC 24843;
RX PubMed=14722091; DOI=10.1074/jbc.m311895200;
RA Hamasaki-Katagiri N., Molchanova T., Takeda K., Ames J.B.;
RT "Fission yeast homolog of neuronal calcium sensor-1 (Ncs1p) regulates
RT sporulation and confers calcium tolerance.";
RL J. Biol. Chem. 279:12744-12754(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Negatively regulates sporulation perhaps by controlling
CC Ca(2+)-dependent desensitization of git3.
CC {ECO:0000269|PubMed:14722091}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14722091};
CC Peripheral membrane protein {ECO:0000269|PubMed:14722091}.
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; AY225216; AAP48992.1; -; mRNA.
DR EMBL; CU329670; CAA90589.1; -; Genomic_DNA.
DR PIR; S58303; S58303.
DR RefSeq; NP_592879.1; NM_001018279.2.
DR PDB; 2L2E; NMR; -; A=2-190.
DR PDBsum; 2L2E; -.
DR AlphaFoldDB; Q09711; -.
DR BMRB; Q09711; -.
DR SMR; Q09711; -.
DR BioGRID; 278981; 3.
DR STRING; 4896.SPAC18B11.04.1; -.
DR iPTMnet; Q09711; -.
DR MaxQB; Q09711; -.
DR PaxDb; Q09711; -.
DR EnsemblFungi; SPAC18B11.04.1; SPAC18B11.04.1:pep; SPAC18B11.04.
DR GeneID; 2542523; -.
DR KEGG; spo:SPAC18B11.04; -.
DR PomBase; SPAC18B11.04; ncs1.
DR VEuPathDB; FungiDB:SPAC18B11.04; -.
DR eggNOG; KOG0044; Eukaryota.
DR HOGENOM; CLU_072366_1_2_1; -.
DR InParanoid; Q09711; -.
DR OMA; EYVFNVF; -.
DR PhylomeDB; Q09711; -.
DR Reactome; R-SPO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR EvolutionaryTrace; Q09711; -.
DR PRO; PR:Q09711; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0098744; F:1-phosphatidylinositol 4-kinase activator activity; IDA:PomBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:PomBase.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IDA:PomBase.
DR GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; IMP:PomBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; 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; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Reference proteome; Repeat; Sporulation.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..190
FT /note="Calcium-binding protein NCS-1"
FT /id="PRO_0000073794"
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 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:14722091"
FT MUTAGEN 2
FT /note="G->A: Nutrition insensitive sexual development."
FT /evidence="ECO:0000269|PubMed:14722091"
FT MUTAGEN 84
FT /note="E->Q: Growth defect at high levels of extracellular
FT calcium."
FT /evidence="ECO:0000269|PubMed:14722091"
FT MUTAGEN 120
FT /note="E->Q: Growth defect at high levels of extracellular
FT calcium."
FT /evidence="ECO:0000269|PubMed:14722091"
FT MUTAGEN 168
FT /note="E->Q: Growth defect at high levels of extracellular
FT calcium."
FT /evidence="ECO:0000269|PubMed:14722091"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:2L2E"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:2L2E"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:2L2E"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:2L2E"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2L2E"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:2L2E"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:2L2E"
FT HELIX 118..135
FT /evidence="ECO:0007829|PDB:2L2E"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:2L2E"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:2L2E"
FT HELIX 178..184
FT /evidence="ECO:0007829|PDB:2L2E"
SQ SEQUENCE 190 AA; 22033 MW; 2C82DCF096D0F787 CRC64;
MGKSQSKLSQ DQLQDLVRST RFDKKELQQW YKGFFKDCPS GHLNKSEFQK IYKQFFPFGD
PSAFAEYVFN VFDADKNGYI DFKEFICALS VTSRGELNDK LIWAFQLYDL DNNGLISYDE
MLRIVDAIYK MVGSMVKLPE DEDTPEKRVN KIFNMMDKNK DGQLTLEEFC EGSKRDPTIV
SALSLYDGLV
