NCS1_YEAST
ID NCS1_YEAST Reviewed; 190 AA.
AC Q06389; D6VT04;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Calcium-binding protein NCS-1;
GN Name=FRQ1; Synonyms=NCS1; OrderedLocusNames=YDR373W; ORFNames=D9481.6;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, INTERACTION WITH PIK1, MUTAGENESIS OF GLY-2, AND MYRISTOYLATION
RP AT GLY-2.
RX PubMed=10559922; DOI=10.1038/12058;
RA Hendricks K.B., Wang B.Q., Schnieders E.A., Thorner J.;
RT "Yeast homologue of neuronal frequenin is a regulator of
RT phosphatidylinositol-4-OH kinase.";
RL Nat. Cell Biol. 1:234-241(1999).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP STRUCTURE BY NMR IN COMPLEX WITH CALCIUM IONS AND PIK1, INTERACTION WITH
RP PIK1, CALCIUM-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=11015193; DOI=10.1021/bi0012890;
RA Ames J.B., Hendricks K.B., Strahl T., Huttner I.G., Hamasaki N.,
RA Thorner J.;
RT "Structure and calcium-binding properties of Frq1, a novel calcium sensor
RT in the yeast Saccharomyces cerevisiae.";
RL Biochemistry 39:12149-12161(2000).
CC -!- FUNCTION: Regulator of phosphatidylinositol 4-kinase PIK1.
CC {ECO:0000269|PubMed:10559922}.
CC -!- SUBUNIT: Binds PIK1. {ECO:0000269|PubMed:11015193}.
CC -!- INTERACTION:
CC Q06389; P53112: PEX14; NbExp=3; IntAct=EBI-11946, EBI-13212;
CC Q06389; P39104: PIK1; NbExp=3; IntAct=EBI-11946, EBI-13423;
CC -!- SUBCELLULAR LOCATION: Bud membrane {ECO:0000269|PubMed:11015193};
CC Peripheral membrane protein {ECO:0000269|PubMed:11015193}. Note=Buds
CC and bud scars.
CC -!- MISCELLANEOUS: Binds 3 calcium ions via the second, third and fourth
CC EF-hand.
CC -!- MISCELLANEOUS: Present with 7160 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; U28373; AAB64809.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12214.1; -; Genomic_DNA.
DR PIR; S61168; S61168.
DR RefSeq; NP_010661.3; NM_001180681.3.
DR PDB; 1FPW; NMR; -; A=1-190.
DR PDB; 2JU0; NMR; -; A=1-190.
DR PDBsum; 1FPW; -.
DR PDBsum; 2JU0; -.
DR AlphaFoldDB; Q06389; -.
DR BMRB; Q06389; -.
DR SMR; Q06389; -.
DR BioGRID; 32432; 295.
DR DIP; DIP-2733N; -.
DR IntAct; Q06389; 38.
DR MINT; Q06389; -.
DR STRING; 4932.YDR373W; -.
DR iPTMnet; Q06389; -.
DR MaxQB; Q06389; -.
DR PaxDb; Q06389; -.
DR PRIDE; Q06389; -.
DR EnsemblFungi; YDR373W_mRNA; YDR373W; YDR373W.
DR GeneID; 851979; -.
DR KEGG; sce:YDR373W; -.
DR SGD; S000002781; FRQ1.
DR VEuPathDB; FungiDB:YDR373W; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000166508; -.
DR HOGENOM; CLU_072366_1_2_1; -.
DR InParanoid; Q06389; -.
DR OMA; EYVFNVF; -.
DR BioCyc; YEAST:G3O-29923-MON; -.
DR Reactome; R-SCE-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR EvolutionaryTrace; Q06389; -.
DR PRO; PR:Q06389; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06389; protein.
DR GO; GO:0033101; C:cellular bud membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008047; F:enzyme activator activity; IDA:SGD.
DR GO; GO:0043128; P:positive regulation of 1-phosphatidylinositol 4-kinase activity; IMP:SGD.
DR GO; GO:0009966; P:regulation of signal transduction; IMP:SGD.
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; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..190
FT /note="Calcium-binding protein NCS-1"
FT /id="PRO_0000073795"
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 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:10559922"
FT MUTAGEN 2
FT /note="G->A: Abolishes N-myristoylation."
FT /evidence="ECO:0000269|PubMed:10559922"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:2JU0"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:1FPW"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:1FPW"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:1FPW"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:1FPW"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:1FPW"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:1FPW"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:1FPW"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:1FPW"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1FPW"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:1FPW"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1FPW"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:1FPW"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:1FPW"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1FPW"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:1FPW"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:1FPW"
SQ SEQUENCE 190 AA; 22011 MW; 5E9D7F48F8AADA21 CRC64;
MGAKTSKLSK DDLTCLKQST YFDRREIQQW HKGFLRDCPS GQLAREDFVK IYKQFFPFGS
PEDFANHLFT VFDKDNNGFI HFEEFITVLS TTSRGTLEEK LSWAFELYDL NHDGYITFDE
MLTIVASVYK MMGSMVTLNE DEATPEMRVK KIFKLMDKNE DGYITLDEFR EGSKVDPSII
GALNLYDGLI
