CP1_ARATH
ID CP1_ARATH Reviewed; 160 AA.
AC Q9FDX6; O22368;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Calcium-binding protein CP1;
DE AltName: Full=NaCl-inducible Ca2+-binding protein {ECO:0000303|PubMed:9678579};
DE Short=AtCP1 {ECO:0000303|PubMed:9678579};
GN Name=CP1 {ECO:0000303|PubMed:9678579};
GN Synonyms=ACP1 {ECO:0000312|EMBL:AAC27657.1};
GN OrderedLocusNames=At5g49480 {ECO:0000312|Araport:AT5G49480};
GN ORFNames=K6M13.2 {ECO:0000312|EMBL:BAB10761.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION BY SALT STRESS.
RC STRAIN=cv. Columbia;
RX PubMed=9678579; DOI=10.1023/a:1006043006211;
RA Jang H.J., Pih K.T., Kang S.G., Lim J.H., Jin J.B., Piao H.L., Hwang I.;
RT "Molecular cloning of a novel Ca2+-binding protein that is induced by NaCl
RT stress.";
RL Plant Mol. Biol. 37:839-847(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP INDUCTION BY SALT STRESS.
RX PubMed=11351099; DOI=10.1104/pp.126.1.363;
RA Gong Z., Koiwa H., Cushman M.A., Ray A., Bufford D., Kore-eda S.,
RA Matsumoto T.K., Zhu J., Cushman J.C., Bressan R.A., Hasegawa P.M.;
RT "Genes that are uniquely stress regulated in salt overly sensitive (sos)
RT mutants.";
RL Plant Physiol. 126:363-375(2001).
CC -!- FUNCTION: Binds calcium in vitro. {ECO:0000269|PubMed:9678579}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9678579}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers.
CC {ECO:0000269|PubMed:9678579}.
CC -!- INDUCTION: Induced by salt stress. {ECO:0000269|PubMed:11351099,
CC ECO:0000269|PubMed:9678579}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC27657.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF009228; AAC27657.1; ALT_FRAME; mRNA.
DR EMBL; AB023033; BAB10761.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95819.1; -; Genomic_DNA.
DR EMBL; AF325028; AAG40380.1; -; mRNA.
DR EMBL; AF378884; AAK55687.1; -; mRNA.
DR EMBL; AY052740; AAK96454.1; -; mRNA.
DR RefSeq; NP_199759.1; NM_124325.3.
DR AlphaFoldDB; Q9FDX6; -.
DR SMR; Q9FDX6; -.
DR STRING; 3702.AT5G49480.1; -.
DR iPTMnet; Q9FDX6; -.
DR PaxDb; Q9FDX6; -.
DR PRIDE; Q9FDX6; -.
DR ProteomicsDB; 224400; -.
DR EnsemblPlants; AT5G49480.1; AT5G49480.1; AT5G49480.
DR GeneID; 835008; -.
DR Gramene; AT5G49480.1; AT5G49480.1; AT5G49480.
DR KEGG; ath:AT5G49480; -.
DR Araport; AT5G49480; -.
DR TAIR; locus:2157864; AT5G49480.
DR eggNOG; KOG0027; Eukaryota.
DR HOGENOM; CLU_1689852_0_0_1; -.
DR InParanoid; Q9FDX6; -.
DR OMA; EMEGMIS; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; Q9FDX6; -.
DR PRO; PR:Q9FDX6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FDX6; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; IEP:TAIR.
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 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; Cytoplasm; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..160
FT /note="Calcium-binding protein CP1"
FT /id="PRO_0000443502"
FT DOMAIN 22..49
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 52..87
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 93..128
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 160 AA; 17211 MW; F3461AF2388E291C CRC64;
MCPSGRIAIP ITTTANPNFR PAFEIIDTDH DGKISSDDLR AFYAGIPSGE NNDETMIGTM
ISVADANKDG FVEFDEFEKV LETTPFSRSG NGGDDGLMKD VFKVMDKDGD GRLSYGDLKS
YMDSAGLAVT DDEIKSMIRL AGGDLNDGVS FDGLLKIFGC
