CARP1_ARATH
ID CARP1_ARATH Reviewed; 130 AA.
AC O81831;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Calcium-binding protein KRP1 {ECO:0000305};
DE AltName: Full=KIC-related protein 1 {ECO:0000303|PubMed:14688294};
GN Name=KRP1 {ECO:0000303|PubMed:14688294};
GN OrderedLocusNames=At4g27280 {ECO:0000312|Araport:AT4G27280};
GN ORFNames=M4I22.90 {ECO:0000312|EMBL:CAA19722.1};
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], AND FUNCTION.
RX PubMed=14688294; DOI=10.1105/tpc.016600;
RA Reddy V.S., Day I.S., Thomas T., Reddy A.S.N.;
RT "KIC, a novel Ca2+ binding protein with one EF-hand motif, interacts with a
RT microtubule motor protein and regulates trichome morphogenesis.";
RL Plant Cell 16:185-200(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION BY CHR12.
RX PubMed=17605754; DOI=10.1111/j.1365-313x.2007.03185.x;
RA Mlynarova L., Nap J.-P., Bisseling T.;
RT "The SWI/SNF chromatin-remodeling gene AtCHR12 mediates temporary growth
RT arrest in Arabidopsis thaliana upon perceiving environmental stress.";
RL Plant J. 51:874-885(2007).
CC -!- FUNCTION: Potential calcium sensor that binds calcium in vitro.
CC {ECO:0000269|PubMed:14688294}.
CC -!- INDUCTION: By CHR12. {ECO:0000269|PubMed:17605754}.
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DR EMBL; AY363867; AAR16085.1; -; mRNA.
DR EMBL; AL030978; CAA19722.1; -; Genomic_DNA.
DR EMBL; AL161566; CAB79583.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85320.1; -; Genomic_DNA.
DR EMBL; AY058165; AAL25579.1; -; mRNA.
DR EMBL; AY098973; AAM19983.1; -; mRNA.
DR EMBL; AY085115; AAM61669.1; -; mRNA.
DR PIR; T05752; T05752.
DR RefSeq; NP_194458.1; NM_118862.3.
DR AlphaFoldDB; O81831; -.
DR SMR; O81831; -.
DR IntAct; O81831; 1.
DR STRING; 3702.AT4G27280.1; -.
DR PaxDb; O81831; -.
DR PRIDE; O81831; -.
DR ProteomicsDB; 223925; -.
DR EnsemblPlants; AT4G27280.1; AT4G27280.1; AT4G27280.
DR GeneID; 828836; -.
DR Gramene; AT4G27280.1; AT4G27280.1; AT4G27280.
DR KEGG; ath:AT4G27280; -.
DR Araport; AT4G27280; -.
DR TAIR; locus:2131759; AT4G27280.
DR eggNOG; KOG0028; Eukaryota.
DR HOGENOM; CLU_137017_1_0_1; -.
DR InParanoid; O81831; -.
DR OMA; RCMIKEG; -.
DR OrthoDB; 1495109at2759; -.
DR PhylomeDB; O81831; -.
DR PRO; PR:O81831; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81831; baseline and differential.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009733; P:response to auxin; IDA:TAIR.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR044205; KIC/PBP1/KRP1.
DR PANTHER; PTHR47319; PTHR47319; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Metal-binding; Reference proteome.
FT CHAIN 1..130
FT /note="Calcium-binding protein KRP1"
FT /id="PRO_0000443736"
FT DOMAIN 72..107
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 130 AA; 14503 MW; 543443C26D0657DE CRC64;
MASPKSPTRP TQQNPQPNFH DFLPTMAGNL GGEGLIGELC NGFELLMDRE KGVITFESLR
RNAAAVLGLG DLTDEDVRCM IKEGDFDCDG ALNQMEFCVL MFRLSPDLME ASRCLVTEVI
EEEFGFTRRH
