KIC_ARATH
ID KIC_ARATH Reviewed; 135 AA.
AC Q9ZPX9; Q8L9A5; Q94EH6;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Calcium-binding protein KIC {ECO:0000303|PubMed:14688294};
DE AltName: Full=KCBP-interacting calcium-binding protein {ECO:0000303|PubMed:14688294};
GN Name=KIC {ECO:0000303|PubMed:14688294};
GN OrderedLocusNames=At2g46600 {ECO:0000312|Araport:AT2G46600};
GN ORFNames=F13A10.13 {ECO:0000312|EMBL:AAD20170.2};
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, TISSUE SPECIFICITY, AND INTERACTION
RP WITH KCBP.
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 INTERACTION WITH CML42.
RX PubMed=19720824; DOI=10.1074/jbc.m109.056770;
RA Dobney S., Chiasson D., Lam P., Smith S.P., Snedden W.A.;
RT "The calmodulin-related calcium sensor CML42 plays a role in trichome
RT branching.";
RL J. Biol. Chem. 284:31647-31657(2009).
RN [7]
RP INTERACTION WITH ABCG36.
RC STRAIN=cv. Columbia;
RX PubMed=26315018; DOI=10.1111/nph.13582;
RA Campe R., Langenbach C., Leissing F., Popescu G.V., Popescu S.C.,
RA Goellner K., Beckers G.J., Conrath U.;
RT "ABC transporter PEN3/PDR8/ABCG36 interacts with calmodulin that, like
RT PEN3, is required for Arabidopsis nonhost resistance.";
RL New Phytol. 209:294-306(2016).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH CALCIUM ION AND
RP KCBP.
RX PubMed=19416847; DOI=10.1073/pnas.0811131106;
RA Vinogradova M.V., Malanina G.G., Reddy A.S., Fletterick R.J.;
RT "Structure of the complex of a mitotic kinesin with its calcium binding
RT regulator.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8175-8179(2009).
CC -!- FUNCTION: Calcium-binding regulatory protein that interacts with
CC kinesin motor protein KCBP in a calcium-dependent manner. Inhibits KCBP
CC microtubule binding activity and microtubule-stimulated ATPase
CC activity. Involved in the regulation of trichome branching through its
CC interaction with KCBP. {ECO:0000269|PubMed:14688294}.
CC -!- SUBUNIT: Interacts with KCBP (via C-terminus). KIC and calmodulin show
CC competitive binding to KCBP. Interacts with CML42. Binds to ABCG36
CC (PubMed:26315018). {ECO:0000269|PubMed:14688294,
CC ECO:0000269|PubMed:19416847, ECO:0000269|PubMed:19720824,
CC ECO:0000269|PubMed:26315018}.
CC -!- INTERACTION:
CC Q9ZPX9; Q9SVG9: CML42; NbExp=4; IntAct=EBI-2353491, EBI-2434394;
CC Q9ZPX9; Q9FHN8: KIN14E; NbExp=5; IntAct=EBI-2353491, EBI-1749651;
CC Q9ZPX9; Q9FHN8-1: KIN14E; NbExp=2; IntAct=EBI-2353491, EBI-15777922;
CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves and flowers.
CC {ECO:0000269|PubMed:14688294}.
CC -!- MISCELLANEOUS: Plants overexpressing KIC1 causes a reduction in the
CC number of trichome branches.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM66085.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY363866; AAR17001.1; -; mRNA.
DR EMBL; AC006418; AAD20170.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10727.1; -; Genomic_DNA.
DR EMBL; AF410313; AAK95299.1; -; mRNA.
DR EMBL; AY093725; AAM10349.1; -; mRNA.
DR EMBL; AY088553; AAM66085.1; ALT_INIT; mRNA.
DR PIR; H84904; H84904.
DR RefSeq; NP_566082.1; NM_130225.3.
DR PDB; 3H4S; X-ray; 2.40 A; E=1-135.
DR PDBsum; 3H4S; -.
DR AlphaFoldDB; Q9ZPX9; -.
DR SMR; Q9ZPX9; -.
DR BioGRID; 4607; 3.
DR DIP; DIP-52859N; -.
DR IntAct; Q9ZPX9; 2.
DR STRING; 3702.AT2G46600.1; -.
DR PaxDb; Q9ZPX9; -.
DR PRIDE; Q9ZPX9; -.
DR ProteomicsDB; 250668; -.
DR EnsemblPlants; AT2G46600.1; AT2G46600.1; AT2G46600.
DR GeneID; 819272; -.
DR Gramene; AT2G46600.1; AT2G46600.1; AT2G46600.
DR KEGG; ath:AT2G46600; -.
DR Araport; AT2G46600; -.
DR TAIR; locus:2039969; AT2G46600.
DR eggNOG; KOG0028; Eukaryota.
DR HOGENOM; CLU_137017_0_0_1; -.
DR InParanoid; Q9ZPX9; -.
DR OMA; MQDAEVW; -.
DR OrthoDB; 1575398at2759; -.
DR PhylomeDB; Q9ZPX9; -.
DR EvolutionaryTrace; Q9ZPX9; -.
DR PRO; PR:Q9ZPX9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZPX9; baseline and differential.
DR Genevisible; Q9ZPX9; AT.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0010091; P:trichome branching; IMP:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Metal-binding; Reference proteome.
FT CHAIN 1..135
FT /note="Calcium-binding protein KIC"
FT /id="PRO_0000403272"
FT DOMAIN 74..109
FT /note="EF-hand"
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 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:3H4S"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:3H4S"
SQ SEQUENCE 135 AA; 15168 MW; 2D7A9E3971F3697B CRC64;
MEPTEKSMLL ETTSTTKMET KYEDMLPVMA EKMDVEEFVS ELCKGFSLLA DPERHLITAE
SLRRNSGILG IEGMSKEDAQ GMVREGDLDG DGALNQTEFC VLMVRLSPEM MEDAETWLEK
ALTQELCNHN LSSMP
