ID CALM1_ARATH Reviewed; 149 AA. AC P25854; Q03510; Q9FJ05; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-MAR-2010, entry version 103. DE RecName: Full=Calmodulin-1/4; DE Short=CaM-1/4; GN Name=CAM1; OrderedLocusNames=At5g37780; ORFNames=K22F20.2, T31G3.3; GN and GN Name=CAM4; OrderedLocusNames=At1g66410; ORFNames=T27F4.1, F28G11.13; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; malvids; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (CAM4). RX MEDLINE=93283627; PubMed=8507825; DOI=10.1007/BF00014930; RA Gawienowski M.C., Szymanski D., Perera I.Y., Zielinski R.E.; RT "Calmodulin isoforms in Arabidopsis encoded by multiple divergent RT mRNAs."; RL Plant Mol. Biol. 22:215-225(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (CAM1). RC STRAIN=cv. Columbia; RX MEDLINE=99087489; PubMed=9872454; DOI=10.1093/dnares/5.5.297; RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. RT Sequence features of the regions of 1,013,767 bp covered by sixteen RT physically assigned P1 and TAC clones."; RL DNA Res. 5:297-308(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (CAM4). RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CAM1 AND CAM4). RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., 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] (CAM4). 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 NUCLEOTIDE SEQUENCE [MRNA] OF 14-149 (CAM1). RX PubMed=16668320; RA Ling V., Perera I.Y., Zielinski R.E.; RT "Primary structures of Arabidopsis calmodulin isoforms deduced from RT the sequences of cDNA clones."; RL Plant Physiol. 96:1196-1202(1991). RN [7] RP GENE FAMILY, AND NOMENCLATURE. RX DOI=10.1046/j.1469-8137.2003.00845.x; RA McCormack E., Braam J.; RT "Calmodulins and related potential calcium sensors of Arabidopsis."; RL New Phytol. 159:585-598(2003). CC -!- FUNCTION: Calmodulin mediates the control of a large number of CC enzymes and other proteins by Ca(2+). Among the enzymes to be CC stimulated by the calmodulin-Ca(2+) complex are a number of CC protein kinases and phosphatases. CC -!- INTERACTION: CC O22179:-; NbExp=1; IntAct=EBI-1235664, EBI-1238013; CC P27450:-; NbExp=1; IntAct=EBI-1235664, EBI-1238108; CC Q29Q72:-; NbExp=1; IntAct=EBI-1235664, EBI-1238714; CC Q2V359:-; NbExp=2; IntAct=EBI-1235664, EBI-1235819; CC Q39130:-; NbExp=1; IntAct=EBI-1235664, EBI-1749651; CC Q3EAG3:-; NbExp=1; IntAct=EBI-1235664, EBI-1238312; CC Q3EBV7:-; NbExp=2; IntAct=EBI-1235664, EBI-1235683; CC Q4PSE3:-; NbExp=1; IntAct=EBI-1235664, EBI-1238507; CC Q7X9H6:-; NbExp=1; IntAct=EBI-1235664, EBI-1238497; CC Q7X9N2:-; NbExp=1; IntAct=EBI-1235664, EBI-622264; CC Q84W01:-; NbExp=1; IntAct=EBI-1235664, EBI-1238923; CC Q84WW1:-; NbExp=1; IntAct=EBI-1235664, EBI-1238751; CC Q8H1D6:-; NbExp=1; IntAct=EBI-1235664, EBI-1238166; CC Q8VZ70:-; NbExp=1; IntAct=EBI-1235664, EBI-1238078; CC Q8VZK4:-; NbExp=1; IntAct=EBI-1235664, EBI-1238776; CC Q93Z30:-; NbExp=1; IntAct=EBI-1235664, EBI-1237782; CC Q944J2:-; NbExp=1; IntAct=EBI-1235664, EBI-1238944; CC Q9FGX2:-; NbExp=1; IntAct=EBI-1235664, EBI-942623; CC Q9FGZ5:-; NbExp=1; IntAct=EBI-1235664, EBI-622281; CC Q9FIW6:-; NbExp=1; IntAct=EBI-1235664, EBI-1237967; CC Q9FL19:-; NbExp=1; IntAct=EBI-1235664, EBI-622440; CC Q9FLL0:-; NbExp=1; IntAct=EBI-1235664, EBI-1238516; CC Q9FM69:-; NbExp=1; IntAct=EBI-1235664, EBI-1238525; CC Q9FME9:-; NbExp=1; IntAct=EBI-1235664, EBI-1238771; CC Q9FMY3:-; NbExp=1; IntAct=EBI-1235664, EBI-1239013; CC Q9FUD3:-; NbExp=1; IntAct=EBI-1235664, EBI-942633; CC Q9LNX6:-; NbExp=1; IntAct=EBI-1235664, EBI-1238840; CC Q9LS24:-; NbExp=1; IntAct=EBI-1235664, EBI-1238916; CC Q9LW66:-; NbExp=1; IntAct=EBI-1235664, EBI-1238066; CC Q9LX56:-; NbExp=2; IntAct=EBI-1235664, EBI-1235891; CC Q9SJX8:-; NbExp=1; IntAct=EBI-1235664, EBI-1238001; CC Q9SKN2:-; NbExp=1; IntAct=EBI-1235664, EBI-1237944; CC Q9SL70:-; NbExp=1; IntAct=EBI-1235664, EBI-1238421; CC Q9M7Q2:ABF4; NbExp=1; IntAct=EBI-1235664, EBI-1237867; CC Q8LAW2:AFR; NbExp=1; IntAct=EBI-1235664, EBI-604438; CC Q38847:AGL15; NbExp=1; IntAct=EBI-1235664, EBI-622076; CC Q9SZJ6:AGL21; NbExp=1; IntAct=EBI-1235664, EBI-621986; CC Q4PSU4:AGL61; NbExp=1; IntAct=EBI-1235664, EBI-1237976; CC Q38876:AGL8; NbExp=1; IntAct=EBI-1235664, EBI-621912; CC Q9FJK3:AGL80; NbExp=1; IntAct=EBI-1235664, EBI-622424; CC Q70E96:ALDH3F1; NbExp=1; IntAct=EBI-1235664, EBI-1237774; CC O49839:APK2A; NbExp=1; IntAct=EBI-1235664, EBI-1238631; CC O49840:APK2B; NbExp=1; IntAct=EBI-1235664, EBI-1238651; CC Q39019:ASK10; NbExp=1; IntAct=EBI-1235664, EBI-1238904; CC Q39010:ASK6; NbExp=1; IntAct=EBI-1235664, EBI-1238323; CC Q56W43:At1g08320; NbExp=1; IntAct=EBI-1235664, EBI-1237844; CC O04567:At1g27190; NbExp=1; IntAct=EBI-1235664, EBI-1238687; CC Q9SGN7:At1g28390; NbExp=1; IntAct=EBI-1235664, EBI-1238190; CC Q9ZVM9:At1g54610; NbExp=2; IntAct=EBI-1235664, EBI-1235713; CC Q84WC8:At1g58110; NbExp=1; IntAct=EBI-1235664, EBI-1237819; CC Q9ZUI9:At1g60040; NbExp=1; IntAct=EBI-1235664, EBI-622185; CC Q9M9C3:At1g68380/T2E12_7; NbExp=1; IntAct=EBI-1235664, EBI-1238618; CC O80651:At1g77145; NbExp=1; IntAct=EBI-1235664, EBI-1238133; CC Q9SSC7:At1g80120; NbExp=1; IntAct=EBI-1235664, EBI-1238625; CC O48788:At2g26730; NbExp=1; IntAct=EBI-1235664, EBI-1239029; CC Q9SDB3:At2g43850; NbExp=1; IntAct=EBI-1235664, EBI-1238366; CC Q9M8T0:At3g02880; NbExp=1; IntAct=EBI-1235664, EBI-1238677; CC Q9M8W6:At3g04100; NbExp=1; IntAct=EBI-1235664, EBI-1238487; CC Q9M844:At3g04430; NbExp=1; IntAct=EBI-1235664, EBI-1238479; CC Q2VW98:At3g17600; NbExp=1; IntAct=EBI-1235664, EBI-1235997; CC Q9LJL9:At3g19100; NbExp=1; IntAct=EBI-1235664, EBI-1238393; CC O81292:AT4g02410; NbExp=1; IntAct=EBI-1235664, EBI-1237950; CC O22763:AT4g02640; NbExp=1; IntAct=EBI-1235664, EBI-969959; CC Q8GYP4:At4g18630/F28A21_40; NbExp=1; IntAct=EBI-1235664, EBI-1239007; CC Q9SZ03:AT4g34380; NbExp=1; IntAct=EBI-1235664, EBI-1238343; CC Q8LE56:At4g37240/C7A10_120; NbExp=1; IntAct=EBI-1235664, EBI-1237996; CC Q8GY88:At4g39540/F23K16_170; NbExp=1; IntAct=EBI-1235664, EBI-1238334; CC Q9FLV4:At5g24080; NbExp=1; IntAct=EBI-1235664, EBI-1238700; CC Q9FMC2:At5g38800; NbExp=1; IntAct=EBI-1235664, EBI-1237855; CC Q8GZ99:At5g49760/K2I5_13; NbExp=1; IntAct=EBI-1235664, EBI-1238218; CC Q9FFN7:At5g63770/MBK5.25; NbExp=1; IntAct=EBI-1235664, EBI-1238994; CC P92525:AtMg00870; NbExp=1; IntAct=EBI-1235664, EBI-1238547; CC Q9M2K4:BZIP61; NbExp=1; IntAct=EBI-1235664, EBI-1237830; CC Q39254:CAX2; NbExp=1; IntAct=EBI-1235664, EBI-1238729; CC Q8LG64:CDKB2-2; NbExp=2; IntAct=EBI-1235664, EBI-1235761; CC Q9LDI3:CIPK24; NbExp=2; IntAct=EBI-1235664, EBI-537551; CC O65554:CIPK6; NbExp=2; IntAct=EBI-1235664, EBI-537615; CC Q39050:CKI1; NbExp=1; IntAct=EBI-1235664, EBI-1237881; CC Q93Z27:CML45; NbExp=2; IntAct=EBI-1235664, EBI-1235938; CC Q42479:CPK3; NbExp=1; IntAct=EBI-1235664, EBI-1235782; CC Q9SSF8:CPK30; NbExp=2; IntAct=EBI-1235664, EBI-1235738; CC Q3E9X6:CRK21; NbExp=1; IntAct=EBI-1235664, EBI-1238983; CC Q9SYS3:CRK40; NbExp=1; IntAct=EBI-1235664, EBI-1238119; CC O65469:CRK9; NbExp=1; IntAct=EBI-1235664, EBI-1238158; CC Q38867:CYP19-3; NbExp=1; IntAct=EBI-1235664, EBI-1235851; CC Q9LJY7:CYP705A20; NbExp=1; IntAct=EBI-1235664, EBI-1237907; CC Q9SLP1:CYP78A9; NbExp=1; IntAct=EBI-1235664, EBI-1238437; CC O23552:dl4570w; NbExp=1; IntAct=EBI-1235664, EBI-1235805; CC Q9SND6:F11C1_150; NbExp=2; IntAct=EBI-1235664, EBI-1235872; CC Q9LFU3:F14F8_210; NbExp=1; IntAct=EBI-1235664, EBI-1237805; CC Q9LYL6:F18O21_230; NbExp=1; IntAct=EBI-1235664, EBI-1238139; CC O82754:F7H19.240; NbExp=1; IntAct=EBI-1235664, EBI-1238561; CC Q9ZPE4:FBW2; NbExp=1; IntAct=EBI-1235664, EBI-604740; CC Q8RWQ8:FBX14; NbExp=1; IntAct=EBI-1235664, EBI-1235922; CC P55737:HSP81-2; NbExp=2; IntAct=EBI-1235664, EBI-1235834; CC Q9C9Q4:JAC1; NbExp=1; IntAct=EBI-1235664, EBI-1238741; CC Q3ECN4:LRR-RLK; NbExp=1; IntAct=EBI-1235664, EBI-1238268; CC Q8VYG7:LRR-RLK; NbExp=1; IntAct=EBI-1235664, EBI-1238236; CC Q9LSI9:LRR-RLK; NbExp=1; IntAct=EBI-1235664, EBI-1238253; CC Q9M9C5:LRR-RLK; NbExp=1; IntAct=EBI-1235664, EBI-1238661; CC P43294:MHK; NbExp=1; IntAct=EBI-1235664, EBI-1238022; CC Q39021:MPK1; NbExp=1; IntAct=EBI-1235664, EBI-1238932; CC Q9C5C0:MPK18; NbExp=1; IntAct=EBI-1235664, EBI-1238534; CC Q0WPH8:NEK5; NbExp=1; IntAct=EBI-1235664, EBI-1238972; CC Q9LHI7:NEK7; NbExp=1; IntAct=EBI-1235664, EBI-1238055; CC Q9T074:PCKA; NbExp=1; IntAct=EBI-1235664, EBI-1238593; CC Q8W490:PEPKR2; NbExp=1; IntAct=EBI-1235664, EBI-1238381; CC Q9FIK0:PFK2; NbExp=1; IntAct=EBI-1235664, EBI-1238609; CC Q94AA4:PFK3; NbExp=1; IntAct=EBI-1235664, EBI-1238600; CC P83755:psbA; NbExp=2; IntAct=EBI-1235664, EBI-1236013; CC P93050:RKF3; NbExp=1; IntAct=EBI-1235664, EBI-1238281; CC Q9ZRF9:RPK1; NbExp=1; IntAct=EBI-1235664, EBI-1238953; CC Q9S7H5:SCL21; NbExp=1; IntAct=EBI-1235664, EBI-1238472; CC Q9FHZ1:SCL23; NbExp=1; IntAct=EBI-1235664, EBI-1238460; CC Q9FL03:SCL4; NbExp=1; IntAct=EBI-1235664, EBI-1238466; CC Q5XXJ3:SHP1; NbExp=1; IntAct=EBI-1235664, EBI-1237985; CC Q9LZP8:T12C14_120; NbExp=1; IntAct=EBI-1235664, EBI-942845; CC Q9LZV7:T20L15_160; NbExp=1; IntAct=EBI-1235664, EBI-1238200; CC Q9LQ65:T4M14.10; NbExp=1; IntAct=EBI-1235664, EBI-942986; CC Q39140:TGA6; NbExp=1; IntAct=EBI-1235664, EBI-541321; CC Q8RYD9:TT16; NbExp=1; IntAct=EBI-1235664, EBI-621993; CC Q8GYF5:WAKL21; NbExp=1; IntAct=EBI-1235664, EBI-1238355; CC Q8GY11:WRKY43; NbExp=2; IntAct=EBI-1235664, EBI-1235953; CC Q9SUP6:WRKY53; NbExp=2; IntAct=EBI-1235664, EBI-1235980; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences; CC Name=1; CC IsoId=P25854-1; Sequence=Displayed; CC -!- MISCELLANEOUS: This protein has four functional calcium-binding CC sites. CC -!- SIMILARITY: Belongs to the calmodulin family. CC -!- SIMILARITY: Contains 4 EF-hand domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z12022; CAA78057.1; -; mRNA. DR EMBL; AB016873; BAB10354.1; -; Genomic_DNA. DR EMBL; AB026662; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC020665; AAG52168.1; -; Genomic_DNA. DR EMBL; AC074025; AAG51164.1; -; Genomic_DNA. DR EMBL; AY059809; AAL24291.1; -; mRNA. DR EMBL; AF370293; AAK44108.1; -; mRNA. DR EMBL; AY048276; AAK82538.1; -; mRNA. DR EMBL; AY072520; AAL66935.1; -; mRNA. DR EMBL; AY072628; AAL62019.1; -; mRNA. DR EMBL; AY113902; AAM44950.1; -; mRNA. DR EMBL; AY088476; AAM66012.1; -; mRNA. DR EMBL; M38379; AAA32762.1; -; mRNA. DR IPI; IPI00520791; -. DR PIR; E96689; E96689. DR PIR; S35185; S35185. DR PIR; T50929; T50929. DR RefSeq; NP_176814.1; -. DR RefSeq; NP_198594.1; -. DR UniGene; At.23146; -. DR UniGene; At.294; -. DR UniGene; Rra.10933; -. DR UniGene; Rra.1222; -. DR UniGene; Rsa.10147; -. DR SMR; P25854; 1-148. DR IntAct; P25854; 126. DR MINT; MINT-222511; -. DR STRING; P25854; -. DR PRIDE; P25854; -. DR ProMEX; P25854; -. DR GeneID; 833756; -. DR GeneID; 842959; -. DR GenomeReviews; BA000015_GR; AT5G37780. DR GenomeReviews; CT485782_GR; AT1G66410. DR KEGG; ath:AT1G66410; -. DR TAIR; At1g66410; -. DR TAIR; At5g37780; -. DR eggNOG; KOG0027; -. DR HOGENOM; HBG746798; -. DR InParanoid; P25854; -. DR OMA; QVESKER; -. DR PhylomeDB; P25854; -. DR ArrayExpress; P25854; -. DR Genevestigator; P25854; -. DR GermOnline; AT5G37780; Arabidopsis thaliana. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0005886; C:plasma membrane; IDA:TAIR. DR GO; GO:0005509; F:calcium ion binding; TAS:TAIR. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0004871; F:signal transducer activity; TAS:TAIR. DR GO; GO:0009612; P:response to mechanical stimulus; IEP:TAIR. DR InterPro; IPR011992; EF-hand-like_dom. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR018249; EF_HAND_2. DR InterPro; IPR002048; EF_hand_Ca_bd. DR Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1. DR SMART; SM00054; EFh; 4. DR PROSITE; PS00018; EF_HAND_1; 4. DR PROSITE; PS50222; EF_HAND_2; 4. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Calcium; Complete proteome; KW Methylation; Repeat. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 149 Calmodulin-1/4. FT /FTId=PRO_0000198280. FT DOMAIN 8 43 EF-hand 1. FT DOMAIN 44 79 EF-hand 2. FT DOMAIN 81 116 EF-hand 3. FT DOMAIN 117 149 EF-hand 4. FT CA_BIND 21 32 1. FT CA_BIND 57 68 2. FT CA_BIND 94 105 3. FT CA_BIND 130 141 4. FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 116 116 N6,N6,N6-trimethyllysine (By similarity). FT CONFLICT 139 139 Y -> H (in Ref. 1; CAA78057). SQ SEQUENCE 149 AA; 16862 MW; 805B06B97552ECC1 CRC64; MADQLTDEQI SEFKEAFSLF DKDGDGCITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL NLMAKKMKDT DSEEELKEAF RVFDKDQNGF ISAAELRHVM TNLGEKLTDE EVEEMIREAD VDGDGQINYE EFVKIMMAK // ID CALM2_ARATH Reviewed; 149 AA. AC P25069; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-MAR-2010, entry version 109. DE RecName: Full=Calmodulin-2/3/5; DE Short=CaM-2/3/5; GN Name=CAM2; Synonyms=CAL1; OrderedLocusNames=At2g41110; GN ORFNames=T3K9.12; GN and GN Name=CAM3; OrderedLocusNames=At3g56800; ORFNames=T8M16.130; GN and GN Name=CAM5; Synonyms=TCH1; OrderedLocusNames=At2g27030; GN ORFNames=T20P8.8; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; malvids; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (CAM5). RX PubMed=16668320; RA Ling V., Perera I.Y., Zielinski R.E.; RT "Primary structures of Arabidopsis calmodulin isoforms deduced from RT the sequences of cDNA clones."; RL Plant Physiol. 96:1196-1202(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (CAM3). RX MEDLINE=92329725; PubMed=1627778; DOI=10.1007/BF00026791; RA Perera I.Y., Zielinski R.E.; RT "Structure and expression of the Arabidopsis CaM-3 calmodulin gene."; RL Plant Mol. Biol. 19:649-664(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CAM2). RC STRAIN=cv. C24; TISSUE=Seedling; RX MEDLINE=94227846; PubMed=8173593; RA Chandra A., Upadhyaya K.C.; RT "Structure and organization of a novel calmodulin gene of Arabidopsis RT thaliana."; RL Cell. Mol. Biol. Res. 39:509-516(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CAM2). RC STRAIN=cv. Landsberg erecta; RX MEDLINE=96104307; PubMed=8564305; RA Ito T., Hirano M., Akama K., Shimura Y., Okada K.; RT "Touch-inducible genes for calmodulin and a calmodulin-related protein RT are located in tandem on a chromosome of Arabidopsis thaliana."; RL Plant Cell Physiol. 36:1369-1373(1995). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (CAM2 AND CAM5). RC STRAIN=cv. Columbia; RX MEDLINE=20083487; 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., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (CAM3). RC STRAIN=cv. Columbia; RX MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CAM2; CAM3 AND CAM5). RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (CAM3). 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 [9] RP NUCLEOTIDE SEQUENCE OF 13-149 (CAM5). RC STRAIN=cv. Columbia; RX MEDLINE=90150263; PubMed=2302732; DOI=10.1016/0092-8674(90)90587-5; RA Braam J., Davis R.W.; RT "Rain-, wind-, and touch-induced expression of calmodulin and RT calmodulin-related genes in Arabidopsis."; RL Cell 60:357-364(1990). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-149 (CAM2). RX MEDLINE=93283627; PubMed=8507825; DOI=10.1007/BF00014930; RA Gawienowski M.C., Szymanski D., Perera I.Y., Zielinski R.E.; RT "Calmodulin isoforms in Arabidopsis encoded by multiple divergent RT mRNAs."; RL Plant Mol. Biol. 22:215-225(1993). RN [11] RP GENE FAMILY, AND NOMENCLATURE. RX DOI=10.1046/j.1469-8137.2003.00845.x; RA McCormack E., Braam J.; RT "Calmodulins and related potential calcium sensors of Arabidopsis."; RL New Phytol. 159:585-598(2003). CC -!- FUNCTION: Calmodulin mediates the control of a large number of CC enzymes and other proteins by Ca(2+). Among the enzymes to be CC stimulated by the calmodulin-Ca(2+) complex are a number of CC protein kinases and phosphatases. CC -!- INTERACTION: CC O82345:-; NbExp=3; IntAct=EBI-1397259, EBI-1397246; CC Q40828:- (xeno); NbExp=1; IntAct=EBI-1397259, EBI-2410566; CC Q9LD58:-; NbExp=2; IntAct=EBI-1397259, EBI-2112024; CC Q9SXP4:- (xeno); NbExp=1; IntAct=EBI-1397259, EBI-2410585; CC Q9FXS1:NtEIG-D48 (xeno); NbExp=1; IntAct=EBI-1397259, EBI-2410603; CC Q9SV15:WRKY11; NbExp=1; IntAct=EBI-1397259, EBI-2364969; CC O22176:WRKY15; NbExp=1; IntAct=EBI-1397259, EBI-2365008; CC Q9SJA8:WRKY17; NbExp=1; IntAct=EBI-1397259, EBI-2365037; CC O04336:WRKY21; NbExp=1; IntAct=EBI-1397259, EBI-1239118; CC Q9SR07:WRKY39; NbExp=1; IntAct=EBI-1397259, EBI-2365097; CC Q9STX0:WRKY7; NbExp=2; IntAct=EBI-1397259, EBI-2364652; CC Q93WU6:WRKY74; NbExp=1; IntAct=EBI-1397259, EBI-2365125; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences; CC Name=1; CC IsoId=P25069-1; Sequence=Displayed; CC -!- INDUCTION: By rain-, wind-, and touch (thigmomorphogenesis). CC -!- MISCELLANEOUS: This protein has four functional calcium-binding CC sites. CC -!- SIMILARITY: Belongs to the calmodulin family. CC -!- SIMILARITY: Contains 4 EF-hand domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M38380; AAA32763.1; -; mRNA. DR EMBL; X67273; CAA47690.1; -; Genomic_DNA. DR EMBL; D45848; BAA08283.1; -; Genomic_DNA. DR EMBL; M73711; AAA32764.1; -; Genomic_DNA. DR EMBL; M73712; AAA32765.1; -; mRNA. DR EMBL; Z12023; CAA78058.1; -; mRNA. DR EMBL; AC004261; AAD12000.1; -; Genomic_DNA. DR EMBL; AC005623; AAC77861.1; -; Genomic_DNA. DR EMBL; AL390921; CAC00743.1; -; Genomic_DNA. DR EMBL; AY046048; AAK76722.1; -; mRNA. DR EMBL; AY057567; AAL09806.1; -; mRNA. DR EMBL; AY065179; AAL38355.1; -; mRNA. DR EMBL; AY091301; AAM14240.1; -; mRNA. DR EMBL; AY128752; AAM91152.1; -; mRNA. DR EMBL; BT002351; AAN86184.1; -; mRNA. DR EMBL; AY085660; AAM62881.1; -; mRNA. DR IPI; IPI00525270; -. DR PIR; H84667; H84667. DR PIR; S22503; S22503. DR RefSeq; NP_180271.1; -. DR RefSeq; NP_191239.1; -. DR RefSeq; NP_850344.1; -. DR UniGene; At.23067; -. DR UniGene; At.23711; -. DR UniGene; At.48576; -. DR UniGene; At.67188; -. DR UniGene; At.67742; -. DR UniGene; At.69620; -. DR UniGene; Rra.154; -. DR UniGene; Rra.5939; -. DR UniGene; Rsa.11253; -. DR UniGene; Rsa.242; -. DR SMR; P25069; 1-148. DR IntAct; P25069; 16. DR MINT; MINT-1338785; -. DR STRING; P25069; -. DR ProMEX; P25069; -. DR GeneID; 817245; -. DR GeneID; 818710; -. DR GeneID; 824847; -. DR GenomeReviews; BA000014_GR; AT3G56800. DR GenomeReviews; CT485783_GR; AT2G27030. DR GenomeReviews; CT485783_GR; AT2G41110. DR KEGG; ath:AT2G27030; -. DR KEGG; ath:AT2G41110; -. DR KEGG; ath:AT3G56800; -. DR TAIR; At2g27030; -. DR TAIR; At2g41110; -. DR TAIR; At3g56800; -. DR eggNOG; KOG0027; -. DR HOGENOM; HBG746798; -. DR InParanoid; P25069; -. DR PhylomeDB; P25069; -. DR ArrayExpress; P25069; -. DR Genevestigator; P25069; -. DR GermOnline; AT2G41110; Arabidopsis thaliana. DR GO; GO:0005886; C:plasma membrane; IDA:TAIR. DR GO; GO:0005773; C:vacuole; IDA:TAIR. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0019722; P:calcium-mediated signaling; TAS:TAIR. DR GO; GO:0030163; P:protein catabolic process; TAS:TAIR. DR InterPro; IPR011992; EF-hand-like_dom. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR018249; EF_HAND_2. DR InterPro; IPR002048; EF_hand_Ca_bd. DR Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1. DR SMART; SM00054; EFh; 4. DR PROSITE; PS00018; EF_HAND_1; 4. DR PROSITE; PS50222; EF_HAND_2; 4. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Calcium; Complete proteome; KW Methylation; Repeat. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 149 Calmodulin-2/3/5. FT /FTId=PRO_0000198281. FT DOMAIN 8 43 EF-hand 1. FT DOMAIN 44 79 EF-hand 2. FT DOMAIN 81 116 EF-hand 3. FT DOMAIN 117 149 EF-hand 4. FT CA_BIND 21 32 1. FT CA_BIND 57 68 2. FT CA_BIND 94 105 3. FT CA_BIND 130 141 4. FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 116 116 N6,N6,N6-trimethyllysine (By similarity). SQ SEQUENCE 149 AA; 16820 MW; 722B188A90AD423A CRC64; MADQLTDDQI SEFKEAFSLF DKDGDGCITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL NLMARKMKDT DSEEELKEAF RVFDKDQNGF ISAAELRHVM TNLGEKLTDE EVDEMIKEAD VDGDGQINYE EFVKVMMAK // ID CALM6_ARATH Reviewed; 149 AA. AC Q03509; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-MAR-2010, entry version 88. DE RecName: Full=Calmodulin-6; DE Short=CaM-6; GN Name=CAM6; OrderedLocusNames=At5g21274; ORFNames=F13M11.?; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; malvids; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93283627; PubMed=8507825; DOI=10.1007/BF00014930; RA Gawienowski M.C., Szymanski D., Perera I.Y., Zielinski R.E.; RT "Calmodulin isoforms in Arabidopsis encoded by multiple divergent RT mRNAs."; RL Plant Mol. Biol. 22:215-225(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016721; PubMed=11130714; DOI=10.1038/35048507; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis RT thaliana."; RL Nature 408:823-826(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP GENE FAMILY, AND NOMENCLATURE. RX DOI=10.1046/j.1469-8137.2003.00845.x; RA McCormack E., Braam J.; RT "Calmodulins and related potential calcium sensors of Arabidopsis."; RL New Phytol. 159:585-598(2003). CC -!- FUNCTION: Calmodulin mediates the control of a large number of CC enzymes and other proteins by Ca(2+). Among the enzymes to be CC stimulated by the calmodulin-Ca(2+) complex are a number of CC protein kinases and phosphatases. CC -!- INTERACTION: CC O22179:-; NbExp=1; IntAct=EBI-1236097, EBI-1238013; CC P27450:-; NbExp=1; IntAct=EBI-1236097, EBI-1238108; CC Q29Q72:-; NbExp=1; IntAct=EBI-1236097, EBI-1238714; CC Q2V359:-; NbExp=2; IntAct=EBI-1236097, EBI-1235819; CC Q39130:-; NbExp=1; IntAct=EBI-1236097, EBI-1749651; CC Q3EAG3:-; NbExp=1; IntAct=EBI-1236097, EBI-1238312; CC Q3EBV7:-; NbExp=1; IntAct=EBI-1236097, EBI-1235683; CC Q4PSE3:-; NbExp=1; IntAct=EBI-1236097, EBI-1238507; CC Q7X9H6:-; NbExp=1; IntAct=EBI-1236097, EBI-1238497; CC Q7X9N2:-; NbExp=1; IntAct=EBI-1236097, EBI-622264; CC Q84JC2:-; NbExp=1; IntAct=EBI-1236097, EBI-1238377; CC Q8H1D6:-; NbExp=1; IntAct=EBI-1236097, EBI-1238166; CC Q8VZ70:-; NbExp=1; IntAct=EBI-1236097, EBI-1238078; CC Q93Z30:-; NbExp=1; IntAct=EBI-1236097, EBI-1237782; CC Q9FGX2:-; NbExp=1; IntAct=EBI-1236097, EBI-942623; CC Q9FGZ5:-; NbExp=1; IntAct=EBI-1236097, EBI-622281; CC Q9FIW6:-; NbExp=1; IntAct=EBI-1236097, EBI-1237967; CC Q9FL19:-; NbExp=1; IntAct=EBI-1236097, EBI-622440; CC Q9FLL0:-; NbExp=1; IntAct=EBI-1236097, EBI-1238516; CC Q9FUD3:-; NbExp=1; IntAct=EBI-1236097, EBI-942633; CC Q9LUI6:-; NbExp=1; IntAct=EBI-1236097, EBI-1238581; CC Q9LW66:-; NbExp=1; IntAct=EBI-1236097, EBI-1238066; CC Q9LX56:-; NbExp=1; IntAct=EBI-1236097, EBI-1235891; CC Q9SJX8:-; NbExp=1; IntAct=EBI-1236097, EBI-1238001; CC Q9SKN2:-; NbExp=1; IntAct=EBI-1236097, EBI-1237944; CC Q9SL70:-; NbExp=1; IntAct=EBI-1236097, EBI-1238421; CC Q9M7Q2:ABF4; NbExp=1; IntAct=EBI-1236097, EBI-1237867; CC Q9SZJ6:AGL21; NbExp=1; IntAct=EBI-1236097, EBI-621986; CC Q4PSU4:AGL61; NbExp=1; IntAct=EBI-1236097, EBI-1237976; CC Q9FJK3:AGL80; NbExp=1; IntAct=EBI-1236097, EBI-622424; CC Q70E96:ALDH3F1; NbExp=1; IntAct=EBI-1236097, EBI-1237774; CC O22042:ANP3; NbExp=1; IntAct=EBI-1236097, EBI-1239058; CC O49839:APK2A; NbExp=1; IntAct=EBI-1236097, EBI-1238631; CC Q39010:ASK6; NbExp=1; IntAct=EBI-1236097, EBI-1238323; CC Q56W43:At1g08320; NbExp=1; IntAct=EBI-1236097, EBI-1237844; CC O04567:At1g27190; NbExp=1; IntAct=EBI-1236097, EBI-1238687; CC Q9SGN7:At1g28390; NbExp=1; IntAct=EBI-1236097, EBI-1238190; CC Q9ZVM9:At1g54610; NbExp=1; IntAct=EBI-1236097, EBI-1235713; CC Q84WC8:At1g58110; NbExp=1; IntAct=EBI-1236097, EBI-1237819; CC Q9ZUI9:At1g60040; NbExp=1; IntAct=EBI-1236097, EBI-622185; CC Q9M9C3:At1g68380/T2E12_7; NbExp=1; IntAct=EBI-1236097, EBI-1238618; CC O80651:At1g77145; NbExp=1; IntAct=EBI-1236097, EBI-1238133; CC Q9SSC7:At1g80120; NbExp=1; IntAct=EBI-1236097, EBI-1238625; CC Q9M8T0:At3g02880; NbExp=1; IntAct=EBI-1236097, EBI-1238677; CC Q2VW98:At3g17600; NbExp=2; IntAct=EBI-1236097, EBI-1235997; CC Q9LJL9:At3g19100; NbExp=1; IntAct=EBI-1236097, EBI-1238393; CC O81292:AT4g02410; NbExp=1; IntAct=EBI-1236097, EBI-1237950; CC O22763:AT4g02640; NbExp=1; IntAct=EBI-1236097, EBI-969959; CC Q8GYP4:At4g18630/F28A21_40; NbExp=1; IntAct=EBI-1236097, EBI-1239007; CC Q9SZ03:AT4g34380; NbExp=1; IntAct=EBI-1236097, EBI-1238343; CC Q8LE56:At4g37240/C7A10_120; NbExp=1; IntAct=EBI-1236097, EBI-1237996; CC Q8GY88:At4g39540/F23K16_170; NbExp=1; IntAct=EBI-1236097, EBI-1238334; CC Q9FLV4:At5g24080; NbExp=1; IntAct=EBI-1236097, EBI-1238700; CC Q9FMC2:At5g38800; NbExp=1; IntAct=EBI-1236097, EBI-1237855; CC Q8GZ99:At5g49760/K2I5_13; NbExp=1; IntAct=EBI-1236097, EBI-1238218; CC Q8LPR4:At5g56890; NbExp=1; IntAct=EBI-1236097, EBI-1238087; CC P92525:AtMg00870; NbExp=1; IntAct=EBI-1236097, EBI-1238547; CC Q9M2K4:BZIP61; NbExp=1; IntAct=EBI-1236097, EBI-1237830; CC P59220:CAM7; NbExp=1; IntAct=EBI-1236097, EBI-1236031; CC Q8LG64:CDKB2-2; NbExp=2; IntAct=EBI-1236097, EBI-1235761; CC Q9LDI3:CIPK24; NbExp=1; IntAct=EBI-1236097, EBI-537551; CC O65554:CIPK6; NbExp=1; IntAct=EBI-1236097, EBI-537615; CC Q39050:CKI1; NbExp=1; IntAct=EBI-1236097, EBI-1237881; CC Q93Z27:CML45; NbExp=1; IntAct=EBI-1236097, EBI-1235938; CC Q9S744:CML9; NbExp=1; IntAct=EBI-1236097, EBI-1236048; CC Q42479:CPK3; NbExp=2; IntAct=EBI-1236097, EBI-1235782; CC Q9SSF8:CPK30; NbExp=1; IntAct=EBI-1236097, EBI-1235738; CC Q9SYS3:CRK40; NbExp=1; IntAct=EBI-1236097, EBI-1238119; CC O65469:CRK9; NbExp=1; IntAct=EBI-1236097, EBI-1238158; CC Q38867:CYP19-3; NbExp=1; IntAct=EBI-1236097, EBI-1235851; CC Q9LJY7:CYP705A20; NbExp=1; IntAct=EBI-1236097, EBI-1237907; CC Q9SLP1:CYP78A9; NbExp=1; IntAct=EBI-1236097, EBI-1238437; CC O23552:dl4570w; NbExp=1; IntAct=EBI-1236097, EBI-1235805; CC Q9SND6:F11C1_150; NbExp=2; IntAct=EBI-1236097, EBI-1235872; CC Q9LFU3:F14F8_210; NbExp=1; IntAct=EBI-1236097, EBI-1237805; CC Q9LYL6:F18O21_230; NbExp=1; IntAct=EBI-1236097, EBI-1238139; CC Q9ZPE4:FBW2; NbExp=1; IntAct=EBI-1236097, EBI-604740; CC Q8RWQ8:FBX14; NbExp=1; IntAct=EBI-1236097, EBI-1235922; CC P55737:HSP81-2; NbExp=2; IntAct=EBI-1236097, EBI-1235834; CC Q3ECN4:LRR-RLK; NbExp=1; IntAct=EBI-1236097, EBI-1238268; CC Q8VYG7:LRR-RLK; NbExp=1; IntAct=EBI-1236097, EBI-1238236; CC Q9LSI9:LRR-RLK; NbExp=1; IntAct=EBI-1236097, EBI-1238253; CC Q9M9C5:LRR-RLK; NbExp=1; IntAct=EBI-1236097, EBI-1238661; CC P43294:MHK; NbExp=1; IntAct=EBI-1236097, EBI-1238022; CC Q9C5C0:MPK18; NbExp=1; IntAct=EBI-1236097, EBI-1238534; CC Q9LHI7:NEK7; NbExp=1; IntAct=EBI-1236097, EBI-1238055; CC Q9T074:PCKA; NbExp=1; IntAct=EBI-1236097, EBI-1238593; CC Q8W490:PEPKR2; NbExp=1; IntAct=EBI-1236097, EBI-1238381; CC Q9FIK0:PFK2; NbExp=1; IntAct=EBI-1236097, EBI-1238609; CC Q94AA4:PFK3; NbExp=1; IntAct=EBI-1236097, EBI-1238600; CC P83755:psbA; NbExp=1; IntAct=EBI-1236097, EBI-1236013; CC Q9CAG5:PUB7; NbExp=1; IntAct=EBI-1236097, EBI-1239045; CC P93050:RKF3; NbExp=1; IntAct=EBI-1236097, EBI-1238281; CC Q9S7H5:SCL21; NbExp=1; IntAct=EBI-1236097, EBI-1238472; CC Q9FL03:SCL4; NbExp=1; IntAct=EBI-1236097, EBI-1238466; CC Q5XXJ3:SHP1; NbExp=1; IntAct=EBI-1236097, EBI-1237985; CC Q9LZP8:T12C14_120; NbExp=1; IntAct=EBI-1236097, EBI-942845; CC Q9LZV7:T20L15_160; NbExp=1; IntAct=EBI-1236097, EBI-1238200; CC Q9LQ65:T4M14.10; NbExp=1; IntAct=EBI-1236097, EBI-942986; CC Q8RYD9:TT16; NbExp=1; IntAct=EBI-1236097, EBI-621993; CC Q8GYF5:WAKL21; NbExp=1; IntAct=EBI-1236097, EBI-1238355; CC Q8GY11:WRKY43; NbExp=1; IntAct=EBI-1236097, EBI-1235953; CC Q9SUP6:WRKY53; NbExp=2; IntAct=EBI-1236097, EBI-1235980; CC -!- MISCELLANEOUS: This protein has four functional calcium-binding CC sites. CC -!- SIMILARITY: Belongs to the calmodulin family. CC -!- SIMILARITY: Contains 4 EF-hand domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z12024; CAA78059.1; -; mRNA. DR EMBL; AC140977; AAO73886.1; -; Genomic_DNA. DR EMBL; AY050350; AAK91367.1; -; mRNA. DR EMBL; AY094037; AAM16193.1; -; mRNA. DR IPI; IPI00520449; -. DR PIR; S35187; S35187. DR RefSeq; NP_850860.1; -. DR UniGene; At.21106; -. DR UniGene; Rra.1222; -. DR UniGene; Rsa.2523; -. DR SMR; Q03509; 1-148. DR IntAct; Q03509; 104. DR STRING; Q03509; -. DR PRIDE; Q03509; -. DR GeneID; 832245; -. DR GenomeReviews; BA000015_GR; AT5G21274. DR KEGG; ath:AT5G21274; -. DR NMPDR; fig|3702.1.peg.24337; -. DR TAIR; At5g21274; -. DR eggNOG; KOG0027; -. DR HOGENOM; HBG746798; -. DR InParanoid; Q03509; -. DR OMA; DEQIAEF; -. DR PhylomeDB; Q03509; -. DR Genevestigator; Q03509; -. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0019722; P:calcium-mediated signaling; TAS:TAIR. DR InterPro; IPR011992; EF-hand-like_dom. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR018249; EF_HAND_2. DR InterPro; IPR002048; EF_hand_Ca_bd. DR Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1. DR SMART; SM00054; EFh; 4. DR PROSITE; PS00018; EF_HAND_1; 4. DR PROSITE; PS50222; EF_HAND_2; 4. PE 1: Evidence at protein level; KW Acetylation; Calcium; Complete proteome; Methylation; Repeat. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 149 Calmodulin-6. FT /FTId=PRO_0000198282. FT DOMAIN 8 43 EF-hand 1. FT DOMAIN 44 79 EF-hand 2. FT DOMAIN 81 116 EF-hand 3. FT DOMAIN 117 149 EF-hand 4. FT CA_BIND 21 32 1 (By similarity). FT CA_BIND 57 68 2 (By similarity). FT CA_BIND 94 105 3 (By similarity). FT CA_BIND 130 141 4 (By similarity). FT MOD_RES 2 2 N-acetylalanine (By similarity). FT MOD_RES 116 116 N6,N6,N6-trimethyllysine (By similarity). SQ SEQUENCE 149 AA; 16834 MW; AA6E088A90AD508A CRC64; MADQLTDDQI SEFKEAFSLF DKDGDGCITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL NLMARKMKDT DSEEELKEAF RVFDKDQNGF ISAAELRHVM TNLGEKLSDE EVDEMIREAD VDGDGQINYE EFVKVMMAK //