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Entry: Q39890_SOYBN
LinkDB: Q39890_SOYBN
Original site: Q39890_SOYBN 
ID   Q39890_SOYBN            Unreviewed;       150 AA.
AC   Q39890;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   SubName: Full=Calmodulin {ECO:0000313|EMBL:AAA34015.1};
GN   Name=SCaM-4 {ECO:0000313|EMBL:AAA34015.1};
GN   Synonyms=547787 {ECO:0000313|EnsemblPlants:KRH34350};
GN   ORFNames=GLYMA_10G178400 {ECO:0000313|EMBL:KRH34350.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:AAA34015.1};
RN   [1] {ECO:0000313|EMBL:AAA34015.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Hypocotyl {ECO:0000313|EMBL:AAA34015.1};
RA   Lee S.H., Kim J.C., Choi Y.J., Bahk J.D., Hong J.C., Cho M.J.;
RT   "Isolation and characterization of a soybean calmodulin multigene family.";
RL   Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:2ROA, ECO:0007829|PDB:2ROB}
RP   STRUCTURE BY NMR OF 2-80 IN COMPLEX WITH CALCIUM.
RX   PubMed=18347016; DOI=10.1074/jbc.M801398200;
RA   Ishida H., Huang H., Yamniuk A.P., Takaya Y., Vogel H.J.;
RT   "The solution structures of two soybean calmodulin isoforms provide a
RT   structural basis for their selective target activation properties.";
RL   J. Biol. Chem. 283:14619-14628(2008).
RN   [3] {ECO:0007829|PDB:2KN2}
RP   STRUCTURE BY NMR OF 79-150 IN COMPLEX WITH CALCIUM.
RX   PubMed=19667066; DOI=10.1074/jbc.M109.025080;
RA   Ishida H., Rainaldi M., Vogel H.J.;
RT   "Structural studies of soybean calmodulin isoform 4 bound to the
RT   calmodulin-binding domain of tobacco mitogen-activated protein kinase
RT   phosphatase-1 provide insights into a sequential target binding mode.";
RL   J. Biol. Chem. 284:28292-28305(2009).
RN   [4] {ECO:0000313|EMBL:ACU15622.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA   Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D.,
RA   Vonstein V.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0007829|PDB:2L1W}
RP   STRUCTURE BY NMR OF 2-150.
RX   PubMed=20880850; DOI=.1074/jbc.M110.131201;
RA   Ishida H., Vogel H.J.;
RT   "The solution structure of a plant calmodulin and the CaM-binding domain of
RT   the vacuolar calcium-ATPase BCA1 reveals a new binding and activation
RT   mechanism.";
RL   J. Biol. Chem. 285:38502-38510(2010).
RN   [6] {ECO:0000313|EMBL:KRH34350.1, ECO:0000313|EnsemblPlants:KRH34350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH34350};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH34350.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [7] {ECO:0007829|PDB:2KSZ}
RP   STRUCTURE BY NMR OF 2-77 IN COMPLEX WITH MAGNESIUM.
RX   PubMed=20054830; DOI=10.1002/pro.325;
RA   Huang H., Ishida H., Vogel H.J.;
RT   "The solution structure of the Mg2+ form of soybean calmodulin isoform 4
RT   reveals unique features of plant calmodulins in resting cells.";
RL   Protein Sci. 19:475-485(2010).
RN   [8] {ECO:0000313|EnsemblPlants:KRH34350}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH34350};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [9] {ECO:0000313|EMBL:KRH34350.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH34350.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; L01433; AAA34015.1; -; mRNA.
DR   EMBL; BT091456; ACU15622.1; -; mRNA.
DR   EMBL; CM000843; KRH34350.1; -; Genomic_DNA.
DR   PIR; T08585; T08585.
DR   RefSeq; NP_001237902.1; NM_001250973.1.
DR   PDB; 2KN2; NMR; -; A=79-150.
DR   PDB; 2KSZ; NMR; -; A=2-77.
DR   PDB; 2L1W; NMR; -; A=2-150.
DR   PDB; 2ROA; NMR; -; A=2-80.
DR   PDB; 2ROB; NMR; -; A=81-150.
DR   PDBsum; 2KN2; -.
DR   PDBsum; 2KSZ; -.
DR   PDBsum; 2L1W; -.
DR   PDBsum; 2ROA; -.
DR   PDBsum; 2ROB; -.
DR   AlphaFoldDB; Q39890; -.
DR   SMR; Q39890; -.
DR   STRING; 3847.Q39890; -.
DR   PaxDb; 3847-GLYMA10G32190-1; -.
DR   EnsemblPlants; KRH34350; KRH34350; GLYMA_10G178400.
DR   GeneID; 547787; -.
DR   Gramene; KRH34350; KRH34350; GLYMA_10G178400.
DR   KEGG; gmx:547787; -.
DR   eggNOG; KOG0027; Eukaryota.
DR   HOGENOM; CLU_061288_2_0_1; -.
DR   InParanoid; Q39890; -.
DR   OMA; MGETKQQ; -.
DR   OrthoDB; 351899at2759; -.
DR   EvolutionaryTrace; Q39890; -.
DR   Proteomes; UP000008827; Chromosome 10.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 3.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR23050; CALCIUM BINDING PROTEIN; 1.
DR   PANTHER; PTHR23050:SF453; CALMODULIN-LIKE PROTEIN 8; 1.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2KN2, ECO:0007829|PDB:2KSZ};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          8..43
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          44..79
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          81..116
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          117..150
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   150 AA;  17018 MW;  E074D5E60F89893C CRC64;
     MADILSEEQI VDFKEAFGLF DKDGDGCITV EELATVIRSL DQNPTEEELQ DMISEVDADG
     NGTIEFDEFL SLMAKKVKDT DAEEELKEAF KVFDKDQNGY ISASELRHVM INLGEKLTDE
     EVEQMIKEAD LDGDGQVNYE EFVKMMMTVR
//
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