ID CALM_HUMAN STANDARD; PRT; 148 AA.
AC P62158; P02593; P70667; P99014; Q61379; Q61380;
DT 21-JUL-1986 (Rel. 01, Created)
DT 21-JUL-1986 (Rel. 01, Last sequence update)
DT 01-OCT-2004 (Rel. 45, Last annotation update)
DE Calmodulin (CaM).
GN Name=CALM1; Synonyms=CAM1, CALM, CAM;
GN and
GN Name=CALM2; Synonyms=CAM2, CAMB;
GN and
GN Name=CALM3; Synonyms=CAM3, CAMC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP SEQUENCE, ACETYLATION SITE ALA-1, AND METHYLATION SITE LYS-115.
RC TISSUE=Brain;
RX MEDLINE=82231946; PubMed=7093203;
RA Sasagawa T., Ericsson L.H., Walsh K.A., Schreiber W.E., Fischer E.H.,
RA Titani K.;
RT "Complete amino acid sequence of human brain calmodulin.";
RL Biochemistry 21:2565-2569(1982).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE=89034207; PubMed=3182832;
RA Fischer R., Koller M., Flura M., Mathews S., Strehler-Page M.A.,
RA Krebs J., Penniston J.T., Carafoli E., Strehler E.E.;
RT "Multiple divergent mRNAs code for a single human calmodulin.";
RL J. Biol. Chem. 263:17055-17062(1988).
RN [3]
RP SEQUENCE FROM N.A.
RX MEDLINE=88059053; PubMed=2445749;
RA Sengupta B., Friedberg F., Detera-Wadleigh S.D.;
RT "Molecular analysis of human and rat calmodulin complementary DNA
RT clones. Evidence for additional active genes in these species.";
RL J. Biol. Chem. 262:16663-16670(1987).
RN [4]
RP SEQUENCE FROM N.A.
RX MEDLINE=85022688; PubMed=6385987;
RA Wawrzynczak E.J., Perham R.N.;
RT "Isolation and nucleotide sequence of a cDNA encoding human
RT calmodulin.";
RL Biochem. Int. 9:177-185(1984).
RN [5]
RP SEQUENCE FROM N.A. (CALM1).
RC TISSUE=Blood;
RX MEDLINE=95010144; PubMed=7925473;
RA Rhyner J.A., Ottiger M., Wicki R., Greenwood T.M., Strehler E.E.;
RT "Structure of the human CALM1 calmodulin gene and identification of
RT two CALM1-related pseudogenes CALM1P1 and CALM1P2.";
RL Eur. J. Biochem. 225:71-82(1994).
RN [6]
RP SEQUENCE FROM N.A.
RC TISSUE=Lymphoma;
RA Kato S.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SEQUENCE FROM N.A. (CALM2).
RX MEDLINE=98346173; PubMed=9681195;
RA Toutenhoofd S.L., Foletti D., Wicki R., Rhyner J.A., Garcia F.,
RA Tolon R., Strehler E.E.;
RT "Characterization of the human CALM2 calmodulin gene and comparison of
RT the transcriptional activity of CALM1, CALM2 and CALM3.";
RL Cell Calcium 23:323-338(1998).
RN [8]
RP SEQUENCE FROM N.A.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP SEQUENCE FROM N.A. (CALM1).
RX MEDLINE=22459283; PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [10]
RP SEQUENCE FROM N.A.
RC TISSUE=Brain, Lung, Lymph, Placenta, and Urinary bladder;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [11]
RP STRUCTURE BY NMR OF 94-103.
RX PubMed=9927666;
RA Siedlecka M., Goch G., Ejchart A., Sticht H., Bierzyski A.;
RT "Alpha-helix nucleation by a calcium-binding peptide loop.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:903-908(1999).
RN [12]
RP STRUCTURE BY NMR OF 1-76 AND 82-148.
RX PubMed=11685248; DOI=10.1038/nsb1101-990;
RA Chou J.J., Li S., Klee C.B., Bax A.;
RT "Solution structure of Ca(2+)-calmodulin reveals flexible hand-like
RT properties of its domains.";
RL Nat. Struct. Biol. 8:990-997(2001).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=1474585;
RA Chattopadhyaya R., Meador W.E., Means A.R., Quiocho F.A.;
RT "Calmodulin structure refined at 1.7 A resolution.";
RL J. Mol. Biol. 228:1177-1192(1992).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RX PubMed=7803388;
RA Cook W.J., Walter L.J., Walter M.R.;
RT "Drug binding by calmodulin: crystal structure of a calmodulin-
RT trifluoperazine complex.";
RL Biochemistry 33:15259-15265(1994).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 5-148.
RX MEDLINE=21666515; PubMed=11807546; DOI=10.1038/415396a;
RA Drum C.L., Yan S.-Z., Bard J., Shen Y.Q., Lu D., Soelaiman S.,
RA Grabarek Z., Bohm A., Tang W.-J.;
RT "Structural basis for the activation of anthrax adenylyl cyclase
RT exotoxin by calmodulin.";
RL Nature 415:396-402(2002).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1-148.
RX PubMed=12485993;
RA Shen Y., Lee Y.-S., Soelaiman S., Bergson P., Lu D., Chen A.,
RA Beckingham K., Grabarek Z., Mrksich M., Tang W.-J.;
RT "Physiological calcium concentrations regulate calmodulin binding and
RT catalysis of adenylyl cyclase exotoxins.";
RL EMBO J. 21:6721-6732(2002).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=12577052; DOI=10.1038/nsb900;
RA Yamauchi E., Nakatsu T., Matsubara M., Kato H., Taniguchi H.;
RT "Crystal structure of a MARCKS peptide containing the calmodulin-
RT binding domain in complex with Ca2+-calmodulin.";
RL Nat. Struct. Biol. 10:226-231(2003).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of
CC enzymes by Ca(2+). Among the enzymes to be stimulated by the
CC calmodulin-Ca(2+) complex are a number of protein kinases and
CC phosphatases.
CC -!- PTM: Ubiquitylation results in a strongly decreased activity (By
CC similarity).
CC -!- PTM: Phosphorylation results in a decreased activity (By
CC similarity).
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding
CC sites.
CC -!- SIMILARITY: Contains 4 EF-hand calcium-binding domains.
CC --------------------------------------------------------------------------
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CC the European Bioinformatics Institute. There are no restrictions on its
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DR EMBL; J04046; AAA51918.1; -.
DR EMBL; M19311; AAA35641.1; -.
DR EMBL; M27319; AAA35635.1; -.
DR EMBL; U12022; AAB60644.1; -.
DR EMBL; U11886; AAB60644.1; JOINED.
DR EMBL; D45887; BAA08302.1; -.
DR EMBL; U94728; AAC83174.1; -.
DR EMBL; U94725; AAC83174.1; JOINED.
DR EMBL; U94726; AAC83174.1; JOINED.
DR EMBL; BT006818; AAP35464.1; -.
DR EMBL; BT006855; AAP35501.1; -.
DR EMBL; BT009916; AAP88918.1; -.
DR EMBL; AC006536; AAD45181.1; -.
DR EMBL; BC000454; AAH00454.1; -.
DR EMBL; BC003354; AAH03354.1; -.
DR EMBL; BC005137; AAH05137.1; -.
DR EMBL; BC006464; AAH06464.1; -.
DR EMBL; BC008597; AAH08597.1; -.
DR EMBL; BC011834; AAH11834.1; -.
DR EMBL; BC017385; AAH17385.1; -.
DR EMBL; BC018677; AAH18677.1; -.
DR EMBL; BC026065; AAH26065.1; -.
DR EMBL; BC047523; AAH47523.1; -.
DR PIR; S48728; MCHU.
DR PDB; 1AJI; 17-SEP-97.
DR PDB; 1CLL; 31-OCT-93.
DR PDB; 1CTR; 20-DEC-94.
DR PDB; 1IWQ; 11-MAR-03.
DR PDB; 1J7O; 07-NOV-01.
DR PDB; 1J7P; 07-NOV-01.
DR PDB; 1K90; 23-JAN-02.
DR PDB; 1K93; 23-JAN-02.
DR PDB; 1LVC; 04-DEC-02.
DR PDB; 1NKF; 23-MAR-99.
DR SWISS-2DPAGE; P62158; HUMAN.
DR Aarhus/Ghent-2DPAGE; 9048; IEF.
DR OGP; P02593; -.
DR Genew; HGNC:1442; CALM1.
DR Genew; HGNC:1445; CALM2.
DR Genew; HGNC:1449; CALM3.
DR Reactome; P62158; -.
DR MIM; 114180; -.
DR MIM; 114182; -.
DR MIM; 114183; -.
DR GO; GO:0005737; C:cytoplasm; TAS.
DR GO; GO:0005886; C:plasma membrane; TAS.
DR GO; GO:0005509; F:calcium ion binding; TAS.
DR GO; GO:0005515; F:protein binding; NAS.
DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS.
DR InterPro; IPR002048; EF-hand.
DR Pfam; PF00036; efhand; 4.
DR PRINTS; PR00450; RECOVERIN.
DR ProDom; PD000012; EF-hand; 2.
DR PROSITE; PS00018; EF_HAND; 4.
KW 3D-structure; Acetylation; Calcium-binding; Direct protein sequencing;
KW Methylation; Phosphorylation; Repeat; Ubl conjugation.
FT INIT_MET 0 0
FT MOD_RES 1 1 N-acetylalanine.
FT CA_BIND 20 31 EF-hand 1.
FT CA_BIND 56 67 EF-hand 2.
FT CA_BIND 93 104 EF-hand 3.
FT CA_BIND 129 140 EF-hand 4.
FT BINDING 21 21 Ubiquitin (multi-) (By similarity).
FT MOD_RES 44 44 Phosphothreonine (by CaMK4) (By
FT similarity).
FT MOD_RES 115 115 N6,N6,N6-trimethyllysine.
FT HELIX 6 18
FT TURN 21 22
FT TURN 29 30
FT HELIX 33 36
FT TURN 37 40
FT TURN 45 46
FT HELIX 47 54
FT TURN 55 55
FT HELIX 66 72
FT TURN 73 74
FT HELIX 75 77
FT TURN 78 78
FT TURN 81 81
FT HELIX 82 92
FT TURN 94 95
FT STRAND 99 100
FT HELIX 102 111
FT TURN 112 113
FT HELIX 118 128
FT STRAND 136 137
FT HELIX 138 146
SQ SEQUENCE 148 AA; 16706 MW; 464B8A287475A1CA CRC64;
ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN
GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE
VDEMIREADI DGDGQVNYEE FVQMMTAK
//