| blob | 28f6237b0caf4654187c1fca003215a7bedae198 |
1 ID CALM_HUMAN STANDARD; PRT; 148 AA.
2 AC P62158; P02593; P70667; P99014; Q61379; Q61380;
3 DT 21-JUL-1986 (Rel. 01, Created)
4 DT 21-JUL-1986 (Rel. 01, Last sequence update)
5 DT 01-OCT-2004 (Rel. 45, Last annotation update)
6 DE Calmodulin (CaM).
7 GN Name=CALM1; Synonyms=CAM1, CALM, CAM;
8 GN and
9 GN Name=CALM2; Synonyms=CAM2, CAMB;
10 GN and
11 GN Name=CALM3; Synonyms=CAM3, CAMC;
12 OS Homo sapiens (Human).
13 OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
14 OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
15 OX NCBI_TaxID=9606;
16 RN [1]
17 RP SEQUENCE, ACETYLATION SITE ALA-1, AND METHYLATION SITE LYS-115.
18 RC TISSUE=Brain;
19 RX MEDLINE=82231946; PubMed=7093203;
20 RA Sasagawa T., Ericsson L.H., Walsh K.A., Schreiber W.E., Fischer E.H.,
21 RA Titani K.;
22 RT "Complete amino acid sequence of human brain calmodulin.";
23 RL Biochemistry 21:2565-2569(1982).
24 RN [2]
25 RP SEQUENCE FROM N.A.
26 RX MEDLINE=89034207; PubMed=3182832;
27 RA Fischer R., Koller M., Flura M., Mathews S., Strehler-Page M.A.,
28 RA Krebs J., Penniston J.T., Carafoli E., Strehler E.E.;
29 RT "Multiple divergent mRNAs code for a single human calmodulin.";
30 RL J. Biol. Chem. 263:17055-17062(1988).
31 RN [3]
32 RP SEQUENCE FROM N.A.
33 RX MEDLINE=88059053; PubMed=2445749;
34 RA Sengupta B., Friedberg F., Detera-Wadleigh S.D.;
35 RT "Molecular analysis of human and rat calmodulin complementary DNA
36 RT clones. Evidence for additional active genes in these species.";
37 RL J. Biol. Chem. 262:16663-16670(1987).
38 RN [4]
39 RP SEQUENCE FROM N.A.
40 RX MEDLINE=85022688; PubMed=6385987;
41 RA Wawrzynczak E.J., Perham R.N.;
42 RT "Isolation and nucleotide sequence of a cDNA encoding human
43 RT calmodulin.";
44 RL Biochem. Int. 9:177-185(1984).
45 RN [5]
46 RP SEQUENCE FROM N.A. (CALM1).
47 RC TISSUE=Blood;
48 RX MEDLINE=95010144; PubMed=7925473;
49 RA Rhyner J.A., Ottiger M., Wicki R., Greenwood T.M., Strehler E.E.;
50 RT "Structure of the human CALM1 calmodulin gene and identification of
51 RT two CALM1-related pseudogenes CALM1P1 and CALM1P2.";
52 RL Eur. J. Biochem. 225:71-82(1994).
53 RN [6]
54 RP SEQUENCE FROM N.A.
55 RC TISSUE=Lymphoma;
56 RA Kato S.;
57 RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
58 RN [7]
59 RP SEQUENCE FROM N.A. (CALM2).
60 RX MEDLINE=98346173; PubMed=9681195;
61 RA Toutenhoofd S.L., Foletti D., Wicki R., Rhyner J.A., Garcia F.,
62 RA Tolon R., Strehler E.E.;
63 RT "Characterization of the human CALM2 calmodulin gene and comparison of
64 RT the transcriptional activity of CALM1, CALM2 and CALM3.";
65 RL Cell Calcium 23:323-338(1998).
66 RN [8]
67 RP SEQUENCE FROM N.A.
68 RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
69 RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
70 RA Phelan M., Farmer A.;
71 RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
72 RT vector.";
73 RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
74 RN [9]
75 RP SEQUENCE FROM N.A. (CALM1).
76 RX MEDLINE=22459283; PubMed=12508121; DOI=10.1038/nature01348;
77 RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
78 RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
79 RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
80 RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
81 RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
82 RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
83 RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
84 RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
85 RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
86 RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
87 RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
88 RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
89 RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
90 RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
91 RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
92 RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
93 RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
94 RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
95 RA Quetier F., Waterston R., Hood L., Weissenbach J.;
96 RT "The DNA sequence and analysis of human chromosome 14.";
97 RL Nature 421:601-607(2003).
98 RN [10]
99 RP SEQUENCE FROM N.A.
100 RC TISSUE=Brain, Lung, Lymph, Placenta, and Urinary bladder;
101 RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
102 RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
103 RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
104 RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
105 RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
106 RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
107 RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
108 RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
109 RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
110 RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
111 RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
112 RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
113 RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
114 RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
115 RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
116 RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
117 RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
118 RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
119 RT "Generation and initial analysis of more than 15,000 full-length human
120 RT and mouse cDNA sequences.";
121 RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
122 RN [11]
123 RP STRUCTURE BY NMR OF 94-103.
124 RX PubMed=9927666;
125 RA Siedlecka M., Goch G., Ejchart A., Sticht H., Bierzyski A.;
126 RT "Alpha-helix nucleation by a calcium-binding peptide loop.";
127 RL Proc. Natl. Acad. Sci. U.S.A. 96:903-908(1999).
128 RN [12]
129 RP STRUCTURE BY NMR OF 1-76 AND 82-148.
130 RX PubMed=11685248; DOI=10.1038/nsb1101-990;
131 RA Chou J.J., Li S., Klee C.B., Bax A.;
132 RT "Solution structure of Ca(2+)-calmodulin reveals flexible hand-like
133 RT properties of its domains.";
134 RL Nat. Struct. Biol. 8:990-997(2001).
135 RN [13]
136 RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
137 RX PubMed=1474585;
138 RA Chattopadhyaya R., Meador W.E., Means A.R., Quiocho F.A.;
139 RT "Calmodulin structure refined at 1.7 A resolution.";
140 RL J. Mol. Biol. 228:1177-1192(1992).
141 RN [14]
142 RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
143 RX PubMed=7803388;
144 RA Cook W.J., Walter L.J., Walter M.R.;
145 RT "Drug binding by calmodulin: crystal structure of a calmodulin-
146 RT trifluoperazine complex.";
147 RL Biochemistry 33:15259-15265(1994).
148 RN [15]
149 RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 5-148.
150 RX MEDLINE=21666515; PubMed=11807546; DOI=10.1038/415396a;
151 RA Drum C.L., Yan S.-Z., Bard J., Shen Y.Q., Lu D., Soelaiman S.,
152 RA Grabarek Z., Bohm A., Tang W.-J.;
153 RT "Structural basis for the activation of anthrax adenylyl cyclase
154 RT exotoxin by calmodulin.";
155 RL Nature 415:396-402(2002).
156 RN [16]
157 RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 1-148.
158 RX PubMed=12485993;
159 RA Shen Y., Lee Y.-S., Soelaiman S., Bergson P., Lu D., Chen A.,
160 RA Beckingham K., Grabarek Z., Mrksich M., Tang W.-J.;
161 RT "Physiological calcium concentrations regulate calmodulin binding and
162 RT catalysis of adenylyl cyclase exotoxins.";
163 RL EMBO J. 21:6721-6732(2002).
164 RN [17]
165 RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
166 RX PubMed=12577052; DOI=10.1038/nsb900;
167 RA Yamauchi E., Nakatsu T., Matsubara M., Kato H., Taniguchi H.;
168 RT "Crystal structure of a MARCKS peptide containing the calmodulin-
169 RT binding domain in complex with Ca2+-calmodulin.";
170 RL Nat. Struct. Biol. 10:226-231(2003).
171 CC -!- FUNCTION: Calmodulin mediates the control of a large number of
172 CC enzymes by Ca(2+). Among the enzymes to be stimulated by the
173 CC calmodulin-Ca(2+) complex are a number of protein kinases and
174 CC phosphatases.
175 CC -!- PTM: Ubiquitylation results in a strongly decreased activity (By
176 CC similarity).
177 CC -!- PTM: Phosphorylation results in a decreased activity (By
178 CC similarity).
179 CC -!- MISCELLANEOUS: This protein has four functional calcium-binding
180 CC sites.
181 CC -!- SIMILARITY: Contains 4 EF-hand calcium-binding domains.
182 CC --------------------------------------------------------------------------
183 CC This SWISS-PROT entry is copyright. It is produced through a collaboration
184 CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
185 CC the European Bioinformatics Institute. There are no restrictions on its
186 CC use by non-profit institutions as long as its content is in no way
187 CC modified and this statement is not removed. Usage by and for commercial
188 CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
189 CC or send an email to license@isb-sib.ch).
190 CC --------------------------------------------------------------------------
191 DR EMBL; J04046; AAA51918.1; -.
192 DR EMBL; M19311; AAA35641.1; -.
193 DR EMBL; M27319; AAA35635.1; -.
194 DR EMBL; U12022; AAB60644.1; -.
195 DR EMBL; U11886; AAB60644.1; JOINED.
196 DR EMBL; D45887; BAA08302.1; -.
197 DR EMBL; U94728; AAC83174.1; -.
198 DR EMBL; U94725; AAC83174.1; JOINED.
199 DR EMBL; U94726; AAC83174.1; JOINED.
200 DR EMBL; BT006818; AAP35464.1; -.
201 DR EMBL; BT006855; AAP35501.1; -.
202 DR EMBL; BT009916; AAP88918.1; -.
203 DR EMBL; AC006536; AAD45181.1; -.
204 DR EMBL; BC000454; AAH00454.1; -.
205 DR EMBL; BC003354; AAH03354.1; -.
206 DR EMBL; BC005137; AAH05137.1; -.
207 DR EMBL; BC006464; AAH06464.1; -.
208 DR EMBL; BC008597; AAH08597.1; -.
209 DR EMBL; BC011834; AAH11834.1; -.
210 DR EMBL; BC017385; AAH17385.1; -.
211 DR EMBL; BC018677; AAH18677.1; -.
212 DR EMBL; BC026065; AAH26065.1; -.
213 DR EMBL; BC047523; AAH47523.1; -.
214 DR PIR; S48728; MCHU.
215 DR PDB; 1AJI; 17-SEP-97.
216 DR PDB; 1CLL; 31-OCT-93.
217 DR PDB; 1CTR; 20-DEC-94.
218 DR PDB; 1IWQ; 11-MAR-03.
219 DR PDB; 1J7O; 07-NOV-01.
220 DR PDB; 1J7P; 07-NOV-01.
221 DR PDB; 1K90; 23-JAN-02.
222 DR PDB; 1K93; 23-JAN-02.
223 DR PDB; 1LVC; 04-DEC-02.
224 DR PDB; 1NKF; 23-MAR-99.
225 DR SWISS-2DPAGE; P62158; HUMAN.
226 DR Aarhus/Ghent-2DPAGE; 9048; IEF.
227 DR OGP; P02593; -.
228 DR Genew; HGNC:1442; CALM1.
229 DR Genew; HGNC:1445; CALM2.
230 DR Genew; HGNC:1449; CALM3.
231 DR Reactome; P62158; -.
232 DR MIM; 114180; -.
233 DR MIM; 114182; -.
234 DR MIM; 114183; -.
235 DR GO; GO:0005737; C:cytoplasm; TAS.
236 DR GO; GO:0005886; C:plasma membrane; TAS.
237 DR GO; GO:0005509; F:calcium ion binding; TAS.
238 DR GO; GO:0005515; F:protein binding; NAS.
239 DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS.
240 DR InterPro; IPR002048; EF-hand.
241 DR Pfam; PF00036; efhand; 4.
242 DR PRINTS; PR00450; RECOVERIN.
243 DR ProDom; PD000012; EF-hand; 2.
244 DR PROSITE; PS00018; EF_HAND; 4.
245 KW 3D-structure; Acetylation; Calcium-binding; Direct protein sequencing;
246 KW Methylation; Phosphorylation; Repeat; Ubl conjugation.
247 FT INIT_MET 0 0
248 FT MOD_RES 1 1 N-acetylalanine.
249 FT CA_BIND 20 31 EF-hand 1.
250 FT CA_BIND 56 67 EF-hand 2.
251 FT CA_BIND 93 104 EF-hand 3.
252 FT CA_BIND 129 140 EF-hand 4.
253 FT BINDING 21 21 Ubiquitin (multi-) (By similarity).
254 FT MOD_RES 44 44 Phosphothreonine (by CaMK4) (By
255 FT similarity).
256 FT MOD_RES 115 115 N6,N6,N6-trimethyllysine.
257 FT HELIX 6 18
258 FT TURN 21 22
259 FT TURN 29 30
260 FT HELIX 33 36
261 FT TURN 37 40
262 FT TURN 45 46
263 FT HELIX 47 54
264 FT TURN 55 55
265 FT HELIX 66 72
266 FT TURN 73 74
267 FT HELIX 75 77
268 FT TURN 78 78
269 FT TURN 81 81
270 FT HELIX 82 92
271 FT TURN 94 95
272 FT STRAND 99 100
273 FT HELIX 102 111
274 FT TURN 112 113
275 FT HELIX 118 128
276 FT STRAND 136 137
277 FT HELIX 138 146
278 SQ SEQUENCE 148 AA; 16706 MW; 464B8A287475A1CA CRC64;
279 ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN
280 GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE
281 VDEMIREADI DGDGQVNYEE FVQMMTAK
282 //