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[bioperl-live.git] / t / data / sequencefamily.dat
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1 ID MA32_HUMAN STANDARD; PRT; 282 AA.
2 AC Q07021;
3 DT 01-FEB-1995 (Rel. 31, Created)
4 DT 01-FEB-1995 (Rel. 31, Last sequence update)
5 DT 01-OCT-2000 (Rel. 40, Last annotation update)
6 DE COMPLEMENT COMPONENT 1, Q SUBCOMPONENT BINDING PROTEIN, MITOCHONDRIAL
7 DE PRECURSOR (GLYCOPROTEIN GC1QBP) (GC1Q-R PROTEIN) (HYALURONAN-BINDING
8 DE PROTEIN 1) (PRE-MRNA SPLICING FACTOR SF2, P32 SUBUNIT) (P33).
9 GN GC1QBP OR HABP1 OR SF2P32 OR C1QBP.
10 OS Homo sapiens (Human).
11 OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
12 OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
13 OX NCBI_TaxID=9606;
14 RN [1]
15 RP SEQUENCE FROM N.A., AND SEQUENCE OF 74; 76-93 AND 208-216.
16 RC TISSUE=FIBROBLAST;
17 RX MEDLINE=94085792; PubMed=8262387;
18 RA Honore B., Madsen P., Rasmussen H.H., Vandekerckhove J., Celis J.E.,
19 RA Leffers H.;
20 RT "Cloning and expression of a cDNA covering the complete coding region
21 RT of the P32 subunit of human pre-mRNA splicing factor SF2.";
22 RL Gene 134:283-287(1993).
23 RN [2]
24 RP SEQUENCE OF 5-282 FROM N.A., AND SEQUENCE OF 74-114.
25 RX MEDLINE=91309150; PubMed=1830244;
26 RA Krainer A.R., Mayeda A., Kozak D., Binns G.;
27 RT "Functional expression of cloned human splicing factor SF2: homology
28 RT to RNA-binding proteins, U1 70K, and Drosophila splicing regulators.";
29 RL Cell 66:383-394(1991).
30 RN [3]
31 RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE.
32 RX MEDLINE=94253723; PubMed=8195709;
33 RA Ghebrehiwet B., Lim B.L., Peerschke E.I., Willis A.C., Reid K.B.;
34 RT "Isolation, cDNA cloning, and overexpression of a 33-kD cell surface
35 RT glycoprotein that binds to the globular 'heads' of C1q.";
36 RL J. Exp. Med. 179:1809-1821(1994).
37 RN [4]
38 RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
39 RX MEDLINE=99199225; PubMed=10097078;
40 RA Jiang J., Zhang Y., Krainer A.R., Xu R.-M.;
41 RT "Crystal structure of human p32, a doughnut-shaped acidic
42 RT mitochondrial matrix protein.";
43 RL Proc. Natl. Acad. Sci. U.S.A. 96:3572-3577(1999).
44 CC -!- FUNCTION: NOT KNOWN. BINDS TO THE GLOBULAR "HEADS" OF C1Q THUS
45 CC INHIBITING C1 ACTIVATION.
46 CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
47 CC -!- SIMILARITY: BELONGS TO THE MAM33 FAMILY.
48 CC -!- CAUTION: WAS ORIGINALLY (REF.1 AND REF.2) THOUGHT TO BE A PRE-MRNA
49 CC SPLICING FACTOR THAT PLAYS A ROLE IN PREVENTING EXON SKIPPING,
50 CC ENSURING THE ACCURACY OF SPLICING AND REGULATING ALTERNATIVE
51 CC SPLICING.
52 CC --------------------------------------------------------------------------
53 CC This SWISS-PROT entry is copyright. It is produced through a collaboration
54 CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
55 CC the European Bioinformatics Institute. There are no restrictions on its
56 CC use by non-profit institutions as long as its content is in no way
57 CC modified and this statement is not removed. Usage by and for commercial
58 CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
59 CC or send an email to license@isb-sib.ch).
60 CC --------------------------------------------------------------------------
61 DR EMBL; L04636; AAA16315.1; -.
62 DR EMBL; M69039; AAA73055.1; -.
63 DR EMBL; X75913; CAA53512.1; -.
64 DR PIR; JT0762; JT0762.
65 DR PIR; S44104; S44104.
66 DR PDB; 1P32; 06-APR-99.
67 DR MIM; 601269; -.
68 KW Mitochondrion; Transit peptide; 3D-structure.
69 FT TRANSIT 1 73 MITOCHONDRION.
70 FT CHAIN 74 282 COMPLEMENT COMPONENT 1, Q SUBCOMPONENT
71 FT BINDING PROTEIN.
72 SQ SEQUENCE 282 AA; 31362 MW; 2F747FA73BB1314B CRC64;
73 MLPLLRCVPR VLGSSVAGLR AAAPASPFRQ LLQPAPRLCT RPFGLLSVRA GSERRPGLLR
74 PRGPCACGCG CGSLHTDGDK AFVDFLSDEI KEERKIQKHK TLPKMSGGWE LELNGTEAKL
75 VRKVAGEKIT VTFNINNSIP PTFDGEEEPS QGQKVEEQEP ELTSTPNFVV EVIKNDDGKK
76 ALVLDCHYPE DEVGQEDEAE SDIFSIREVS FQSTGESEWK DTNYTLNTDS LDWALYDHLM
77 DFLADRGVDN TFADELVELS TALEHQEYIT FLEDLKSFVK SQ
78 //
79 ID ACON_CAEEL STANDARD; PRT; 788 AA.
80 AC P34455;
81 DT 01-FEB-1994 (Rel. 28, Created)
82 DT 01-FEB-1994 (Rel. 28, Last sequence update)
83 DT 15-JUL-1999 (Rel. 38, Last annotation update)
84 DE Probable aconitate hydratase, mitochondrial precursor (EC 4.2.1.3)
85 DE (Citrate hydro-lyase) (Aconitase).
86 GN F54H12.1.
87 OS Caenorhabditis elegans.
88 OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
89 OC Rhabditidae; Peloderinae; Caenorhabditis.
90 OX NCBI_TaxID=6239;
91 RN [1]
92 RP SEQUENCE FROM N.A.
93 RC STRAIN=BRISTOL N2;
94 RX MEDLINE=94150718; PubMed=7906398;
95 RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M.,
96 RA Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A.,
97 RA Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A.,
98 RA Fulton L., Gardner A., Green P., Hawkins T., Hillier L., Jier M.,
99 RA Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N.,
100 RA Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M.,
101 RA Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R.,
102 RA Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R.,
103 RA Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K.,
104 RA Waterson R., Watson A., Weinstock L., Wilkinson-Sproat J.,
105 RA Wohldman P.;
106 RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
107 RT elegans.";
108 RL Nature 368:32-38(1994).
109 CC -!- CATALYTIC ACTIVITY: Citrate = cis-aconitate + H(2)O.
110 CC -!- COFACTOR: ACONITASE HAS AN ACTIVE (4FE-4S) AND AN INACTIVE (3FE-
111 CC 4S) FORMS. THE ACTIVE (4FE-4S) CLUSTER IS PART OF THE CATALYTIC
112 CC SITE THAT INTERCONVERTS CITRATE, CIS-ACONITASE, AND ISOCITRATE (BY
113 CC SIMILARITY).
114 CC -!- PATHWAY: TRICARBOXYLIC ACID CYCLE.
115 CC -!- SUBUNIT: MONOMER (BY SIMILARITY).
116 CC -!- SUBCELLULAR LOCATION: Mitochondrial (By similarity).
117 CC -!- SIMILARITY: BELONGS TO THE ACONITASE/IPM ISOMERASE FAMILY.
118 CC --------------------------------------------------------------------------
119 CC This SWISS-PROT entry is copyright. It is produced through a collaboration
120 CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
121 CC the European Bioinformatics Institute. There are no restrictions on its
122 CC use by non-profit institutions as long as its content is in no way
123 CC modified and this statement is not removed. Usage by and for commercial
124 CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
125 CC or send an email to license@isb-sib.ch).
126 CC --------------------------------------------------------------------------
127 DR EMBL; L25599; AAA28050.1; -.
128 DR PIR; S44831; S44831.
129 DR HSSP; P20004; 1AMJ.
130 DR WormPep; F54H12.1; CE00516.
131 DR InterPro; IPR001030; Aconitase.
132 DR InterPro; IPR000573; Aconitase_C.
133 DR Pfam; PF00330; aconitase; 1.
134 DR Pfam; PF00694; Aconitase_C; 1.
135 DR PRINTS; PR00415; ACONITASE.
136 DR ProDom; PD000511; Aconitase; 1.
137 DR PROSITE; PS00450; ACONITASE_1; 1.
138 DR PROSITE; PS01244; ACONITASE_2; 1.
139 KW Hypothetical protein; Lyase; Tricarboxylic acid cycle; Iron-sulfur;
140 KW Mitochondrion; Transit peptide; 4Fe-4S.
141 FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL).
142 FT CHAIN ? 788 PROBABLE ACONITATE HYDRATASE.
143 FT METAL 393 393 IRON-SULFUR (4FE-4S) (BY SIMILARITY).
144 FT METAL 456 456 IRON-SULFUR (4FE-4S) (BY SIMILARITY).
145 FT METAL 459 459 IRON-SULFUR (4FE-4S) (BY SIMILARITY).
146 SQ SEQUENCE 788 AA; 85712 MW; 8861E6FC198B70D9 CRC64;
147 MRYHFLFGSL RNHLFSFRGV IYCREKLFNC SKLSFRPSKV AISKFEPKSY LPYEKLSQTV
148 KIVKDRLKRP LTLSEKILYG HLDQPKTQDI ERGVSYLRLR PDRVAMQDAT AQMAMLQFIS
149 SGLPKTAVPS TIHCDHLIEA QKGGAQDLAR AKDLNKEVFN FLATAGSKYG VGFWKPGSGI
150 IHQIILENYA FPGLLLIGTD SHTPNGGGLG GLCIGVGGAD AVDVMADIPW ELKCPKVIGI
151 KLTGKLNGWT SAKDVILKVA DILTVKGGTG AIVEYFGPGV DSISATGMGT ICNMGAEIGA
152 TTSVFPYNES MYKYLEATGR KEIAEEARKY KDLLTADDGA NYDQIIEINL DTLTPHVNGP
153 FTPDLASSID KLGENAKKNG WPLDVKVSLI GSCTNSSYED MTRAASIAKQ ALDKGLKAKT
154 IFTITPGSEQ VRATIERDGL SKIFADFGGM VLANACGPCI GQWDRQDVKK GEKNTIVTSY
155 NRNFTGRNDA NPATHGFVTS PDITTAMAIS GRLDFNPLTD ELTAADGSKF KLQAPTGLDL
156 PPKGYDPGED TFQAPSGSGQ VDVSPSSDRL QLLSPFDKWD GKDLEDMKIL IKVTGKCTTD
157 HISAAGPWLK YRGHLDNISN NLFLTAINAD NGEMNKVKNQ VTGEYGAVPA TARKYKADGV
158 RWVAIGDENY GEGSSREHAA LEPRHLGGRA IIVKSFARIH ETNLKKQGML PLTFANPADY
159 DKIDPSDNVS IVGLSSFAPG KPLTAIFKKT NGSKVEVTLN HTFNEQQIEW FKAGSALNRM
160 KEVFAKSK
161 //
162 ID 143E_HUMAN STANDARD; PRT; 255 AA.
163 AC P42655; P29360; Q63631;
164 DT 01-NOV-1995 (Rel. 32, Created)
165 DT 01-NOV-1995 (Rel. 32, Last sequence update)
166 DT 15-JUL-1999 (Rel. 38, Last annotation update)
167 DE 14-3-3 protein epsilon (Mitochondrial import stimulation factor L
168 DE subunit) (Protein kinase C inhibitor protein-1) (KCIP-1) (14-3-3E).
169 GN YWHAE.
170 OS Homo sapiens (Human),
171 OS Mus musculus (Mouse),
172 OS Rattus norvegicus (Rat),
173 OS Bos taurus (Bovine), and
174 OS Ovis aries (Sheep).
175 OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
176 OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
177 OX NCBI_TaxID=9606, 10090, 10116, 9913, 9940;
178 RN [1]
179 RP SEQUENCE FROM N.A.
180 RC SPECIES=Human;
181 RX MEDLINE=95372385; PubMed=7644510;
182 RA Conklin D.S., Galaktionov K., Beach D.;
183 RT "14-3-3 proteins associate with cdc25 phosphatases.";
184 RL Proc. Natl. Acad. Sci. U.S.A. 92:7892-7896(1995).
185 RN [2]
186 RP SEQUENCE FROM N.A.
187 RC SPECIES=Human; TISSUE=Heart;
188 RA Luk S.C.W., Lee C.Y., Waye M.M.Y.;
189 RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
190 RN [3]
191 RP SEQUENCE FROM N.A.
192 RC SPECIES=Human;
193 RX MEDLINE=96300316; PubMed=8684458;
194 RA Jin D.-Y., Lyu M.S., Kozak C.A., Jeang K.-T.;
195 RT "Function of 14-3-3 proteins.";
196 RL Nature 382:308-308(1996).
197 RN [4]
198 RP SEQUENCE FROM N.A.
199 RC SPECIES=Human; TISSUE=Liver;
200 RX MEDLINE=97011338; PubMed=8858348;
201 RA Chong S.S., Tanigami A., Roschke A.V., Ledbetter D.H.;
202 RT "14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on
203 RT chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome
204 RT region.";
205 RL Genome Res. 6:735-741(1996).
206 RN [5]
207 RP SEQUENCE FROM N.A.
208 RC SPECIES=Human;
209 RA Tanigami A., Chong S.S., Ledbetter D.H.;
210 RT "14-3-3 epsilon genomic sequence.";
211 RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
212 RN [6]
213 RP SEQUENCE FROM N.A.
214 RC SPECIES=Human; TISSUE=Placenta;
215 RA Strausberg R.;
216 RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
217 RN [7]
218 RP SEQUENCE FROM N.A.
219 RC SPECIES=Rat, and Sheep; TISSUE=Pineal gland;
220 RX MEDLINE=94296566; PubMed=8024705;
221 RA Roseboom P.H., Weller J.L., Babila T., Aitken A., Sellers L.A.,
222 RA Moffet J.R., Namboodiri M.A., Klein D.C.;
223 RT "Cloning and characterization of the epsilon and zeta isoforms of the
224 RT 14-3-3 proteins.";
225 RL DNA Cell Biol. 13:629-640(1994).
226 RN [8]
227 RP SEQUENCE FROM N.A.
228 RC SPECIES=Rat; TISSUE=Liver;
229 RX MEDLINE=95122474; PubMed=7822263;
230 RA Alam R., Hachiya N., Sakaguchi M., Shun-Ichiro K., Iwanaga S.,
231 RA Kitajima M., Mihara K., Omura T.;
232 RT "cDNA cloning and characterization of mitochondrial import
233 RT stimulation factor (MSF) purified from rat liver cytosol.";
234 RL J. Biochem. 116:416-425(1994).
235 RN [9]
236 RP SEQUENCE FROM N.A.
237 RC SPECIES=Rat; TISSUE=Brain;
238 RX MEDLINE=96280718; PubMed=8694795;
239 RA Gao L., Gu X.B., Yu D.S., Yu R.K., Zeng G.;
240 RT "Association of a 14-3-3 protein with CMP-NeuAc:GM1 alpha 2,3-
241 RT sialyltransferase.";
242 RL Biochem. Biophys. Res. Commun. 224:103-107(1996).
243 RN [10]
244 RP SEQUENCE FROM N.A.
245 RC SPECIES=Mouse; STRAIN=SWISS; TISSUE=Kidney;
246 RX MEDLINE=95269876; PubMed=7750640;
247 RA McConnell J.E., Armstrong J.F., Bard J.B.;
248 RT "The mouse 14-3-3 epsilon isoform, a kinase regulator whose
249 RT expression pattern is modulated in mesenchyme and neuronal
250 RT differentiation.";
251 RL Dev. Biol. 169:218-228(1995).
252 RN [11]
253 RP SEQUENCE FROM N.A.
254 RC SPECIES=Mouse; STRAIN=129/SV;
255 RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K.,
256 RA Shimada K.;
257 RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
258 RN [12]
259 RP SEQUENCE FROM N.A.
260 RC SPECIES=Bovine;
261 RA Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J.,
262 RA McConnell D.G.;
263 RT "Expression of 14-3-3 proteins in bovine retinal photoreceptors.";
264 RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
265 RN [13]
266 RP SEQUENCE OF 1-152; 165-184 AND 216-255.
267 RC SPECIES=Sheep; TISSUE=Brain;
268 RX MEDLINE=92283271; PubMed=1317796;
269 RA Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.;
270 RT "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3)
271 RT from sheep brain. Amino acid sequence of phosphorylated forms.";
272 RL Eur. J. Biochem. 206:453-461(1992).
273 RN [14]
274 RP SEQUENCE OF 1-23 AND 125-140.
275 RC SPECIES=Sheep; TISSUE=Brain;
276 RX MEDLINE=90345949; PubMed=2143472;
277 RA Toker A., Ellis C.A., Sellers L.A., Aitken A.;
278 RT "Protein kinase C inhibitor proteins. Purification from sheep brain
279 RT and sequence similarity to lipocortins and 14-3-3 protein.";
280 RL Eur. J. Biochem. 191:421-429(1990).
281 CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE
282 CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND
283 CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL
284 CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH
285 CC KINASES.
286 CC -!- SUBUNIT: HOMODIMER.
287 CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
288 CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND
289 CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO
290 CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES.
291 CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY.
292 CC --------------------------------------------------------------------------
293 CC This SWISS-PROT entry is copyright. It is produced through a collaboration
294 CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
295 CC the European Bioinformatics Institute. There are no restrictions on its
296 CC use by non-profit institutions as long as its content is in no way
297 CC modified and this statement is not removed. Usage by and for commercial
298 CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
299 CC or send an email to license@isb-sib.ch).
300 CC --------------------------------------------------------------------------
301 DR EMBL; U28936; AAA75301.1; -.
302 DR EMBL; U20972; AAC50175.1; -.
303 DR EMBL; U43399; AAC50625.1; -.
304 DR EMBL; U43430; AAD00026.1; -.
305 DR EMBL; U54778; AAC50710.1; -.
306 DR EMBL; AB017103; BAA32538.1; -.
307 DR EMBL; AB017098; BAA32538.1; JOINED.
308 DR EMBL; AB017099; BAA32538.1; JOINED.
309 DR EMBL; AB017100; BAA32538.1; JOINED.
310 DR EMBL; AB017101; BAA32538.1; JOINED.
311 DR EMBL; AB017102; BAA32538.1; JOINED.
312 DR EMBL; BC000179; AAH00179.1; -.
313 DR EMBL; BC001440; AAH01440.1; -.
314 DR EMBL; M84416; AAC37659.1; -.
315 DR EMBL; D30739; BAA06401.1; -.
316 DR EMBL; Z19599; CAA79659.1; -.
317 DR EMBL; U53882; AAC52676.1; -.
318 DR EMBL; L07914; AAC37321.1; -.
319 DR EMBL; D87663; BAA13424.1; -.
320 DR EMBL; AF043735; AAC61927.1; -.
321 DR PIR; S10806; S10806.
322 DR PIR; S10807; S10807.
323 DR HSSP; P29312; 1A38.
324 DR MIM; 605066; -.
325 DR MGD; MGI:894689; Ywhae.
326 DR InterPro; IPR000308; 14-3-3.
327 DR Pfam; PF00244; 14-3-3; 1.
328 DR PRINTS; PR00305; 1433ZETA.
329 DR ProDom; PD000600; 14-3-3; 1.
330 DR SMART; SM00101; 14_3_3; 1.
331 DR PROSITE; PS00796; 1433_1; 1.
332 DR PROSITE; PS00797; 1433_2; 1.
333 KW Brain; Neurone; Acetylation; Multigene family.
334 FT MOD_RES 1 1 ACETYLATION.
335 FT CONFLICT 73 73 K -> T (IN REF. 9).
336 FT CONFLICT 120 120 F -> S (IN REF. 9).
337 FT CONFLICT 123 123 K -> Y (IN REF. 9).
338 FT CONFLICT 129 129 H -> Y (IN REF. 14).
339 SQ SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64;
340 MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW
341 RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF
342 YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF
343 YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE
344 EQNKEALQDV EDENQ
345 //
346 ID 143B_BOVIN STANDARD; PRT; 245 AA.
347 AC P29358;
348 DT 01-DEC-1992 (Rel. 24, Created)
349 DT 01-FEB-1996 (Rel. 33, Last sequence update)
350 DT 16-OCT-2001 (Rel. 40, Last annotation update)
351 DE 14-3-3 protein beta/alpha (Protein kinase C inhibitor protein-1)
352 DE (KCIP-1).
353 GN YWHAB.
354 OS Bos taurus (Bovine), and
355 OS Ovis aries (Sheep).
356 OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
357 OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea;
358 OC Bovidae; Bovinae; Bos.
359 OX NCBI_TaxID=9913, 9940;
360 RN [1]
361 RP SEQUENCE.
362 RC SPECIES=Bovine;
363 RX MEDLINE=91108808; PubMed=1671102;
364 RA Isobe T., Ichimura T., Sunaya T., Okuyama T., Takahashi N., Kuwano R.,
365 RA Takahashi Y.;
366 RT "Distinct forms of the protein kinase-dependent activator of tyrosine
367 RT and tryptophan hydroxylases.";
368 RL J. Mol. Biol. 217:125-132(1991).
369 RN [2]
370 RP SEQUENCE OF 2-145 FROM N.A.
371 RC SPECIES=Bovine; TISSUE=Retina;
372 RA Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J.,
373 RA McConnell D.G.;
374 RT "Expression of 14-3-3 proteins in bovine retinal photoreceptors.";
375 RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
376 RN [3]
377 RP SEQUENCE OF 2-83; 121-186 AND 199-241.
378 RC SPECIES=Sheep; TISSUE=Brain;
379 RX MEDLINE=92283271; PubMed=1317796;
380 RA Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.;
381 RT "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3)
382 RT from sheep brain. Amino acid sequence of phosphorylated forms.";
383 RL Eur. J. Biochem. 206:453-461(1992).
384 RN [4]
385 RP SEQUENCE OF 2-23.
386 RC SPECIES=Sheep; TISSUE=Brain;
387 RX MEDLINE=90345949; PubMed=2143472;
388 RA Toker A., Ellis C.A., Sellers L.A., Aitken A.;
389 RT "Protein kinase C inhibitor proteins. Purification from sheep brain
390 RT and sequence similarity to lipocortins and 14-3-3 protein.";
391 RL Eur. J. Biochem. 191:421-429(1990).
392 RN [5]
393 RP PHOSPHORYLATION.
394 RC SPECIES=Sheep;
395 RX MEDLINE=95197587; PubMed=7890696;
396 RA Aitken A., Howell S., Jones D., Madrazo J., Patel Y.;
397 RT "14-3-3 alpha and delta are the phosphorylated forms of
398 RT raf-activating 14-3-3 beta and zeta. In vivo stoichiometric
399 RT phosphorylation in brain at a Ser-Pro-Glu-Lys motif.";
400 RL J. Biol. Chem. 270:5706-5709(1995).
401 RN [6]
402 RP POST-TRANSLATIONAL MODIFICATIONS.
403 RC SPECIES=Sheep;
404 RA Aitken A., Patel Y., Martin H., Jones D., Robinson K., Madrazo J.,
405 RA Howell S.;
406 RT "Electrospray mass spectroscopy analysis with online trapping of
407 RT posttranslationally modified mammalian and avian brain 14-3-3
408 RT isoforms.";
409 RL J. Protein Chem. 13:463-465(1994).
410 CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE
411 CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND
412 CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL
413 CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH
414 CC KINASES.
415 CC -!- SUBUNIT: HOMODIMER.
416 CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
417 CC -!- ALTERNATIVE PRODUCTS: TWO FORMS ARE PRODUCED BY ALTERNATIVE
418 CC INITIATION.
419 CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND
420 CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO
421 CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES.
422 CC -!- PTM: ISOFORM ALPHA DIFFERS FROM ISOFORM BETA IN BEING
423 CC PHOSPHORYLATED.
424 CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY.
425 CC --------------------------------------------------------------------------
426 CC This SWISS-PROT entry is copyright. It is produced through a collaboration
427 CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
428 CC the European Bioinformatics Institute. There are no restrictions on its
429 CC use by non-profit institutions as long as its content is in no way
430 CC modified and this statement is not removed. Usage by and for commercial
431 CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
432 CC or send an email to license@isb-sib.ch).
433 CC --------------------------------------------------------------------------
434 DR EMBL; AF043736; AAC02090.1; -.
435 DR PIR; S13467; S13467.
436 DR PIR; S10804; S10804.
437 DR PIR; S23179; S23179.
438 DR HSSP; P29312; 1A38.
439 DR InterPro; IPR000308; 14-3-3.
440 DR Pfam; PF00244; 14-3-3; 1.
441 DR PRINTS; PR00305; 1433ZETA.
442 DR ProDom; PD000600; 14-3-3; 1.
443 DR SMART; SM00101; 14_3_3; 1.
444 DR PROSITE; PS00796; 1433_1; 1.
445 DR PROSITE; PS00797; 1433_2; 1.
446 KW Brain; Neurone; Phosphorylation; Acetylation; Multigene family;
447 KW Alternative initiation.
448 FT INIT_MET 0 0
449 FT CHAIN 1 245 14-3-3 PROTEIN BETA/ALPHA, LONG ISOFORM.
450 FT CHAIN 2 245 14-3-3 PROTEIN BETA/ALPHA, SHORT ISOFORM.
451 FT INIT_MET 2 2 FOR SHORT ISOFORM.
452 FT MOD_RES 1 1 ACETYLATION.
453 FT MOD_RES 2 2 ACETYLATION (IN SHORT ISOFORM).
454 FT MOD_RES 185 185 PHOSPHORYLATION.
455 SQ SEQUENCE 245 AA; 27950 MW; AA91C2314D99549F CRC64;
456 TMDKSELVQK AKLAEQAERY DDMAAAMKAV TEQGHELSNE ERNLLSVAYK NVVGARRSSW
457 RVISSIEQKT ERNEKKQQMG KEYREKIEAE LQDICNDVLQ LLDKYLIPNA TQPESKVFYL
458 KMKGDYFRYL SEVASGDNKQ TTVSNSQQAY QEAFEISKKE MQPTHPIRLG LALNFSVFYY
459 EILNSPEKAC SLAKTAFDEA IAELDTLNEE SYKDSTLIMQ LLRDNLTLWT SENQGDEGDA
460 GEGEN
461 //
462 ID CALM_HUMAN STANDARD; PRT; 148 AA.
463 AC P02593; P99014; P70667; Q61379; Q61380;
464 DT 21-JUL-1986 (Rel. 01, Created)
465 DT 21-JUL-1986 (Rel. 01, Last sequence update)
466 DT 16-OCT-2001 (Rel. 40, Last annotation update)
467 DE Calmodulin.
468 GN (CALM1 OR CAM1 OR CALM OR CAM) AND (CALM2 OR CAM2 OR CAMB) AND
469 GN (CALM3 OR CAM3 OR CAMC).
470 OS Homo sapiens (Human),
471 OS Mus musculus (Mouse),
472 OS Rattus norvegicus (Rat),
473 OS Oryctolagus cuniculus (Rabbit),
474 OS Bos taurus (Bovine),
475 OS Gallus gallus (Chicken),
476 OS Anas platyrhynchos (Domestic duck),
477 OS Xenopus laevis (African clawed frog),
478 OS Arbacia punctulata (Punctuate sea urchin),
479 OS Oncorhynchus sp. (Salmon), and
480 OS Oryzias latipes (Medaka fish).
481 OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
482 OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
483 OX NCBI_TaxID=9606, 10090, 10116, 9986, 9913, 9031, 8839, 8355, 7641,
484 OX 8025, 8090;
485 RN [1]
486 RP SEQUENCE FROM N.A.
487 RC SPECIES=Human;
488 RX MEDLINE=89034207; PubMed=3182832;
489 RA Fischer R., Koller M., Flura M., Mathews S., Strehler-Page M.A.,
490 RA Krebs J., Penniston J.T., Carafoli E., Strehler E.E.;
491 RT "Multiple divergent mRNAs code for a single human calmodulin.";
492 RL J. Biol. Chem. 263:17055-17062(1988).
493 RN [2]
494 RP SEQUENCE FROM N.A.
495 RC SPECIES=Human;
496 RX MEDLINE=88059053; PubMed=2445749;
497 RA Sengupta B., Friedberg F., Detera-Wadleigh S.D.;
498 RT "Molecular analysis of human and rat calmodulin complementary DNA
499 RT clones. Evidence for additional active genes in these species.";
500 RL J. Biol. Chem. 262:16663-16670(1987).
501 RN [3]
502 RP SEQUENCE FROM N.A.
503 RC SPECIES=Human;
504 RX MEDLINE=85022688; PubMed=6385987;
505 RA Wawrzynczak E.J., Perham R.N.;
506 RT "Isolation and nucleotide sequence of a cDNA encoding human
507 RT calmodulin.";
508 RL Biochem. Int. 9:177-185(1984).
509 RN [4]
510 RP SEQUENCE FROM N.A.
511 RC SPECIES=Human; TISSUE=Blood;
512 RX MEDLINE=95010144; PubMed=7925473;
513 RA Rhyner J.A., Ottiger M., Wicki R., Greenwood T.M., Strehler E.E.;
514 RT "Structure of the human CALM1 calmodulin gene and identification of
515 RT two CALM1-related pseudogenes CALM1P1 and CALM1P2.";
516 RL Eur. J. Biochem. 225:71-82(1994).
517 RN [5]
518 RP SEQUENCE FROM N.A.
519 RC SPECIES=Human; TISSUE=Lymphoma;
520 RA Kato S.;
521 RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
522 RN [6]
523 RP SEQUENCE.
524 RC SPECIES=Human; TISSUE=Brain;
525 RX MEDLINE=82231946; PubMed=7093203;
526 RA Sasagawa T., Ericsson L.H., Walsh K.A., Schreiber W.E., Fischer E.H.,
527 RA Titani K.;
528 RT "Complete amino acid sequence of human brain calmodulin.";
529 RL Biochemistry 21:2565-2569(1982).
530 RN [7]
531 RP SEQUENCE.
532 RC SPECIES=Rabbit; TISSUE=Skeletal muscle;
533 RX MEDLINE=81138220; PubMed=7202416;
534 RA Grand R.J.A., Shenolikar S., Cohen P.;
535 RT "The amino acid sequence of the delta subunit (calmodulin) of rabbit
536 RT skeletal muscle phosphorylase kinase.";
537 RL Eur. J. Biochem. 113:359-367(1981).
538 RN [8]
539 RP SEQUENCE.
540 RC SPECIES=Bovine; TISSUE=Brain;
541 RA Kasai H., Kato Y., Isobe T., Kawasaki H., Okuyama T.;
542 RT "Determination of the complete amino acid sequence of calmodulin
543 RT (phenylalanine-rich acidic protein II) from bovine brain.";
544 RL Biomed. Res. 1:248-264(1980).
545 RN [9]
546 RP SEQUENCE.
547 RC SPECIES=Bovine; TISSUE=Brain;
548 RX MEDLINE=80094551; PubMed=7356670;
549 RA Watterson D.M., Sharief F., Vanaman T.C.;
550 RT "The complete amino acid sequence of the Ca2+-dependent modulator
551 RT protein (calmodulin) of bovine brain.";
552 RL J. Biol. Chem. 255:962-975(1980).
553 RN [10]
554 RP SEQUENCE.
555 RC SPECIES=Bovine; TISSUE=Uterus;
556 RA Grand R.J.A., Perry S.V.;
557 RT "The amino acid sequence of the troponin C-like protein (modulator
558 RT protein) from bovine uterus.";
559 RL FEBS Lett. 92:137-142(1978).
560 RN [11]
561 RP SEQUENCE OF 38-60.
562 RC SPECIES=Bovine;
563 RX MEDLINE=89064822; PubMed=3058479;
564 RA Pribilla I., Krueger H., Buchner K., Otto H., Schiebler W.,
565 RA Tripier D., Hucho F.;
566 RT "Heat-resistant inhibitors of protein kinase C from bovine brain.";
567 RL Eur. J. Biochem. 177:657-664(1988).
568 RN [12]
569 RP SEQUENCE FROM N.A.
570 RC SPECIES=Mouse;
571 RX MEDLINE=88257100; PubMed=3384819;
572 RA Bender P.K., Dedman J.R., Emerson C.P.;
573 RT "The abundance of calmodulin mRNAs is regulated in phosphorylase
574 RT kinase-deficient skeletal muscle.";
575 RL J. Biol. Chem. 263:9733-9737(1988).
576 RN [13]
577 RP SEQUENCE FROM N.A.
578 RC SPECIES=Mouse;
579 RX MEDLINE=90006775; PubMed=2551780;
580 RA Danchin A., Sezer O., Glaser P., Chalon P., Caput D.;
581 RT "Cloning and expression of mouse-brain calmodulin as an activator of
582 RT Bordetella pertussis adenylate cyclase in Escherichia coli.";
583 RL Gene 80:145-149(1989).
584 RN [14]
585 RP SEQUENCE FROM N.A.
586 RC SPECIES=Mouse; STRAIN=BALB/C; TISSUE=Brain;
587 RA Kato K.;
588 RT "A collection of cDNA clones with specific expression patterns in
589 RT mouse brain.";
590 RL Eur. J. Neurosci. 2:704-711(1991).
591 RN [15]
592 RP SEQUENCE.
593 RC SPECIES=Rat; TISSUE=Testis;
594 RX MEDLINE=78066877; PubMed=201628;
595 RA Dedman J.R., Jackson R.L., Schreiber W.E., Means A.R.;
596 RT "Sequence homology of the Ca2+-dependent regulator of cyclic
597 RT nucleotide phosphodiesterase from rat testis with other Ca2+-binding
598 RT proteins.";
599 RL J. Biol. Chem. 253:343-346(1978).
600 RN [16]
601 RP SEQUENCE FROM N.A.
602 RC SPECIES=Rat; TISSUE=Brain;
603 RX MEDLINE=87246077; PubMed=2885164;
604 RA Sherbany A.A., Parent A.S., Brosius J.;
605 RT "Rat calmodulin cDNA.";
606 RL DNA 6:267-272(1987).
607 RN [17]
608 RP SEQUENCE FROM N.A.
609 RC SPECIES=Rat; TISSUE=Brain;
610 RX MEDLINE=87226204; PubMed=3035194;
611 RA Nojima H., Hirofumi S.;
612 RT "Structure of a gene for rat calmodulin.";
613 RL J. Mol. Biol. 193:439-445(1987).
614 RN [18]
615 RP SEQUENCE FROM N.A.
616 RC SPECIES=Rat;
617 RX MEDLINE=87257889; PubMed=3037336;
618 RA Nojima H., Kishi K., Sokabe H.;
619 RT "Multiple calmodulin mRNA species are derived from two distinct
620 RT genes.";
621 RL Mol. Cell. Biol. 7:1873-1880(1987).
622 RN [19]
623 RP SEQUENCE FROM N.A.
624 RC SPECIES=Rat; STRAIN=SHR;
625 RX MEDLINE=89362474; PubMed=2527998;
626 RA Nojima H.;
627 RT "Structural organization of multiple rat calmodulin genes.";
628 RL J. Mol. Biol. 208:269-282(1989).
629 RN [20]
630 RP SEQUENCE FROM N.A.
631 RC SPECIES=Chicken;
632 RX MEDLINE=84008199; PubMed=6137485;
633 RA Putkey J.A., Ts'Ui K.F., Tanaka T., Lagace L., Stein J.P., Lai E.C.,
634 RA Means A.R.;
635 RT "Chicken calmodulin genes. A species comparison of cDNA sequences and
636 RT isolation of a genomic clone.";
637 RL J. Biol. Chem. 258:11864-11870(1983).
638 RN [21]
639 RP SEQUENCE FROM N.A.
640 RC SPECIES=Chicken;
641 RX MEDLINE=85104969; PubMed=2981850;
642 RA Simmen R.C.M., Tanaka T., Ts'Ui K.F., Putkey J.A., Scott M.J.,
643 RA Lai E.C., Means A.R.;
644 RT "The structural organization of the chicken calmodulin gene.";
645 RL J. Biol. Chem. 260:907-912(1985).
646 RN [22]
647 RP ERRATUM.
648 RC SPECIES=Chicken;
649 RA Simmen R.C.M., Tanaka T., Ts'Ui K.F., Putkey J.A., Scott M.J.,
650 RA Lai E.C., Means A.R.;
651 RL J. Biol. Chem. 262:4928-4929(1987).
652 RN [23]
653 RP SEQUENCE FROM N.A.
654 RC SPECIES=Chicken;
655 RA Iida Y.;
656 RT "cDNA sequences and molecular evolution of calmodulin genes of
657 RT chicken and eel.";
658 RL Bull. Chem. Soc. Jpn. 57:2667-2668(1984).
659 RN [24]
660 RP SEQUENCE FROM N.A.
661 RC SPECIES=A.platyrhynchos;
662 RX MEDLINE=93287810; PubMed=8389959;
663 RA Kimura N., Kurosawa N., Kondo K., Tsukada Y.;
664 RT "Molecular cloning of the kainate-binding protein and calmodulin
665 RT genes which are induced by an imprinting stimulus in ducklings.";
666 RL Brain Res. Mol. Brain Res. 17:351-355(1993).
667 RN [25]
668 RP SEQUENCE FROM N.A.
669 RC SPECIES=X.laevis;
670 RX MEDLINE=84191128; PubMed=6325880;
671 RA Chien Y.-H., Dawid I.B.;
672 RT "Isolation and characterization of calmodulin genes from Xenopus
673 RT laevis.";
674 RL Mol. Cell. Biol. 4:507-513(1984).
675 RN [26]
676 RP SEQUENCE OF 1-141 FROM N.A.
677 RC SPECIES=A.punctulata;
678 RX MEDLINE=88172463; PubMed=3351921;
679 RA Hardy D.O., Bender P.K., Kretsinger R.H.;
680 RT "Two calmodulin genes are expressed in Arbacia punctulata. An ancient
681 RT gene duplication is indicated.";
682 RL J. Mol. Biol. 199:223-227(1988).
683 RN [27]
684 RP SEQUENCE.
685 RC SPECIES=Salmon;
686 RA Yazawa M., Toda H., Yagi Y.;
687 RT "Amino acid sequence of salmon calmodulin.";
688 RL Seikagaku 57:1037-1037(1985).
689 RN [28]
690 RP SEQUENCE FROM N.A.
691 RC SPECIES=O.latipes;
692 RX MEDLINE=93012998; PubMed=1398109;
693 RA Matsuo K., Sato K., Ikeshima H., Shimoda K., Takano T.;
694 RT "Four synonymous genes encode calmodulin in the teleost fish, medaka
695 RT (Oryzias latipes): conservation of the multigene one-protein
696 RT principle.";
697 RL Gene 119:279-281(1992).
698 RN [29]
699 RP SEQUENCE OF 1-27, AND UBIQUITYLATION OF LYS-21.
700 RC SPECIES=Bovine;
701 RX MEDLINE=98380241; PubMed=9716384;
702 RA Laub M., Steppuhn J.A., Blueggel M., Immler D., Meyer H.E.,
703 RA Jennissen H.P.;
704 RT "Modulation of calmodulin function by ubiquitin-calmodulin ligase and
705 RT identification of the responsible ubiquitylation site in vertebrate
706 RT calmodulin.";
707 RL Eur. J. Biochem. 255:422-431(1998).
708 RN [30]
709 RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
710 RC SPECIES=Rat;
711 RX MEDLINE=85188323; PubMed=3990807;
712 RA Babu Y.S., Sack J.S., Greenhough T.J., Bugg C.E., Means A.R.,
713 RA Cook W.J.;
714 RT "Three-dimensional structure of calmodulin.";
715 RL Nature 315:37-40(1985).
716 RN [31]
717 RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
718 RC SPECIES=Rat;
719 RX MEDLINE=89110997; PubMed=3145979;
720 RA Babu Y.S., Bugg C.E., Cook W.J.;
721 RT "Structure of calmodulin refined at 2.2-A resolution.";
722 RL J. Mol. Biol. 204:191-204(1988).
723 RN [32]
724 RP X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
725 RC SPECIES=Bovine;
726 RX MEDLINE=98104088; PubMed=9438860;
727 RA Wall M.E., Clarage J.B., Phillips G.N.;
728 RT "Motions of calmodulin characterized using both Bragg and diffuse
729 RT X-ray scattering.";
730 RL Structure 5:1599-1612(1997).
731 RN [33]
732 RP STRUCTURE BY NMR OF 76-148.
733 RX MEDLINE=94085641; PubMed=8262263;
734 RA Finn B.E., Drakenberg T., Forsen S.;
735 RT "The structure of apo-calmodulin. A 1H NMR examination of the
736 RT carboxy-terminal domain.";
737 RL FEBS Lett. 336:368-374(1993).
738 RN [34]
739 RP STRUCTURE BY NMR OF 76-148.
740 RX MEDLINE=96018615; PubMed=7552749;
741 RA Finn B.E., Evenas J., Drakenberg T., Waltho J.P., Thulin E.,
742 RA Forsen S.;
743 RT "Calcium-induced structural changes and domain autonomy in
744 RT calmodulin.";
745 RL Nat. Struct. Biol. 2:777-783(1995).
746 RN [35]
747 RP STRUCTURE BY NMR.
748 RX MEDLINE=96018613; PubMed=7552747;
749 RA Zhang M., Tanaka T., Ikura M.;
750 RT "Calcium-induced conformational transition revealed by the solution
751 RT structure of apo calmodulin.";
752 RL Nat. Struct. Biol. 2:758-767(1995).
753 RN [36]
754 RP STRUCTURE BY NMR.
755 RX MEDLINE=96018614; PubMed=7552748;
756 RA Kuboniwa H., Tjandra N., Grzesiek S., Ren H., Klee C.B., Bax A.;
757 RT "Solution structure of calcium-free calmodulin.";
758 RL Nat. Struct. Biol. 2:768-776(1995).
759 RN [37]
760 RP STRUCTURE BY NMR.
761 RX MEDLINE=98179557; PubMed=9514729;
762 RA Osawa M., Swindells M.B., Tanikawa J., Tanaka T., Mase T., Furuya T.,
763 RA Ikura M.;
764 RT "Solution structure of calmodulin-W-7 complex: the basis of diversity
765 RT in molecular recognition.";
766 RL J. Mol. Biol. 276:165-176(1998).
767 RN [38]
768 RP STRUCTURE BY NMR.
769 RX MEDLINE=99425120; PubMed=10493800;
770 RA Elshorst B., Hennig M., Foersterling H., Diener A., Maurer M.,
771 RA Schulte P., Schwalbe H., Griesinger C., Krebs J., Schmid H.,
772 RA Vorherr T., Carafoli E.;
773 RT "NMR solution structure of a complex of calmodulin with a binding
774 RT peptide of the Ca(2+) pump.";
775 RL Biochemistry 38:12320-12332(1999).
776 CC -!- FUNCTION: CALMODULIN MEDIATES THE CONTROL OF A LARGE NUMBER OF
777 CC ENZYMES BY CA(++). AMONG THE ENZYMES TO BE STIMULATED BY THE
778 CC CALMODULIN-CA(++) COMPLEX ARE A NUMBER OF PROTEIN KINASES AND
779 CC PHOSPHATASES.
780 CC -!- PTM: UBIQUITYLATION STRONGLY DECREASES THE ACTIVITY.
781 CC -!- MISCELLANEOUS: THIS PROTEIN HAS FOUR FUNCTIONAL CALCIUM-BINDING
782 CC SITES.
783 CC -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS.
784 CC --------------------------------------------------------------------------
785 CC This SWISS-PROT entry is copyright. It is produced through a collaboration
786 CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
787 CC the European Bioinformatics Institute. There are no restrictions on its
788 CC use by non-profit institutions as long as its content is in no way
789 CC modified and this statement is not removed. Usage by and for commercial
790 CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
791 CC or send an email to license@isb-sib.ch).
792 CC --------------------------------------------------------------------------
793 DR EMBL; L00101; AAA48653.1; -.
794 DR EMBL; L00096; AAA48653.1; JOINED.
795 DR EMBL; L00097; AAA48653.1; JOINED.
796 DR EMBL; L00098; AAA48653.1; JOINED.
797 DR EMBL; L00099; AAA48653.1; JOINED.
798 DR EMBL; L00100; AAA48653.1; JOINED.
799 DR EMBL; M16659; AAA40864.1; -.
800 DR EMBL; M27319; AAA35635.1; -.
801 DR EMBL; U12022; AAB60644.1; -.
802 DR EMBL; U11886; AAB60644.1; JOINED.
803 DR EMBL; D45887; BAA08302.1; -.
804 DR EMBL; X13817; CAA32050.1; -.
805 DR EMBL; J04046; AAA51918.1; -.
806 DR EMBL; M19311; AAA35641.1; -.
807 DR EMBL; M19312; AAA40862.1; -.
808 DR EMBL; M17069; AAA40863.1; -.
809 DR EMBL; X13933; CAA32120.1; -.
810 DR EMBL; X13931; CAA32119.1; -.
811 DR EMBL; X13932; CAA32119.1; JOINED.
812 DR EMBL; X05117; CAA32119.1; JOINED.
813 DR EMBL; X13833; CAA32062.1; -.
814 DR EMBL; X13834; CAA32062.1; JOINED.
815 DR EMBL; X13835; CAA32062.1; JOINED.
816 DR EMBL; X14265; CAA32478.1; -.
817 DR EMBL; D83350; BAA11896.1; -.
818 DR EMBL; M36167; AAA48650.1; -.
819 DR EMBL; K01944; AAA49668.1; -.
820 DR EMBL; K01945; AAA49669.1; -.
821 DR EMBL; D10363; BAA01195.1; -.
822 DR EMBL; M19380; AAA66181.1; -.
823 DR EMBL; M19381; AAA66182.1; -.
824 DR EMBL; L31642; AAA65934.1; -.
825 DR EMBL; M27844; AAA37365.1; -.
826 DR EMBL; X61432; CAA43674.1; -.
827 DR PIR; S13159; MCHU.
828 DR PIR; JK0013; MCON.
829 DR PIR; A90719; MCBO.
830 DR PIR; A91104; MCRB.
831 DR PIR; S03206; MCRT.
832 DR PIR; A92394; MCCH.
833 DR PIR; S02690; S02690.
834 DR PIR; A60781; A60781.
835 DR PIR; JC1305; JC1305.
836 DR PDB; 2CLN; 15-OCT-94.
837 DR PDB; 3CLN; 09-JAN-89.
838 DR PDB; 1TRC; 15-OCT-91.
839 DR PDB; 1AK8; 17-SEP-97.
840 DR PDB; 1CDL; 31-AUG-94.
841 DR PDB; 1CDM; 31-AUG-94.
842 DR PDB; 1CFC; 07-DEC-95.
843 DR PDB; 1CFD; 07-DEC-95.
844 DR PDB; 1CLL; 31-OCT-93.
845 DR PDB; 1CM1; 04-MAR-98.
846 DR PDB; 1CM4; 04-MAR-98.
847 DR PDB; 1CMF; 07-DEC-95.
848 DR PDB; 1CMG; 07-DEC-95.
849 DR PDB; 1CTR; 20-DEC-94.
850 DR PDB; 1DEG; 31-MAY-94.
851 DR PDB; 1DMO; 01-AUG-96.
852 DR PDB; 1LIN; 08-MAR-96.
853 DR PDB; 1AJI; 17-SEP-97.
854 DR PDB; 1A29; 16-SEP-98.
855 DR PDB; 1MUX; 25-NOV-98.
856 DR PDB; 1CFF; 24-SEP-91.
857 DR SWISS-2DPAGE; P99014; MOUSE.
858 DR Aarhus/Ghent-2DPAGE; 9048; IEF.
859 DR MIM; 114180; -.
860 DR MIM; 114182; -.
861 DR MIM; 114183; -.
862 DR MGD; MGI:88251; Calm.
863 DR MGD; MGI:103250; Calm2.
864 DR MGD; MGI:103249; Calm3.
865 DR InterPro; IPR002048; EF-hand.
866 DR Pfam; PF00036; efhand; 4.
867 DR SMART; SM00054; EFh; 4.
868 DR PROSITE; PS00018; EF_HAND; 4.
869 KW Calcium-binding; Duplication; Methylation; Acetylation;
870 KW 3D-structure.
871 FT INIT_MET 0 0
872 FT MOD_RES 1 1 ACETYLATION.
873 FT MOD_RES 115 115 METHYLATION (TRI-) (IN CHICKEN).
874 FT CA_BIND 20 31 EF-HAND 1.
875 FT CA_BIND 56 67 EF-HAND 2.
876 FT CA_BIND 93 104 EF-HAND 3.
877 FT CA_BIND 129 140 EF-HAND 4.
878 FT BINDING 21 21 UBIQUITIN (MULTI-).
879 FT CONFLICT 25 25 G -> N (IN REF. 12; AAA66182).
880 FT HELIX 5 19
881 FT TURN 21 22
882 FT STRAND 26 27
883 FT HELIX 29 37
884 FT TURN 38 40
885 FT HELIX 45 55
886 FT TURN 57 58
887 FT STRAND 63 64
888 FT HELIX 65 92
889 FT TURN 94 95
890 FT STRAND 100 100
891 FT HELIX 102 111
892 FT TURN 112 113
893 FT HELIX 118 128
894 FT STRAND 136 136
895 FT HELIX 138 146
896 SQ SEQUENCE 148 AA; 16706 MW; 464B8A287475A1CA CRC64;
897 ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN
898 GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE
899 VDEMIREADI DGDGQVNYEE FVQMMTAK
900 //
BioPerl core