branch-1-6/t/data/sequencefamily.dat

   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 //