ID   MA32_HUMAN     STANDARD;      PRT;   282 AA.
AC   Q07021;
DT   01-FEB-1995 (Rel. 31, Created)
DT   01-FEB-1995 (Rel. 31, Last sequence update)
DT   01-OCT-2000 (Rel. 40, Last annotation update)
DE   COMPLEMENT COMPONENT 1, Q SUBCOMPONENT BINDING PROTEIN, MITOCHONDRIAL
DE   PRECURSOR (GLYCOPROTEIN GC1QBP) (GC1Q-R PROTEIN) (HYALURONAN-BINDING
DE   PROTEIN 1) (PRE-MRNA SPLICING FACTOR SF2, P32 SUBUNIT) (P33).
GN   GC1QBP OR HABP1 OR SF2P32 OR C1QBP.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 74; 76-93 AND 208-216.
RC   TISSUE=FIBROBLAST;
RX   MEDLINE=94085792; PubMed=8262387;
RA   Honore B., Madsen P., Rasmussen H.H., Vandekerckhove J., Celis J.E.,
RA   Leffers H.;
RT   "Cloning and expression of a cDNA covering the complete coding region
RT   of the P32 subunit of human pre-mRNA splicing factor SF2.";
RL   Gene 134:283-287(1993).
RN   [2]
RP   SEQUENCE OF 5-282 FROM N.A., AND SEQUENCE OF 74-114.
RX   MEDLINE=91309150; PubMed=1830244;
RA   Krainer A.R., Mayeda A., Kozak D., Binns G.;
RT   "Functional expression of cloned human splicing factor SF2: homology
RT   to RNA-binding proteins, U1 70K, and Drosophila splicing regulators.";
RL   Cell 66:383-394(1991).
RN   [3]
RP   SEQUENCE FROM N.A., AND PARTIAL SEQUENCE.
RX   MEDLINE=94253723; PubMed=8195709;
RA   Ghebrehiwet B., Lim B.L., Peerschke E.I., Willis A.C., Reid K.B.;
RT   "Isolation, cDNA cloning, and overexpression of a 33-kD cell surface
RT   glycoprotein that binds to the globular 'heads' of C1q.";
RL   J. Exp. Med. 179:1809-1821(1994).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX   MEDLINE=99199225; PubMed=10097078;
RA   Jiang J., Zhang Y., Krainer A.R., Xu R.-M.;
RT   "Crystal structure of human p32, a doughnut-shaped acidic
RT   mitochondrial matrix protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:3572-3577(1999).
CC   -!- FUNCTION: NOT KNOWN. BINDS TO THE GLOBULAR "HEADS" OF C1Q THUS
CC       INHIBITING C1 ACTIVATION.
CC   -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX.
CC   -!- SIMILARITY: BELONGS TO THE MAM33 FAMILY.
CC   -!- CAUTION: WAS ORIGINALLY (REF.1 AND REF.2) THOUGHT TO BE A PRE-MRNA
CC       SPLICING FACTOR THAT PLAYS A ROLE IN PREVENTING EXON SKIPPING,
CC       ENSURING THE ACCURACY OF SPLICING AND REGULATING ALTERNATIVE
CC       SPLICING.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; L04636; AAA16315.1; -.
DR   EMBL; M69039; AAA73055.1; -.
DR   EMBL; X75913; CAA53512.1; -.
DR   PIR; JT0762; JT0762.
DR   PIR; S44104; S44104.
DR   PDB; 1P32; 06-APR-99.
DR   MIM; 601269; -.
KW   Mitochondrion; Transit peptide; 3D-structure.
FT   TRANSIT       1     73       MITOCHONDRION.
FT   CHAIN        74    282       COMPLEMENT COMPONENT 1, Q SUBCOMPONENT
FT                                BINDING PROTEIN.
SQ   SEQUENCE   282 AA;  31362 MW;  2F747FA73BB1314B CRC64;
     MLPLLRCVPR VLGSSVAGLR AAAPASPFRQ LLQPAPRLCT RPFGLLSVRA GSERRPGLLR
     PRGPCACGCG CGSLHTDGDK AFVDFLSDEI KEERKIQKHK TLPKMSGGWE LELNGTEAKL
     VRKVAGEKIT VTFNINNSIP PTFDGEEEPS QGQKVEEQEP ELTSTPNFVV EVIKNDDGKK
     ALVLDCHYPE DEVGQEDEAE SDIFSIREVS FQSTGESEWK DTNYTLNTDS LDWALYDHLM
     DFLADRGVDN TFADELVELS TALEHQEYIT FLEDLKSFVK SQ
//
ID   ACON_CAEEL     STANDARD;      PRT;   788 AA.
AC   P34455;
DT   01-FEB-1994 (Rel. 28, Created)
DT   01-FEB-1994 (Rel. 28, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   Probable aconitate hydratase, mitochondrial precursor (EC 4.2.1.3)
DE   (Citrate hydro-lyase) (Aconitase).
GN   F54H12.1.
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=BRISTOL N2;
RX   MEDLINE=94150718; PubMed=7906398;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M.,
RA   Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A.,
RA   Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A.,
RA   Fulton L., Gardner A., Green P., Hawkins T., Hillier L., Jier M.,
RA   Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N.,
RA   Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M.,
RA   Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R.,
RA   Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R.,
RA   Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K.,
RA   Waterson R., Watson A., Weinstock L., Wilkinson-Sproat J.,
RA   Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
CC   -!- CATALYTIC ACTIVITY: Citrate = cis-aconitate + H(2)O.
CC   -!- COFACTOR: ACONITASE HAS AN ACTIVE (4FE-4S) AND AN INACTIVE (3FE-
CC       4S) FORMS. THE ACTIVE (4FE-4S) CLUSTER IS PART OF THE CATALYTIC
CC       SITE THAT INTERCONVERTS CITRATE, CIS-ACONITASE, AND ISOCITRATE (BY
CC       SIMILARITY).
CC   -!- PATHWAY: TRICARBOXYLIC ACID CYCLE.
CC   -!- SUBUNIT: MONOMER (BY SIMILARITY).
CC   -!- SUBCELLULAR LOCATION: Mitochondrial (By similarity).
CC   -!- SIMILARITY: BELONGS TO THE ACONITASE/IPM ISOMERASE FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; L25599; AAA28050.1; -.
DR   PIR; S44831; S44831.
DR   HSSP; P20004; 1AMJ.
DR   WormPep; F54H12.1; CE00516.
DR   InterPro; IPR001030; Aconitase.
DR   InterPro; IPR000573; Aconitase_C.
DR   Pfam; PF00330; aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   ProDom; PD000511; Aconitase; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
KW   Hypothetical protein; Lyase; Tricarboxylic acid cycle; Iron-sulfur;
KW   Mitochondrion; Transit peptide; 4Fe-4S.
FT   TRANSIT       1      ?       MITOCHONDRION (POTENTIAL).
FT   CHAIN         ?    788       PROBABLE ACONITATE HYDRATASE.
FT   METAL       393    393       IRON-SULFUR (4FE-4S) (BY SIMILARITY).
FT   METAL       456    456       IRON-SULFUR (4FE-4S) (BY SIMILARITY).
FT   METAL       459    459       IRON-SULFUR (4FE-4S) (BY SIMILARITY).
SQ   SEQUENCE   788 AA;  85712 MW;  8861E6FC198B70D9 CRC64;
     MRYHFLFGSL RNHLFSFRGV IYCREKLFNC SKLSFRPSKV AISKFEPKSY LPYEKLSQTV
     KIVKDRLKRP LTLSEKILYG HLDQPKTQDI ERGVSYLRLR PDRVAMQDAT AQMAMLQFIS
     SGLPKTAVPS TIHCDHLIEA QKGGAQDLAR AKDLNKEVFN FLATAGSKYG VGFWKPGSGI
     IHQIILENYA FPGLLLIGTD SHTPNGGGLG GLCIGVGGAD AVDVMADIPW ELKCPKVIGI
     KLTGKLNGWT SAKDVILKVA DILTVKGGTG AIVEYFGPGV DSISATGMGT ICNMGAEIGA
     TTSVFPYNES MYKYLEATGR KEIAEEARKY KDLLTADDGA NYDQIIEINL DTLTPHVNGP
     FTPDLASSID KLGENAKKNG WPLDVKVSLI GSCTNSSYED MTRAASIAKQ ALDKGLKAKT
     IFTITPGSEQ VRATIERDGL SKIFADFGGM VLANACGPCI GQWDRQDVKK GEKNTIVTSY
     NRNFTGRNDA NPATHGFVTS PDITTAMAIS GRLDFNPLTD ELTAADGSKF KLQAPTGLDL
     PPKGYDPGED TFQAPSGSGQ VDVSPSSDRL QLLSPFDKWD GKDLEDMKIL IKVTGKCTTD
     HISAAGPWLK YRGHLDNISN NLFLTAINAD NGEMNKVKNQ VTGEYGAVPA TARKYKADGV
     RWVAIGDENY GEGSSREHAA LEPRHLGGRA IIVKSFARIH ETNLKKQGML PLTFANPADY
     DKIDPSDNVS IVGLSSFAPG KPLTAIFKKT NGSKVEVTLN HTFNEQQIEW FKAGSALNRM
     KEVFAKSK
//
ID   143E_HUMAN     STANDARD;      PRT;   255 AA.
AC   P42655; P29360; Q63631;
DT   01-NOV-1995 (Rel. 32, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   15-JUL-1999 (Rel. 38, Last annotation update)
DE   14-3-3 protein epsilon (Mitochondrial import stimulation factor L
DE   subunit) (Protein kinase C inhibitor protein-1) (KCIP-1) (14-3-3E).
GN   YWHAE.
OS   Homo sapiens (Human),
OS   Mus musculus (Mouse),
OS   Rattus norvegicus (Rat),
OS   Bos taurus (Bovine), and
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606, 10090, 10116, 9913, 9940;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Human;
RX   MEDLINE=95372385; PubMed=7644510;
RA   Conklin D.S., Galaktionov K., Beach D.;
RT   "14-3-3 proteins associate with cdc25 phosphatases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:7892-7896(1995).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Human; TISSUE=Heart;
RA   Luk S.C.W., Lee C.Y., Waye M.M.Y.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Human;
RX   MEDLINE=96300316; PubMed=8684458;
RA   Jin D.-Y., Lyu M.S., Kozak C.A., Jeang K.-T.;
RT   "Function of 14-3-3 proteins.";
RL   Nature 382:308-308(1996).
RN   [4]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Human; TISSUE=Liver;
RX   MEDLINE=97011338; PubMed=8858348;
RA   Chong S.S., Tanigami A., Roschke A.V., Ledbetter D.H.;
RT   "14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on
RT   chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome
RT   region.";
RL   Genome Res. 6:735-741(1996).
RN   [5]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Human;
RA   Tanigami A., Chong S.S., Ledbetter D.H.;
RT   "14-3-3 epsilon genomic sequence.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Human; TISSUE=Placenta;
RA   Strausberg R.;
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Rat, and Sheep; TISSUE=Pineal gland;
RX   MEDLINE=94296566; PubMed=8024705;
RA   Roseboom P.H., Weller J.L., Babila T., Aitken A., Sellers L.A.,
RA   Moffet J.R., Namboodiri M.A., Klein D.C.;
RT   "Cloning and characterization of the epsilon and zeta isoforms of the
RT   14-3-3 proteins.";
RL   DNA Cell Biol. 13:629-640(1994).
RN   [8]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Rat; TISSUE=Liver;
RX   MEDLINE=95122474; PubMed=7822263;
RA   Alam R., Hachiya N., Sakaguchi M., Shun-Ichiro K., Iwanaga S.,
RA   Kitajima M., Mihara K., Omura T.;
RT   "cDNA cloning and characterization of mitochondrial import
RT   stimulation factor (MSF) purified from rat liver cytosol.";
RL   J. Biochem. 116:416-425(1994).
RN   [9]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Rat; TISSUE=Brain;
RX   MEDLINE=96280718; PubMed=8694795;
RA   Gao L., Gu X.B., Yu D.S., Yu R.K., Zeng G.;
RT   "Association of a 14-3-3 protein with CMP-NeuAc:GM1 alpha 2,3-
RT   sialyltransferase.";
RL   Biochem. Biophys. Res. Commun. 224:103-107(1996).
RN   [10]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Mouse; STRAIN=SWISS; TISSUE=Kidney;
RX   MEDLINE=95269876; PubMed=7750640;
RA   McConnell J.E., Armstrong J.F., Bard J.B.;
RT   "The mouse 14-3-3 epsilon isoform, a kinase regulator whose
RT   expression pattern is modulated in mesenchyme and neuronal
RT   differentiation.";
RL   Dev. Biol. 169:218-228(1995).
RN   [11]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Mouse; STRAIN=129/SV;
RA   Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K.,
RA   Shimada K.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Bovine;
RA   Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J.,
RA   McConnell D.G.;
RT   "Expression of 14-3-3 proteins in bovine retinal photoreceptors.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   SEQUENCE OF 1-152; 165-184 AND 216-255.
RC   SPECIES=Sheep; TISSUE=Brain;
RX   MEDLINE=92283271; PubMed=1317796;
RA   Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.;
RT   "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3)
RT   from sheep brain. Amino acid sequence of phosphorylated forms.";
RL   Eur. J. Biochem. 206:453-461(1992).
RN   [14]
RP   SEQUENCE OF 1-23 AND 125-140.
RC   SPECIES=Sheep; TISSUE=Brain;
RX   MEDLINE=90345949; PubMed=2143472;
RA   Toker A., Ellis C.A., Sellers L.A., Aitken A.;
RT   "Protein kinase C inhibitor proteins. Purification from sheep brain
RT   and sequence similarity to lipocortins and 14-3-3 protein.";
RL   Eur. J. Biochem. 191:421-429(1990).
CC   -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE
CC       PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND
CC       STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL
CC       REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH
CC       KINASES.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND
CC       ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO
CC       PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES.
CC   -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; U28936; AAA75301.1; -.
DR   EMBL; U20972; AAC50175.1; -.
DR   EMBL; U43399; AAC50625.1; -.
DR   EMBL; U43430; AAD00026.1; -.
DR   EMBL; U54778; AAC50710.1; -.
DR   EMBL; AB017103; BAA32538.1; -.
DR   EMBL; AB017098; BAA32538.1; JOINED.
DR   EMBL; AB017099; BAA32538.1; JOINED.
DR   EMBL; AB017100; BAA32538.1; JOINED.
DR   EMBL; AB017101; BAA32538.1; JOINED.
DR   EMBL; AB017102; BAA32538.1; JOINED.
DR   EMBL; BC000179; AAH00179.1; -.
DR   EMBL; BC001440; AAH01440.1; -.
DR   EMBL; M84416; AAC37659.1; -.
DR   EMBL; D30739; BAA06401.1; -.
DR   EMBL; Z19599; CAA79659.1; -.
DR   EMBL; U53882; AAC52676.1; -.
DR   EMBL; L07914; AAC37321.1; -.
DR   EMBL; D87663; BAA13424.1; -.
DR   EMBL; AF043735; AAC61927.1; -.
DR   PIR; S10806; S10806.
DR   PIR; S10807; S10807.
DR   HSSP; P29312; 1A38.
DR   MIM; 605066; -.
DR   MGD; MGI:894689; Ywhae.
DR   InterPro; IPR000308; 14-3-3.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   ProDom; PD000600; 14-3-3; 1.
DR   SMART; SM00101; 14_3_3; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
KW   Brain; Neurone; Acetylation; Multigene family.
FT   MOD_RES       1      1       ACETYLATION.
FT   CONFLICT     73     73       K -> T (IN REF. 9).
FT   CONFLICT    120    120       F -> S (IN REF. 9).
FT   CONFLICT    123    123       K -> Y (IN REF. 9).
FT   CONFLICT    129    129       H -> Y (IN REF. 14).
SQ   SEQUENCE   255 AA;  29174 MW;  07817CCBD1F75B26 CRC64;
     MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW
     RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF
     YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF
     YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE
     EQNKEALQDV EDENQ
//
ID   143B_BOVIN     STANDARD;      PRT;   245 AA.
AC   P29358;
DT   01-DEC-1992 (Rel. 24, Created)
DT   01-FEB-1996 (Rel. 33, Last sequence update)
DT   16-OCT-2001 (Rel. 40, Last annotation update)
DE   14-3-3 protein beta/alpha (Protein kinase C inhibitor protein-1)
DE   (KCIP-1).
GN   YWHAB.
OS   Bos taurus (Bovine), and
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea;
OC   Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913, 9940;
RN   [1]
RP   SEQUENCE.
RC   SPECIES=Bovine;
RX   MEDLINE=91108808; PubMed=1671102;
RA   Isobe T., Ichimura T., Sunaya T., Okuyama T., Takahashi N., Kuwano R.,
RA   Takahashi Y.;
RT   "Distinct forms of the protein kinase-dependent activator of tyrosine
RT   and tryptophan hydroxylases.";
RL   J. Mol. Biol. 217:125-132(1991).
RN   [2]
RP   SEQUENCE OF 2-145 FROM N.A.
RC   SPECIES=Bovine; TISSUE=Retina;
RA   Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J.,
RA   McConnell D.G.;
RT   "Expression of 14-3-3 proteins in bovine retinal photoreceptors.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SEQUENCE OF 2-83; 121-186 AND 199-241.
RC   SPECIES=Sheep; TISSUE=Brain;
RX   MEDLINE=92283271; PubMed=1317796;
RA   Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.;
RT   "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3)
RT   from sheep brain. Amino acid sequence of phosphorylated forms.";
RL   Eur. J. Biochem. 206:453-461(1992).
RN   [4]
RP   SEQUENCE OF 2-23.
RC   SPECIES=Sheep; TISSUE=Brain;
RX   MEDLINE=90345949; PubMed=2143472;
RA   Toker A., Ellis C.A., Sellers L.A., Aitken A.;
RT   "Protein kinase C inhibitor proteins. Purification from sheep brain
RT   and sequence similarity to lipocortins and 14-3-3 protein.";
RL   Eur. J. Biochem. 191:421-429(1990).
RN   [5]
RP   PHOSPHORYLATION.
RC   SPECIES=Sheep;
RX   MEDLINE=95197587; PubMed=7890696;
RA   Aitken A., Howell S., Jones D., Madrazo J., Patel Y.;
RT   "14-3-3 alpha and delta are the phosphorylated forms of
RT   raf-activating 14-3-3 beta and zeta. In vivo stoichiometric
RT   phosphorylation in brain at a Ser-Pro-Glu-Lys motif.";
RL   J. Biol. Chem. 270:5706-5709(1995).
RN   [6]
RP   POST-TRANSLATIONAL MODIFICATIONS.
RC   SPECIES=Sheep;
RA   Aitken A., Patel Y., Martin H., Jones D., Robinson K., Madrazo J.,
RA   Howell S.;
RT   "Electrospray mass spectroscopy analysis with online trapping of
RT   posttranslationally modified mammalian and avian brain 14-3-3
RT   isoforms.";
RL   J. Protein Chem. 13:463-465(1994).
CC   -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE
CC       PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND
CC       STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL
CC       REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH
CC       KINASES.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- ALTERNATIVE PRODUCTS: TWO FORMS ARE PRODUCED BY ALTERNATIVE
CC       INITIATION.
CC   -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND
CC       ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO
CC       PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES.
CC   -!- PTM: ISOFORM ALPHA DIFFERS FROM ISOFORM BETA IN BEING
CC       PHOSPHORYLATED.
CC   -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; AF043736; AAC02090.1; -.
DR   PIR; S13467; S13467.
DR   PIR; S10804; S10804.
DR   PIR; S23179; S23179.
DR   HSSP; P29312; 1A38.
DR   InterPro; IPR000308; 14-3-3.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   ProDom; PD000600; 14-3-3; 1.
DR   SMART; SM00101; 14_3_3; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
KW   Brain; Neurone; Phosphorylation; Acetylation; Multigene family;
KW   Alternative initiation.
FT   INIT_MET      0      0
FT   CHAIN         1    245       14-3-3 PROTEIN BETA/ALPHA, LONG ISOFORM.
FT   CHAIN         2    245       14-3-3 PROTEIN BETA/ALPHA, SHORT ISOFORM.
FT   INIT_MET      2      2       FOR SHORT ISOFORM.
FT   MOD_RES       1      1       ACETYLATION.
FT   MOD_RES       2      2       ACETYLATION (IN SHORT ISOFORM).
FT   MOD_RES     185    185       PHOSPHORYLATION.
SQ   SEQUENCE   245 AA;  27950 MW;  AA91C2314D99549F CRC64;
     TMDKSELVQK AKLAEQAERY DDMAAAMKAV TEQGHELSNE ERNLLSVAYK NVVGARRSSW
     RVISSIEQKT ERNEKKQQMG KEYREKIEAE LQDICNDVLQ LLDKYLIPNA TQPESKVFYL
     KMKGDYFRYL SEVASGDNKQ TTVSNSQQAY QEAFEISKKE MQPTHPIRLG LALNFSVFYY
     EILNSPEKAC SLAKTAFDEA IAELDTLNEE SYKDSTLIMQ LLRDNLTLWT SENQGDEGDA
     GEGEN
//
ID   CALM_HUMAN     STANDARD;      PRT;   148 AA.
AC   P02593; P99014; P70667; Q61379; Q61380;
DT   21-JUL-1986 (Rel. 01, Created)
DT   21-JUL-1986 (Rel. 01, Last sequence update)
DT   16-OCT-2001 (Rel. 40, Last annotation update)
DE   Calmodulin.
GN   (CALM1 OR CAM1 OR CALM OR CAM) AND (CALM2 OR CAM2 OR CAMB) AND
GN   (CALM3 OR CAM3 OR CAMC).
OS   Homo sapiens (Human),
OS   Mus musculus (Mouse),
OS   Rattus norvegicus (Rat),
OS   Oryctolagus cuniculus (Rabbit),
OS   Bos taurus (Bovine),
OS   Gallus gallus (Chicken),
OS   Anas platyrhynchos (Domestic duck),
OS   Xenopus laevis (African clawed frog),
OS   Arbacia punctulata (Punctuate sea urchin),
OS   Oncorhynchus sp. (Salmon), and
OS   Oryzias latipes (Medaka fish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606, 10090, 10116, 9986, 9913, 9031, 8839, 8355, 7641,
OX   8025, 8090;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Human;
RX   MEDLINE=89034207; PubMed=3182832;
RA   Fischer R., Koller M., Flura M., Mathews S., Strehler-Page M.A.,
RA   Krebs J., Penniston J.T., Carafoli E., Strehler E.E.;
RT   "Multiple divergent mRNAs code for a single human calmodulin.";
RL   J. Biol. Chem. 263:17055-17062(1988).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Human;
RX   MEDLINE=88059053; PubMed=2445749;
RA   Sengupta B., Friedberg F., Detera-Wadleigh S.D.;
RT   "Molecular analysis of human and rat calmodulin complementary DNA
RT   clones. Evidence for additional active genes in these species.";
RL   J. Biol. Chem. 262:16663-16670(1987).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Human;
RX   MEDLINE=85022688; PubMed=6385987;
RA   Wawrzynczak E.J., Perham R.N.;
RT   "Isolation and nucleotide sequence of a cDNA encoding human
RT   calmodulin.";
RL   Biochem. Int. 9:177-185(1984).
RN   [4]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Human; TISSUE=Blood;
RX   MEDLINE=95010144; PubMed=7925473;
RA   Rhyner J.A., Ottiger M., Wicki R., Greenwood T.M., Strehler E.E.;
RT   "Structure of the human CALM1 calmodulin gene and identification of
RT   two CALM1-related pseudogenes CALM1P1 and CALM1P2.";
RL   Eur. J. Biochem. 225:71-82(1994).
RN   [5]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Human; TISSUE=Lymphoma;
RA   Kato S.;
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SEQUENCE.
RC   SPECIES=Human; TISSUE=Brain;
RX   MEDLINE=82231946; PubMed=7093203;
RA   Sasagawa T., Ericsson L.H., Walsh K.A., Schreiber W.E., Fischer E.H.,
RA   Titani K.;
RT   "Complete amino acid sequence of human brain calmodulin.";
RL   Biochemistry 21:2565-2569(1982).
RN   [7]
RP   SEQUENCE.
RC   SPECIES=Rabbit; TISSUE=Skeletal muscle;
RX   MEDLINE=81138220; PubMed=7202416;
RA   Grand R.J.A., Shenolikar S., Cohen P.;
RT   "The amino acid sequence of the delta subunit (calmodulin) of rabbit
RT   skeletal muscle phosphorylase kinase.";
RL   Eur. J. Biochem. 113:359-367(1981).
RN   [8]
RP   SEQUENCE.
RC   SPECIES=Bovine; TISSUE=Brain;
RA   Kasai H., Kato Y., Isobe T., Kawasaki H., Okuyama T.;
RT   "Determination of the complete amino acid sequence of calmodulin
RT   (phenylalanine-rich acidic protein II) from bovine brain.";
RL   Biomed. Res. 1:248-264(1980).
RN   [9]
RP   SEQUENCE.
RC   SPECIES=Bovine; TISSUE=Brain;
RX   MEDLINE=80094551; PubMed=7356670;
RA   Watterson D.M., Sharief F., Vanaman T.C.;
RT   "The complete amino acid sequence of the Ca2+-dependent modulator
RT   protein (calmodulin) of bovine brain.";
RL   J. Biol. Chem. 255:962-975(1980).
RN   [10]
RP   SEQUENCE.
RC   SPECIES=Bovine; TISSUE=Uterus;
RA   Grand R.J.A., Perry S.V.;
RT   "The amino acid sequence of the troponin C-like protein (modulator
RT   protein) from bovine uterus.";
RL   FEBS Lett. 92:137-142(1978).
RN   [11]
RP   SEQUENCE OF 38-60.
RC   SPECIES=Bovine;
RX   MEDLINE=89064822; PubMed=3058479;
RA   Pribilla I., Krueger H., Buchner K., Otto H., Schiebler W.,
RA   Tripier D., Hucho F.;
RT   "Heat-resistant inhibitors of protein kinase C from bovine brain.";
RL   Eur. J. Biochem. 177:657-664(1988).
RN   [12]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Mouse;
RX   MEDLINE=88257100; PubMed=3384819;
RA   Bender P.K., Dedman J.R., Emerson C.P.;
RT   "The abundance of calmodulin mRNAs is regulated in phosphorylase
RT   kinase-deficient skeletal muscle.";
RL   J. Biol. Chem. 263:9733-9737(1988).
RN   [13]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Mouse;
RX   MEDLINE=90006775; PubMed=2551780;
RA   Danchin A., Sezer O., Glaser P., Chalon P., Caput D.;
RT   "Cloning and expression of mouse-brain calmodulin as an activator of
RT   Bordetella pertussis adenylate cyclase in Escherichia coli.";
RL   Gene 80:145-149(1989).
RN   [14]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Mouse; STRAIN=BALB/C; TISSUE=Brain;
RA   Kato K.;
RT   "A collection of cDNA clones with specific expression patterns in
RT   mouse brain.";
RL   Eur. J. Neurosci. 2:704-711(1991).
RN   [15]
RP   SEQUENCE.
RC   SPECIES=Rat; TISSUE=Testis;
RX   MEDLINE=78066877; PubMed=201628;
RA   Dedman J.R., Jackson R.L., Schreiber W.E., Means A.R.;
RT   "Sequence homology of the Ca2+-dependent regulator of cyclic
RT   nucleotide phosphodiesterase from rat testis with other Ca2+-binding
RT   proteins.";
RL   J. Biol. Chem. 253:343-346(1978).
RN   [16]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Rat; TISSUE=Brain;
RX   MEDLINE=87246077; PubMed=2885164;
RA   Sherbany A.A., Parent A.S., Brosius J.;
RT   "Rat calmodulin cDNA.";
RL   DNA 6:267-272(1987).
RN   [17]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Rat; TISSUE=Brain;
RX   MEDLINE=87226204; PubMed=3035194;
RA   Nojima H., Hirofumi S.;
RT   "Structure of a gene for rat calmodulin.";
RL   J. Mol. Biol. 193:439-445(1987).
RN   [18]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Rat;
RX   MEDLINE=87257889; PubMed=3037336;
RA   Nojima H., Kishi K., Sokabe H.;
RT   "Multiple calmodulin mRNA species are derived from two distinct
RT   genes.";
RL   Mol. Cell. Biol. 7:1873-1880(1987).
RN   [19]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Rat; STRAIN=SHR;
RX   MEDLINE=89362474; PubMed=2527998;
RA   Nojima H.;
RT   "Structural organization of multiple rat calmodulin genes.";
RL   J. Mol. Biol. 208:269-282(1989).
RN   [20]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Chicken;
RX   MEDLINE=84008199; PubMed=6137485;
RA   Putkey J.A., Ts'Ui K.F., Tanaka T., Lagace L., Stein J.P., Lai E.C.,
RA   Means A.R.;
RT   "Chicken calmodulin genes. A species comparison of cDNA sequences and
RT   isolation of a genomic clone.";
RL   J. Biol. Chem. 258:11864-11870(1983).
RN   [21]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Chicken;
RX   MEDLINE=85104969; PubMed=2981850;
RA   Simmen R.C.M., Tanaka T., Ts'Ui K.F., Putkey J.A., Scott M.J.,
RA   Lai E.C., Means A.R.;
RT   "The structural organization of the chicken calmodulin gene.";
RL   J. Biol. Chem. 260:907-912(1985).
RN   [22]
RP   ERRATUM.
RC   SPECIES=Chicken;
RA   Simmen R.C.M., Tanaka T., Ts'Ui K.F., Putkey J.A., Scott M.J.,
RA   Lai E.C., Means A.R.;
RL   J. Biol. Chem. 262:4928-4929(1987).
RN   [23]
RP   SEQUENCE FROM N.A.
RC   SPECIES=Chicken;
RA   Iida Y.;
RT   "cDNA sequences and molecular evolution of calmodulin genes of
RT   chicken and eel.";
RL   Bull. Chem. Soc. Jpn. 57:2667-2668(1984).
RN   [24]
RP   SEQUENCE FROM N.A.
RC   SPECIES=A.platyrhynchos;
RX   MEDLINE=93287810; PubMed=8389959;
RA   Kimura N., Kurosawa N., Kondo K., Tsukada Y.;
RT   "Molecular cloning of the kainate-binding protein and calmodulin
RT   genes which are induced by an imprinting stimulus in ducklings.";
RL   Brain Res. Mol. Brain Res. 17:351-355(1993).
RN   [25]
RP   SEQUENCE FROM N.A.
RC   SPECIES=X.laevis;
RX   MEDLINE=84191128; PubMed=6325880;
RA   Chien Y.-H., Dawid I.B.;
RT   "Isolation and characterization of calmodulin genes from Xenopus
RT   laevis.";
RL   Mol. Cell. Biol. 4:507-513(1984).
RN   [26]
RP   SEQUENCE OF 1-141 FROM N.A.
RC   SPECIES=A.punctulata;
RX   MEDLINE=88172463; PubMed=3351921;
RA   Hardy D.O., Bender P.K., Kretsinger R.H.;
RT   "Two calmodulin genes are expressed in Arbacia punctulata. An ancient
RT   gene duplication is indicated.";
RL   J. Mol. Biol. 199:223-227(1988).
RN   [27]
RP   SEQUENCE.
RC   SPECIES=Salmon;
RA   Yazawa M., Toda H., Yagi Y.;
RT   "Amino acid sequence of salmon calmodulin.";
RL   Seikagaku 57:1037-1037(1985).
RN   [28]
RP   SEQUENCE FROM N.A.
RC   SPECIES=O.latipes;
RX   MEDLINE=93012998; PubMed=1398109;
RA   Matsuo K., Sato K., Ikeshima H., Shimoda K., Takano T.;
RT   "Four synonymous genes encode calmodulin in the teleost fish, medaka
RT   (Oryzias latipes): conservation of the multigene one-protein
RT   principle.";
RL   Gene 119:279-281(1992).
RN   [29]
RP   SEQUENCE OF 1-27, AND UBIQUITYLATION OF LYS-21.
RC   SPECIES=Bovine;
RX   MEDLINE=98380241; PubMed=9716384;
RA   Laub M., Steppuhn J.A., Blueggel M., Immler D., Meyer H.E.,
RA   Jennissen H.P.;
RT   "Modulation of calmodulin function by ubiquitin-calmodulin ligase and
RT   identification of the responsible ubiquitylation site in vertebrate
RT   calmodulin.";
RL   Eur. J. Biochem. 255:422-431(1998).
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RC   SPECIES=Rat;
RX   MEDLINE=85188323; PubMed=3990807;
RA   Babu Y.S., Sack J.S., Greenhough T.J., Bugg C.E., Means A.R.,
RA   Cook W.J.;
RT   "Three-dimensional structure of calmodulin.";
RL   Nature 315:37-40(1985).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RC   SPECIES=Rat;
RX   MEDLINE=89110997; PubMed=3145979;
RA   Babu Y.S., Bugg C.E., Cook W.J.;
RT   "Structure of calmodulin refined at 2.2-A resolution.";
RL   J. Mol. Biol. 204:191-204(1988).
RN   [32]
RP   X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
RC   SPECIES=Bovine;
RX   MEDLINE=98104088; PubMed=9438860;
RA   Wall M.E., Clarage J.B., Phillips G.N.;
RT   "Motions of calmodulin characterized using both Bragg and diffuse
RT   X-ray scattering.";
RL   Structure 5:1599-1612(1997).
RN   [33]
RP   STRUCTURE BY NMR OF 76-148.
RX   MEDLINE=94085641; PubMed=8262263;
RA   Finn B.E., Drakenberg T., Forsen S.;
RT   "The structure of apo-calmodulin. A 1H NMR examination of the
RT   carboxy-terminal domain.";
RL   FEBS Lett. 336:368-374(1993).
RN   [34]
RP   STRUCTURE BY NMR OF 76-148.
RX   MEDLINE=96018615; PubMed=7552749;
RA   Finn B.E., Evenas J., Drakenberg T., Waltho J.P., Thulin E.,
RA   Forsen S.;
RT   "Calcium-induced structural changes and domain autonomy in
RT   calmodulin.";
RL   Nat. Struct. Biol. 2:777-783(1995).
RN   [35]
RP   STRUCTURE BY NMR.
RX   MEDLINE=96018613; PubMed=7552747;
RA   Zhang M., Tanaka T., Ikura M.;
RT   "Calcium-induced conformational transition revealed by the solution
RT   structure of apo calmodulin.";
RL   Nat. Struct. Biol. 2:758-767(1995).
RN   [36]
RP   STRUCTURE BY NMR.
RX   MEDLINE=96018614; PubMed=7552748;
RA   Kuboniwa H., Tjandra N., Grzesiek S., Ren H., Klee C.B., Bax A.;
RT   "Solution structure of calcium-free calmodulin.";
RL   Nat. Struct. Biol. 2:768-776(1995).
RN   [37]
RP   STRUCTURE BY NMR.
RX   MEDLINE=98179557; PubMed=9514729;
RA   Osawa M., Swindells M.B., Tanikawa J., Tanaka T., Mase T., Furuya T.,
RA   Ikura M.;
RT   "Solution structure of calmodulin-W-7 complex: the basis of diversity
RT   in molecular recognition.";
RL   J. Mol. Biol. 276:165-176(1998).
RN   [38]
RP   STRUCTURE BY NMR.
RX   MEDLINE=99425120; PubMed=10493800;
RA   Elshorst B., Hennig M., Foersterling H., Diener A., Maurer M.,
RA   Schulte P., Schwalbe H., Griesinger C., Krebs J., Schmid H.,
RA   Vorherr T., Carafoli E.;
RT   "NMR solution structure of a complex of calmodulin with a binding
RT   peptide of the Ca(2+) pump.";
RL   Biochemistry 38:12320-12332(1999).
CC   -!- FUNCTION: CALMODULIN MEDIATES THE CONTROL OF A LARGE NUMBER OF
CC       ENZYMES BY CA(++). AMONG THE ENZYMES TO BE STIMULATED BY THE
CC       CALMODULIN-CA(++) COMPLEX ARE A NUMBER OF PROTEIN KINASES AND
CC       PHOSPHATASES.
CC   -!- PTM: UBIQUITYLATION STRONGLY DECREASES THE ACTIVITY.
CC   -!- MISCELLANEOUS: THIS PROTEIN HAS FOUR FUNCTIONAL CALCIUM-BINDING
CC       SITES.
CC   -!- SIMILARITY: TO OTHER EF-HAND CALCIUM BINDING PROTEINS.
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; L00101; AAA48653.1; -.
DR   EMBL; L00096; AAA48653.1; JOINED.
DR   EMBL; L00097; AAA48653.1; JOINED.
DR   EMBL; L00098; AAA48653.1; JOINED.
DR   EMBL; L00099; AAA48653.1; JOINED.
DR   EMBL; L00100; AAA48653.1; JOINED.
DR   EMBL; M16659; AAA40864.1; -.
DR   EMBL; M27319; AAA35635.1; -.
DR   EMBL; U12022; AAB60644.1; -.
DR   EMBL; U11886; AAB60644.1; JOINED.
DR   EMBL; D45887; BAA08302.1; -.
DR   EMBL; X13817; CAA32050.1; -.
DR   EMBL; J04046; AAA51918.1; -.
DR   EMBL; M19311; AAA35641.1; -.
DR   EMBL; M19312; AAA40862.1; -.
DR   EMBL; M17069; AAA40863.1; -.
DR   EMBL; X13933; CAA32120.1; -.
DR   EMBL; X13931; CAA32119.1; -.
DR   EMBL; X13932; CAA32119.1; JOINED.
DR   EMBL; X05117; CAA32119.1; JOINED.
DR   EMBL; X13833; CAA32062.1; -.
DR   EMBL; X13834; CAA32062.1; JOINED.
DR   EMBL; X13835; CAA32062.1; JOINED.
DR   EMBL; X14265; CAA32478.1; -.
DR   EMBL; D83350; BAA11896.1; -.
DR   EMBL; M36167; AAA48650.1; -.
DR   EMBL; K01944; AAA49668.1; -.
DR   EMBL; K01945; AAA49669.1; -.
DR   EMBL; D10363; BAA01195.1; -.
DR   EMBL; M19380; AAA66181.1; -.
DR   EMBL; M19381; AAA66182.1; -.
DR   EMBL; L31642; AAA65934.1; -.
DR   EMBL; M27844; AAA37365.1; -.
DR   EMBL; X61432; CAA43674.1; -.
DR   PIR; S13159; MCHU.
DR   PIR; JK0013; MCON.
DR   PIR; A90719; MCBO.
DR   PIR; A91104; MCRB.
DR   PIR; S03206; MCRT.
DR   PIR; A92394; MCCH.
DR   PIR; S02690; S02690.
DR   PIR; A60781; A60781.
DR   PIR; JC1305; JC1305.
DR   PDB; 2CLN; 15-OCT-94.
DR   PDB; 3CLN; 09-JAN-89.
DR   PDB; 1TRC; 15-OCT-91.
DR   PDB; 1AK8; 17-SEP-97.
DR   PDB; 1CDL; 31-AUG-94.
DR   PDB; 1CDM; 31-AUG-94.
DR   PDB; 1CFC; 07-DEC-95.
DR   PDB; 1CFD; 07-DEC-95.
DR   PDB; 1CLL; 31-OCT-93.
DR   PDB; 1CM1; 04-MAR-98.
DR   PDB; 1CM4; 04-MAR-98.
DR   PDB; 1CMF; 07-DEC-95.
DR   PDB; 1CMG; 07-DEC-95.
DR   PDB; 1CTR; 20-DEC-94.
DR   PDB; 1DEG; 31-MAY-94.
DR   PDB; 1DMO; 01-AUG-96.
DR   PDB; 1LIN; 08-MAR-96.
DR   PDB; 1AJI; 17-SEP-97.
DR   PDB; 1A29; 16-SEP-98.
DR   PDB; 1MUX; 25-NOV-98.
DR   PDB; 1CFF; 24-SEP-91.
DR   SWISS-2DPAGE; P99014; MOUSE.
DR   Aarhus/Ghent-2DPAGE; 9048; IEF.
DR   MIM; 114180; -.
DR   MIM; 114182; -.
DR   MIM; 114183; -.
DR   MGD; MGI:88251; Calm.
DR   MGD; MGI:103250; Calm2.
DR   MGD; MGI:103249; Calm3.
DR   InterPro; IPR002048; EF-hand.
DR   Pfam; PF00036; efhand; 4.
DR   SMART; SM00054; EFh; 4.
DR   PROSITE; PS00018; EF_HAND; 4.
KW   Calcium-binding; Duplication; Methylation; Acetylation;
KW   3D-structure.
FT   INIT_MET      0      0
FT   MOD_RES       1      1       ACETYLATION.
FT   MOD_RES     115    115       METHYLATION (TRI-) (IN CHICKEN).
FT   CA_BIND      20     31       EF-HAND 1.
FT   CA_BIND      56     67       EF-HAND 2.
FT   CA_BIND      93    104       EF-HAND 3.
FT   CA_BIND     129    140       EF-HAND 4.
FT   BINDING      21     21       UBIQUITIN (MULTI-).
FT   CONFLICT     25     25       G -> N (IN REF. 12; AAA66182).
FT   HELIX         5     19
FT   TURN         21     22
FT   STRAND       26     27
FT   HELIX        29     37
FT   TURN         38     40
FT   HELIX        45     55
FT   TURN         57     58
FT   STRAND       63     64
FT   HELIX        65     92
FT   TURN         94     95
FT   STRAND      100    100
FT   HELIX       102    111
FT   TURN        112    113
FT   HELIX       118    128
FT   STRAND      136    136
FT   HELIX       138    146
SQ   SEQUENCE   148 AA;  16706 MW;  464B8A287475A1CA CRC64;
     ADQLTEEQIA EFKEAFSLFD KDGDGTITTK ELGTVMRSLG QNPTEAELQD MINEVDADGN
     GTIDFPEFLT MMARKMKDTD SEEEIREAFR VFDKDGNGYI SAAELRHVMT NLGEKLTDEE
     VDEMIREADI DGDGQVNYEE FVQMMTAK
//