BioPerl
view release on metacpan or search on metacpan
t/data/sequencefamily.dat view on Meta::CPAN
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.;
t/data/sequencefamily.dat view on Meta::CPAN
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
//
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