Gene: [02p25/YWHAZ] tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, zeta polypeptide; tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, delta polypeptide (phosphorylated); brain protein 14-3-3, zeta subtype (phosphorylated delta subtype included); phospholipase A2-like? (brain protein 14-3-3 zeta);
COM | [1]
Previously considered a distinctive member of the 14-3-3 family, the delta
isoform is now included in the zeta subtype as the post-transla- tionally
phosphorylated product of the latter (Aitken-1995). [2] Basic information about this protein and its mRNA in man is presented in Zupan LA &:1992. Additional data relevant to functions of the protein can be found in Isobe T &:1992 and Fu H &:1993, although bovine 14-3-3 proteins were mostly discussed in these two publications. [3] It remains yet unclear which particular type of phospholipase A2 ac- tivities is associated with this gene product. There are at least the two other genes which are directly correlated with the mentioned enzyma- tic function (GEM:12q2/PLA2G1B; GEM:01p35/PLA2G2A). On the other hand, in a recent publication by Robinson K &:1994, the authors did not find PLA2 activity in brain 14-3-3 proteins tested including zeta isoform on which the original observation was made. [4] The SwissProt entry_record P29312, directly relevant to human 14-3-3 zeta, contains some confusing comments and references which will be dis- cussed in the sections 'Summary' and 'Coding_region'. [5] For general information about this protein family, see 'Summary' in FAM:BP1433/00.0" |
SUM | <*> [ZUPAN LA &:1992] (Dept of Medicine, Washington Univ School of Med- icine, St.Louis, Missouri 63110), refer to their previus study (Loeb LA, Gross RW: JBC, 261, 10467-470, 1986) in which they reported that the major phospholipase A2 activity (in sheep platelets) is mediated by at least three isoforms of a 30-kDa dimeric polypeptide which are respon- sive to physiologic increments in calcium ion and possess a significant substrate selectivity. Based on these data, they cloned the human homo- logue of one such isoform and showed that it catalyzes the cleavage of the sn-2 fatty acid of choline and ethanolamine glycerophospholipids through the formation of a stable acyl-enzyme intermediate. They also showed that 'transesterification of the sn-2 acyl group of phosphatidyl- choline to the recombinant 30-kDa polypeptide is over 50-fold selective for arachidonic acid, is augmented by calcium ion, and results in the formation of an arachidonoyl-thioester intermediate'. Sequence analysis showed that the polypeptide mediating this transesterification is a mem- ber of the 14-3-3 protein family. Finally, the authors conclude that 'their results demonstrate that at least one intracellular mammalian phospholipase A2 employs a catalytic strategy distinct from that util- ized by extracellular phospholipases A2 (ie, formation of an acyl-enzyme intermediate by nucleophilic attack versus activation of a water mole- cule) and that arachidonic acid in endogenous phospholipid storage de- pots can be sequentially transferred through an acyl-enzyme intermediate without the prior obligatory release of free arachidonic acid'. %----------------------------------------------------------------------- <*> [ISOBE T &:1992] (Dept of Chemistry, Facul of Science, Tokyo Metro- politan Univ, Japan), in their publication entitled 'Activation of pro- tein kinase C by the 14-3-3 proteins homologous with Exo1 protein that stimulates calcium-dependent exocytosis', reported that '..it has been demonstrated that a member of the 14-3-3 family, termed Exo1, stimulates Ca(2+)-dependent exocytosis in permeabilized adrenal chromaffin cells, suggesting that this protein family may influence the protein kinase C -mediated control of Ca(2+)-dependent exocytosis'. Based on these data, the authors showed that the 14-3-3 proteins activate protein kinase C at 2-fold more than the known level of the activated protein kinase C in the presence of Ca2+ and phospholipids. They suggested the possibility 'that the cellular activity of protein kinase C is regulated by diverse members of the 14-3-3 family' and that the ability of Exo1 to reactivate Ca(2+)-dependent exocytosis 'is based on its stimulatory effect on pro- tein kinase C activity.' Thus, the 14-3-3 family can be considered 'a multifunctional regulator of cell signalling processes mediated by two types of Ca(2+)-dependent protein kinase, protein kinase C and type II calmodulin-dependent protein kinase.' /Note: The above text was probably used in updating comments included in the SwissProt entry_record P29312 directly relevant to the human 14-3-3 zeta protein: (the protein) '.. STRONGLY ACTIVATES protein kinase C ..'. However, this remark is evidently inconsistent with the definition (of the protein) presented in the title of the same entry_record (see 'Sources' in 'Coding_region')\ %----------------------------------------------------------------------- <*> [FU H &:1993] (Dept Microbiology & Mol Genetics, Harvard Med School, Boston, MA 02115) discovered that the eukaryotic host factor activating exoenzyme S of Pseudomonas aeruginosa is a member of the 14-3-3 protein family. The authors referred to the following facts: Exoenzyme S, ExoS, that has been implicated as a virulence factor of P.aeruginosa, catalyzes transfer of the ADP-ribose moiety of NAD+ to many eukaryotic cellular proteins; its preferred substrates include Ras and several other 21- to 25-kDa GTP-binding proteins; ExoS absolutely requires a ubiquitous eu- karyotic protein factor, termed FAS (Factor Activating exoS), for enzy- matic activity. The authors described the cloning and expression of a gene encoding FAS from a bovine brain cDNA library and showed that pur- ified recombinant FAS produced in Escherichia coli activates ExoS in a defined cell-free system. The putative amino acid sequence of FAS shows that the protein (245 aa residues; MW 27,743 Da) belongs to a highly conserved, widely distributed eukaryotic protein family, designated as 14-3-3 proteins. Various functions have been reported for members of this family, including phospholipase A2 activity and regulation of tyro- sine/tryptophan hydroxylases and protein kinase C activities. Discovering of FAS as a 14-3-3 protein establishes an additional function for this protein family - the activation of an exogenous ADP-ribosyltransferase. %----------------------------------------------------------------------- <*> [THE CRYSTAL STRUCTURES] of bovine 14-3-3 zeta and human tau homodi- mers were recently published by Dong Liu &:1995 (Dana-Farber Cancer Inst and Dept Biol Chemistry and Mol Pharmacology, Harvard Medical School, 44 Binney Str, Boston, MA 02115, USA) and Bing Xiao &:1995 (Div of Protein Structure, National Inst for Medical Res, The Ridgeway, Mill Hill,London NW7 1AA, UK), respectively. For details of the results, see 'Summary' in FAM:BP1433/00.0" |
COD | "<* ="<*" sources="BR" title="{PRT="><**
during="J" and="phospholysis:" biol="<***" la="/ID:" cited="[GENBank] 'Human phospholipase A2 mRNA, complete cds'; //note: from a placental cDNA library\ /Date: Jul-20-1992\ /Duplicated_by: cbi:189952-953\ %----------------------------------------------------------------------- <*** record="[SwissPROT] '14-3-3 protein zeta - protein kinase C inhibitor protein-1 (KCIP-1) and phospholipase A2 and factor activating exo- enzyme S (FAS)'\ /Date: Dec-01-1992^Oct-01-1994\ /Duplicated_by: cbi:112695\ /Note_1: This swp:entry contains incorrect references to two publica- tions (Isobe T &:1992 and Fu H &:1993) and three entries (gnb:L07955, pir:S15076, and pir:S34754^S29342), none of which are related to the HUMAN 14-3-3 ZETA protein since the sources describe indeed either BOVINE zeta or the human TAU and THETA proteins, respectively. Hence, the 'conflict in the position #25: C/Cys <-|-> A/Ala' mentioned in the item 'Feature' in this swp:record (below) is irrelevant to the human 14-3-3 zeta amino acid sequence\ /Note_2: There is also the following confusing remark: (the protein) '..STRONGLY ACTIVATES protein kinase C', that is inconsistent with the definition of the zeta protein, presented above. On the other hand, this swp:entry refers to Isobe T &:1992, where the authors re- ported that one of the 14-3-3 proteins homologous to ExoI activates the protein kinase C (see 'Summary')\ /Features: total= 1..245 //note: 14-3-3 protein zeta; site= 1 //note: acetylation (putative); site= 58 //note: phosphorylation (putative); site= 63 //note: phosphorylation (putative); region= 172..245 //note: binding region to the regula- tory domain of hydroxylases\ %----------------------------------------------------------------------- <**** record="[PIR] 'phospholipase A2 (acyl-enzyme intermediate-forming; EC:3.1.1.- ), human'\ /Date: Dec-31-1992^Jun-30-1993\ /Note: This pir:record contains the following useful commentary - 'In known examples of extracellular phospholipase A2, activation of a water molecule for cleavage of ester linkages leads to the obliga- tory release of free fatty acids. In contrast, this intracellular phospholipase, a member of the family of 14-3-3 proteins, forms a stable arachidonoyl-enzyme intermediate during catalysis. In prin- ciple, this enzyme could transfer arachidonic acid sequentially to acceptors other than water, without the release of free arachidonic acid.'\ %----------------------------------------------------------------------- <* features="BR"><** notes="BR"> /Note_1: UTL, UnTransLated segment; CDS, CoDing Segment; TLI, TransLation Initiation; TLT, TransLation Termination; TTS, Transcription Termination Signal (polyA-signal); TCT, TransCription Termination site (polyA-site); pAseq, polyA-sequence\ /Note_2: 'ref1' is Zupan LA &:1992\ /Note_3: The region (82..88:gtcATGg) is referred to as the 'Kozak initiation sequence', in ref1 (gnb:M86400), although no evident consensus with other 14-3-3 sequences is found except the 'atg' start codon itself\ <** landmarks="BR"> {seg(1..84) = 5'-UTL(= 84); seg(85..819) = CDS(= 735) //note: for 245 amino acids; pos:85 = TLI_1 //note: <_atg> translation START; seg(820..2834) = 3'-UTL(=2015); pos:820 = TLT_1 //note: <_taa> translation STOP; pos:1187 = TTS_1? //note: pos:1800 = TTS_2? //note: pos:2774 = TTS_3 //note: pos:? = TCT_1? //note: polyA-site?} %----------------------------------------------------------------------- <* ="%-------- ref1: 51=ccttgcttct aggagataaa aagaacatcc agtc=84_ %-------% <** ="%-------- ref1: 85=atg gat aaa aat gag ctg gtt cag aag gcc aaa ctg gcc gag cag= pep: 16= A E R Y D D M A A C M K S V T = ref1: 130=gct gag cga tat gat gac atg gca gcc tgc atg aag tct gta act= pep: 31= E Q G A E L S N E E R N L L S = ref1: 175=gag caa gga gct gaa tta tcc aat gag gag agg aat ctt ctc tca= pep: 46= V A Y K N V V G A R R S S W R = ref1: 220=gtt gct tat aaa aat gtt gta gga gcc cgt agg tca tct tgg agg= pep: 61= V V S S I E Q K T E G A E K K = ref1: 265=gtc gtc tca agt att gaa caa aag acg gaa ggt gct gag aaa aaa= pep: 76= Q Q M A R E Y R E K I E T E L = ref1: 310=cag cag atg gct cga gaa tac aga gag aaa att gag acg gag cta= pep: 91= R D I C N D V L S L L E K F L = ref1: 355=aga gat atc tgc aat gat gta ctg tct ctt ttg gaa aag ttc ttg= pep: 106= I P N A S Q A E S K V F Y L K = ref1: 400=atc ccc aat gct tca caa gca gag agc aaa gtc ttc tat ttg aaa= pep: 121= M K G D Y Y R Y L A E V A A G = ref1: 445=atg aaa gga gat tac tac cgt tac ttg gct gag gtt gcc gct ggt= pep: 136= D D K K G I V D Q S Q Q A Y Q = ref1: 490=gat gac aag aaa ggg att gtc gat cag tca caa caa gca tac caa= pep: 151= E A F E I S K K E M Q P T H P = ref1: 535=gaa gct ttt gaa atc agc aaa aag gaa atg caa cca aca cat cct= pep: 166= I R L G L A L N F S V F Y Y E = ref1: 580=atc aga ctg ggt ctg gcc ctt aac ttc tct gtg ttc tat tat gag= pep: 181= I L N S P E K A C S L A K T A = ref1: 625=att ctg aac tcc cca gag aaa gcc tgc tct ctt gca aag aca gct= pep: 196= F D E A I A E L D T L S E E S = ref1: 670=ttt gat gaa gcc att gct gaa ctt gat aca tta agt gaa gag tca= pep 211= Y K D S T L I M Q L L R D N L = ref1: 715=tac aaa gac agc acg cta ata atg caa tta ctg aga gac aac ttg= pep 226= T L W T S D T Q G D E A E A G = ref1: 760=aca ttg tgg aca tcg gat acc caa gga gac gaa gct gaa gca gga= pep: 241= E G G E N =245\ ref1: 805=gaa gga ggg gaa aat=819_ %-------- <** ="%-------- ref1: 870=accatttgtc atccatgctg tcccacaaat agttttttgt ttacgattta= ref1: 920=tgacaggttt atgttacttc tatttgaatt tctatatttc ccatgtggtt= ref1: 970=tttatgttta atattagggg agtagagcca gttaacattt agggagttat= ref1:1020=ctgttttcat cttgaggtgg ccaatatggg gatgtggaat ttttatacaa= ref1:1070=gttataagtg tttggcatag tacttttggt acattgtggc ttcaaaaggg= ref1:1120=ccagtgtaaa actgcttcca tgtctaagca aagaaaactg cctacatact= ref1:1170=ggtttgtcct ggcggggAAT AAAagggatc attggttcca gtcacaggtg= ref1:1220=tagtaattgt gggtacttta aggtttggag cacttacaag gctgtggtag= ref1:1270=aatcataccc catggatacc acatattaaa ccatgtatat ctgtggaata= ref1:1320=ctcaatgtgt acacctttga ctacagctgc agaagtgttc ctttagacaa= ref1:1370=agttgtgacc cattttactc tggataaggg cagaaacggt tcacattcca= ref1:1420=ttatttgtaa agttacctgc tgttagcttt cattattttt gctacactca= ref1:1470=ttttatttgt atttaaatgt tttaggcaac ctaagaacaa atgtaaaagt= ref1:1520=aaagatgcag gaaaaatgaa ttgcttggta ttcattactt catgtatatc= ref1:1570=aagcacagca gtaaaacaaa aacccatgta tttaactttt ttttaggatt= ref1:1620=tttgcttttg tgattttttt tttttttttt tgatacttgc ctaacatgca= ref1:1670=tgtgctgtaa aaatagttaa cagggaaata acttgagatg atggctagct= ref1:1720=ttgtttaatg tcttatgaaa ttttcatgaa caatccaagc ataattgtta= ref1:1770=agaacacgtg tattaaattc atgtaagtgg AATAAAagtt ttatgaatgg= ref1:1820=acttttcaac tactttctct acagcttttc atgtaaatta gtcttggttc= ref1:1870=tgaaacttct ctaaaggaaa ttgtacattc tttgaaattt attccttatt= ref1:1920=ccctcttggc agctaatggg ctcttaccaa gtttaaacac aaaatttatc= ref1:1970=ataacaaaaa tactactaat ataactactg tttccatgtc ccatgatccc= ref1:2020=ctctcttcct ccccaccctg aaaaaaatga gttcctattt tttctgggag= ref1:2070=agggggggat tgattagaaa aaaatgtagt gtgttccatt taaaattttg= ref1:2120=gcatatggca ttttctaact taggaagcca caatgttctt ggcccatcat= ref1:2170=gacattgggt agcattaact gtaagttttg tgcttccaaa tcactttttg= ref1:2220=gtttttaaga atttcttgat actcttatag cctgccttca attttgatcc= ref1:2270=tttattcttt ctatttgtca ggtgcacaag attaccttcc tgttttagcc= ref1:2320=ttctgtcttg tcaccaacca ttcttacttg gtggccatgt acttggaaaa= ref1:2370=aggccgcatg atctttctgg ctccactcag tgtctaaggc accctgcttc= ref1:2420=ctttgcttgc atcccacaga ctatttccct catcctattt actgcagcaa= ref1:2470=atctctcctt agttgatgag actgtgttta tctcccttta aaaccctacc= ref1:2520=tatcctgaat ggtctgtcat tgtctgcctt taaaatcctt cctctttctt= ref1:2570=cctcctctat tctctaaata atgatggggc taagttatac ccaaagctca= ref1:2620=ctttacaaaa tatttcctca gtactttgca gaaaacacca aacaaaaatg= ref1:2670=ccattttaaa aaaggtgtat tttttctttt agaatgtaag ctcctcaaga= ref1:2720=gcagggacaa tgttttctgt atgttctatt gtgcctagta cactgtaaat= ref1:2770=gctcAATAAA tattgatgat gggaggcagt gagtcttgat gataagggtg= ref1:2820=agaaactgaa atccc=2834\" |
ECR | "<* cross-references="[PROT_DB] /Duplicated_by: cbi:112695\ /ID: pir:A38246^PSHUAM...........| prt= 245 aa /Date: Dec-31-1992^Jun-30-1993\ /ID: prosite:PS00796-797\ <* cross-references="[DNA_DB] /Duplicated_by: cbi:189952-953\" |
REF | PRT,PTM,SYS "Aitken A
&: JBC, 270, N11 (Mar 17), 5706-5709, 1995 FUN,EXP,EVO,MAM "Fu H &: PNAS, 90, N6 (Mar 15), 2320-2324, 1993 FUN,EXP,EVO,MAM "Isobe T &: FEBS Lett, 308, N2 (Aug 17), 121-124, 1992 MOP,STR,MOL "Liu D &: Nature, 376, N6536 (Jul 13), 191-194, 1995 COM,FUN "Robinson K &: Biochem J, 299 (Pt 3), N0 (May 1), 853-861, 1994 LOC "Tommerup N, Leffers H: Genomics, 33, 149-150, 1996 MOP,STR,MOL "Xiao B &: Nature, 376, N6536 (Jul 13), 188-191, 1995 CLO,SEQ,COD,LOC,MOL "Zupan LA &: JBC, 267, N13 (May 5), 8707-8710, 1992 |
SWI | SWISSPROT: P29312 |
KEY | aac, sign, lip, horm |
CLA | coding, basic |
LOC | 02 p25.2-.1 |
MIM | MIM: 601288 |
EZN | ENZYME: 3.1.1.? |
Смотрите также:
