1433Z_BOVIN
ID 1433Z_BOVIN Reviewed; 245 AA.
AC P63103; P29213; P29312; Q3ZCF9;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=14-3-3 protein zeta/delta;
DE AltName: Full=Factor activating exoenzyme S;
DE Short=FAS;
DE AltName: Full=Protein kinase C inhibitor protein 1;
DE Short=KCIP-1;
GN Name=YWHAZ;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1499718; DOI=10.1016/0014-5793(92)81257-m;
RA Isobe T., Hiyane Y., Ichimura T., Okuyama T., Takahashi N., Nakajo S.,
RA Nakaya K.;
RT "Activation of protein kinase C by the 14-3-3 proteins homologous with Exo1
RT protein that stimulates calcium-dependent exocytosis.";
RL FEBS Lett. 308:121-124(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 104-115; 140-157 AND
RP 194-212.
RC TISSUE=Brain;
RX PubMed=8460141; DOI=10.1073/pnas.90.6.2320;
RA Fu H., Coburn J., Collier R.J.;
RT "The eukaryotic host factor that activates exoenzyme S of Pseudomonas
RT aeruginosa is a member of the 14-3-3 protein family.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2320-2324(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=7931346; DOI=10.1046/j.1471-4159.1994.63051908.x;
RA Tanji M., Horwitz R., Rosenfeld G., Waymire J.C.;
RT "Activation of protein kinase C by purified bovine brain 14-3-3: comparison
RT with tyrosine hydroxylase activation.";
RL J. Neurochem. 63:1908-1916(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=7603574; DOI=10.1038/376191a0;
RA Liu D., Blenkowska J., Petosa C., Collier R.J., Fu H., Liddington R.;
RT "Crystal structure of the zeta isoform of the 14-3-3 protein.";
RL Nature 376:191-194(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) IN COMPLEX WITH PHOSPHORYLATED RAF1,
RP INTERACTION WITH PHOSPHOSERINE PEPTIDE, AND SUBUNIT.
RX PubMed=9632691; DOI=10.1074/jbc.273.26.16305;
RA Petosa C., Masters S.C., Bankston L.A., Pohl J., Wang B., Fu H.,
RA Liddington R.C.;
RT "14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated
RT peptide via its conserved amphipathic groove.";
RL J. Biol. Chem. 273:16305-16310(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PHOSPHORYLATED ITGB2,
RP AND INTERACTION WITH PHOSPHORYLATED ITGB2.
RX PubMed=18550856; DOI=10.1182/blood-2007-12-127795;
RA Takala H., Nurminen E., Nurmi S.M., Aatonen M., Strandin T., Takatalo M.,
RA Kiema T., Gahmberg C.G., Ylaenne J., Fagerholm S.C.;
RT "Beta2 integrin phosphorylation on Thr758 acts as a molecular switch to
RT regulate 14-3-3 and filamin binding.";
RL Blood 112:1853-1862(2008).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds to a
CC large number of partners, usually by recognition of a phosphoserine or
CC phosphothreonine motif. Binding generally results in the modulation of
CC the activity of the binding partner. Activates the ADP-
CC ribosyltransferase (exoS) activity of bacterial origin. Induces ARHGEF7
CC activity on RAC1 as well as lamellipodia and membrane ruffle formation
CC (By similarity). In neurons, regulates spine maturation through the
CC modulation of ARHGEF7 activity (By similarity).
CC {ECO:0000250|UniProtKB:O55043, ECO:0000250|UniProtKB:P63104,
CC ECO:0000269|PubMed:7931346}.
CC -!- SUBUNIT: Homodimer. Heterodimerizes with YWHAE (By similarity).
CC Homo- and heterodimerization is inhibited by phosphorylation on Ser-58
CC (By similarity). Interacts with FOXO4, NOXA1, SSH1 ARHGEF2, CDK16 and
CC BSPRY. Interacts with WEE1 (C-terminal). Interacts with MLF1
CC (phosphorylated form); the interaction retains it in the cytoplasm.
CC Interacts with BAX; the interaction occurs in the cytoplasm. Under
CC stress conditions, MAPK8-mediated phosphorylation releases BAX to
CC mitochondria. Interacts with TP53; the interaction enhances p53
CC transcriptional activity. The Ser-58 phosphorylated form inhibits this
CC interaction and p53 transcriptional activity. Interacts with ABL1
CC (phosphorylated form); the interaction retains ABL1 in the cytoplasm.
CC Interacts with PKA-phosphorylated AANAT; the interaction modulates
CC AANAT enzymatic activity by increasing affinity for arylalkylamines and
CC acetyl-CoA and protecting the enzyme from dephosphorylation and
CC proteasomal degradation. It may also prevent thiol-dependent
CC inactivation (By similarity). Interacts with AKT1; the interaction
CC phosphorylates YWHAZ and modulates dimerization (By similarity).
CC Interacts with GAB2. Interacts with BCL2L11, SAMSN1 and TLK2 (By
CC similarity). Interacts with phosphorylated RAF1; the interaction is
CC inhibited when YWHAZ is phosphorylated on Thr-232. Interacts with Thr-
CC phosphorylated ITGB2. Interacts with the 'Thr-369' phosphorylated form
CC of DAPK2 (By similarity). Interacts with PI4KB, TBC1D22A and TBC1D22B
CC (By similarity). Interacts with ZFP36L1 (via phosphorylated form); this
CC interaction occurs in a p38 MAPK- and AKT-signaling pathways (By
CC similarity). Interacts with SLITRK1 (By similarity). Interacts with
CC AK5, LDB1, MADD, MARK3, PDE1A and SMARCB1 (By similarity). Interacts
CC with YWHAZ (By similarity). Interacts with MEFV (By similarity).
CC {ECO:0000250|UniProtKB:P63101, ECO:0000250|UniProtKB:P63104,
CC ECO:0000250|UniProtKB:Q9ES28, ECO:0000269|PubMed:18550856,
CC ECO:0000269|PubMed:9632691}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Located to stage I to
CC stage IV melanosomes. {ECO:0000250}.
CC -!- PTM: The delta, brain-specific form differs from the zeta form in being
CC phosphorylated (By similarity). Phosphorylation on Ser-184 by MAPK8;
CC promotes dissociation of BAX and translocation of BAX to mitochondria.
CC Phosphorylation on Thr-232; inhibits binding of RAF1 (By similarity).
CC Phosphorylated on Ser-58 by PKA and protein kinase C delta type
CC catalytic subunit in a sphingosine-dependent fashion. Phosphorylation
CC on Ser-58 by PKA; disrupts homodimerization and heterodimerization with
CC YHAE and TP53 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; L07955; AAA30514.1; -; mRNA.
DR EMBL; BC102382; AAI02383.1; -; mRNA.
DR PIR; A47389; A47389.
DR PIR; S65013; S65013.
DR RefSeq; NP_777239.1; NM_174814.2.
DR PDB; 1A37; X-ray; 3.60 A; A/B=1-245.
DR PDB; 1A38; X-ray; 3.35 A; A/B=1-245.
DR PDB; 1A4O; X-ray; 2.80 A; A/B/C/D=1-245.
DR PDB; 2V7D; X-ray; 2.50 A; A/B/C/D=1-245.
DR PDBsum; 1A37; -.
DR PDBsum; 1A38; -.
DR PDBsum; 1A4O; -.
DR PDBsum; 2V7D; -.
DR AlphaFoldDB; P63103; -.
DR BMRB; P63103; -.
DR SMR; P63103; -.
DR BioGRID; 160005; 5.
DR IntAct; P63103; 10.
DR MINT; P63103; -.
DR STRING; 9913.ENSBTAP00000000289; -.
DR PaxDb; P63103; -.
DR PeptideAtlas; P63103; -.
DR PRIDE; P63103; -.
DR Ensembl; ENSBTAT00000000289; ENSBTAP00000000289; ENSBTAG00000000236.
DR GeneID; 287022; -.
DR KEGG; bta:287022; -.
DR CTD; 7534; -.
DR VEuPathDB; HostDB:ENSBTAG00000000236; -.
DR VGNC; VGNC:53885; YWHAZ.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; P63103; -.
DR OMA; ERVCQDV; -.
DR OrthoDB; 1176818at2759; -.
DR TreeFam; TF102003; -.
DR Reactome; R-BTA-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-BTA-392517; Rap1 signalling.
DR Reactome; R-BTA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR Reactome; R-BTA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-BTA-9013700; NOTCH4 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-BTA-9614399; Regulation of localization of FOXO transcription factors.
DR EvolutionaryTrace; P63103; -.
DR PRO; PR:P63103; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000000236; Expressed in occipital lobe and 108 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0051683; P:establishment of Golgi localization; IEA:Ensembl.
DR GO; GO:0090168; P:Golgi reassembly; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IEA:Ensembl.
DR GO; GO:0010941; P:regulation of cell death; IEA:Ensembl.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0090128; P:regulation of synapse maturation; IEA:Ensembl.
DR GO; GO:0003016; P:respiratory system process; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR GO; GO:0008039; P:synaptic target recognition; IEA:Ensembl.
DR GO; GO:0035148; P:tube formation; IEA:Ensembl.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..245
FT /note="14-3-3 protein zeta/delta"
FT /id="PRO_0000058626"
FT SITE 56
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT SITE 127
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P63104"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63104"
FT MOD_RES 58
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P63104"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63104"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63104"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63104"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63102"
FT MOD_RES 232
FT /note="Phosphothreonine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P63104"
FT CONFLICT 25
FT /note="C -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:2V7D"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:2V7D"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1A38"
FT HELIX 38..67
FT /evidence="ECO:0007829|PDB:2V7D"
FT HELIX 74..103
FT /evidence="ECO:0007829|PDB:2V7D"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:2V7D"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:2V7D"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:2V7D"
FT HELIX 137..156
FT /evidence="ECO:0007829|PDB:2V7D"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2V7D"
FT HELIX 165..180
FT /evidence="ECO:0007829|PDB:2V7D"
FT HELIX 185..201
FT /evidence="ECO:0007829|PDB:2V7D"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:2V7D"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:2V7D"
FT HELIX 211..226
FT /evidence="ECO:0007829|PDB:2V7D"
SQ SEQUENCE 245 AA; 27745 MW; D464DF2286BBFE60 CRC64;
MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR
VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QAESKVFYLK
MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE
ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG
EGGEN
