1433Z_SHEEP
ID 1433Z_SHEEP Reviewed; 245 AA.
AC P29361;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=14-3-3 protein zeta/delta;
DE AltName: Full=Protein kinase C inhibitor protein 1;
DE Short=KCIP-1;
GN Name=YWHAZ;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Brain;
RX PubMed=1317796; DOI=10.1111/j.1432-1033.1992.tb16946.x;
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) from
RT sheep brain. Amino acid sequence of phosphorylated forms.";
RL Eur. J. Biochem. 206:453-461(1992).
RN [2]
RP PROTEIN SEQUENCE OF 1-22 AND 122-137.
RC TISSUE=Brain;
RX PubMed=2143472; DOI=10.1111/j.1432-1033.1990.tb19138.x;
RA Toker A., Ellis C.A., Sellers L.A., Aitken A.;
RT "Protein kinase C inhibitor proteins. Purification from sheep brain and
RT sequence similarity to lipocortins and 14-3-3 protein.";
RL Eur. J. Biochem. 191:421-429(1990).
RN [3]
RP PHOSPHORYLATION AT SER-184.
RX PubMed=7890696; DOI=10.1074/jbc.270.11.5706;
RA Aitken A., Howell S., Jones D., Madrazo J., Patel Y.;
RT "14-3-3 alpha and delta are the phosphorylated forms of raf-activating 14-
RT 3-3 beta and zeta. In vivo stoichiometric phosphorylation in brain at a
RT Ser-Pro-Glu-Lys motif.";
RL J. Biol. Chem. 270:5706-5709(1995).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 isoforms.";
RL J. Protein Chem. 13:463-465(1994).
RN [5]
RP INTERACTION WITH AANAT.
RX PubMed=11427721; DOI=10.1073/pnas.141118798;
RA Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
RA Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
RA Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
RT "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-
RT binding switch in melatonin synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
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. Induces ARHGEF7 activity on RAC1
CC as well as lamellipodia and membrane ruffle formation (By similarity).
CC In neurons, regulates spine maturation through the modulation of
CC ARHGEF7 activity (By similarity). {ECO:0000250|UniProtKB:O55043,
CC ECO:0000250|UniProtKB:P63104}.
CC -!- SUBUNIT: Interacts with CDK16 and BSPRY (By similarity). Interacts with
CC WEE1 (C-terminal). Interacts with SAMSN1 (By similarity). Interacts
CC with MLF1 (phosphorylated form); the interaction retains it in the
CC cytoplasm (By similarity). Interacts with Thr-phosphorylated ITGB2 (By
CC similarity). Interacts with BCL2L11 (By similarity). Homodimer.
CC Heterodimerizes with YWHAE. Homo- and heterodimerization is inhibited
CC by phosphorylation on Ser-58. Interacts with FOXO4, NOXA1, SSH1 and
CC ARHGEF2. Interacts with Pseudomonas aeruginosa exoS (unphosphorylated
CC form). Interacts with BAX; the interaction occurs in the cytoplasm.
CC Under stress conditions, MAPK8-mediated phosphorylation releases BAX to
CC mitochondria. Interacts with phosphorylated RAF1; the interaction is
CC inhibited when YWHAZ is phosphorylated on Thr-232. Interacts with TP53;
CC the interaction enhances p53 transcriptional activity. The Ser-58
CC phosphorylated form inhibits this interaction and p53 transcriptional
CC activity. Interacts with ABL1 (phosphorylated form); the interaction
CC retains ABL1 in the cytoplasm. Interacts with PKA-phosphorylated AANAT;
CC the interaction modulates AANAT enzymatic activity by increasing
CC affinity for arylalkylamines and acetyl-CoA and protecting the enzyme
CC from dephosphorylation and proteasomal degradation. It may also prevent
CC thiol-dependent inactivation. Interacts with AKT1; the interaction
CC phosphorylates YWHAZ and modulates dimerization. Interacts with GAB2
CC and TLK2. Interacts with the 'Thr-369' phosphorylated form of DAPK2.
CC Interacts with PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts
CC with ZFP36L1 (via phosphorylated form); this interaction occurs in a
CC p38 MAPK- and AKT-signaling pathways (By similarity). Interacts with
CC SLITRK1 (By similarity). Interacts with AK5, LDB1, MADD, MARK3, PDE1A
CC and SMARCB1 (By similarity). Interacts with YWHAZ (By similarity).
CC Interacts with MEFV (By similarity). {ECO:0000250|UniProtKB:P63101,
CC ECO:0000250|UniProtKB:P63104, ECO:0000250|UniProtKB:Q9ES28}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Located to stage I to
CC stage IV melanosomes. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain (at protein level).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S10809; S10809.
DR PIR; S23304; S23304.
DR AlphaFoldDB; P29361; -.
DR BMRB; P29361; -.
DR SMR; P29361; -.
DR STRING; 9940.ENSOARP00000020034; -.
DR iPTMnet; P29361; -.
DR PRIDE; P29361; -.
DR eggNOG; KOG0841; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
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 Acetylation; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..245
FT /note="14-3-3 protein zeta/delta"
FT /id="PRO_0000058631"
FT SITE 56
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 127
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:1317796"
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:0000269|PubMed:7890696"
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"
SQ SEQUENCE 245 AA; 27856 MW; 292158A893B44CE5 CRC64;
MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR
VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNRS QPESKVFYLK
MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE
ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG
EGGEN
