1433Z_RAT
ID 1433Z_RAT Reviewed; 245 AA.
AC P63102; P35215; P70197; P97286; Q52KK1; Q6IRF4;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=14-3-3 protein zeta/delta;
DE AltName: Full=Mitochondrial import stimulation factor S1 subunit;
DE AltName: Full=Protein kinase C inhibitor protein 1;
DE Short=KCIP-1;
GN Name=Ywhaz; Synonyms=Msfs1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=7984035; DOI=10.1016/0169-328x(94)90285-2;
RA Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H.,
RA Inoue Y.;
RT "Molecular cloning of rat cDNAs for the zeta and theta subtypes of 14-3-3
RT protein and differential distributions of their mRNAs in the brain.";
RL Brain Res. Mol. Brain Res. 25:113-121(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX PubMed=8972907; DOI=10.1016/s0378-1119(96)00368-x;
RA Murakami K., Situ S.Y., Eshete F.;
RT "A gene variation of 14-3-3 zeta isoform in rat hippocampus.";
RL Gene 179:245-249(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7822263; DOI=10.1093/oxfordjournals.jbchem.a124541;
RA Alam R., Hachiya N., Sakaguchi M., Shun-Ichiro K., Iwanaga S., Kitajima M.,
RA Mihara K., Omura T.;
RT "cDNA cloning and characterization of mitochondrial import stimulation
RT factor (MSF) purified from rat liver cytosol.";
RL J. Biochem. 116:416-425(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-9; 12-49; 61-68; 92-115; 128-157 AND 213-222,
RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fibroblast, and Pheochromocytoma;
RA Bienvenut W.V., von Kriegsheim A., Kolch W.;
RL Submitted (JUN-2009) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 12-55; 57-68; 84-115; 121-167; 159-187 AND 194-245, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 28-41; 61-68 AND 128-139, INTERACTION WITH AANAT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
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).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-245.
RC STRAIN=Sprague-Dawley; TISSUE=Pineal gland;
RX PubMed=8024705; DOI=10.1089/dna.1994.13.629;
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 14-3-
RT 3 proteins.";
RL DNA Cell Biol. 13:629-640(1994).
RN [9]
RP TISSUE SPECIFICITY, AND INTERACTION WITH BSPRY.
RX PubMed=12615066; DOI=10.1016/s0006-291x(03)00182-7;
RA Birkenfeld J., Kartmann B., Anliker B., Ono K., Schloetcke B., Betz H.,
RA Roth D.;
RT "Characterization of zetin 1/rBSPRY, a novel binding partner of 14-3-3
RT proteins.";
RL Biochem. Biophys. Res. Commun. 302:526-533(2003).
RN [10]
RP FUNCTION.
RX PubMed=16959763; DOI=10.1074/mcp.m600147-mcp200;
RA Angrand P.O., Segura I., Voelkel P., Ghidelli S., Terry R., Brajenovic M.,
RA Vintersten K., Klein R., Superti-Furga G., Drewes G., Kuster B.,
RA Bouwmeester T., Acker-Palmer A.;
RT "Transgenic mouse proteomics identifies new 14-3-3-associated proteins
RT involved in cytoskeletal rearrangements and cell signaling.";
RL Mol. Cell. Proteomics 5:2211-2227(2006).
RN [11]
RP INTERACTION WITH BCL2L11.
RX PubMed=21478148; DOI=10.1074/jbc.m110.197707;
RA Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M., Gafken P.,
RA Henshall D.C., Morris K.T., Simon R.P., Meller R.;
RT "Identification of a novel Bcl-2-interacting mediator of cell death (Bim)
RT E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in
RT rapid ischemic tolerance-induced neuroprotection.";
RL J. Biol. Chem. 286:19331-19339(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-210, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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
CC (PubMed:16959763). In neurons, regulates spine maturation through the
CC modulation of ARHGEF7 activity (PubMed:16959763).
CC {ECO:0000269|PubMed:16959763}.
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 and ARHGEF2.
CC Interacts with CDK16 and with WEE1 (C-terminal). Interacts with MLF1
CC (phosphorylated form); the interaction retains it in the cytoplasm.
CC Interacts with Thr-phosphorylated ITGB2. Interacts with Pseudomonas
CC aeruginosa exoS (unphosphorylated form). Interacts with BAX; the
CC interaction occurs in the cytoplasm. Under stress conditions, MAPK8-
CC mediated phosphorylation releases BAX to mitochondria. Interacts with
CC phosphorylated RAF1; the interaction is inhibited when YWHAZ is
CC phosphorylated on Thr-232. Interacts with TP53; the interaction
CC enhances p53 transcriptional activity. The Ser-58 phosphorylated form
CC inhibits this interaction and p53 transcriptional activity. Interacts
CC with ABL1 (phosphorylated form); the interaction retains ABL1 in the
CC cytoplasm. Interacts with PKA-phosphorylated AANAT; the interaction
CC modulates AANAT enzymatic activity by increasing affinity for
CC arylalkylamines and acetyl-CoA and protecting the enzyme from
CC dephosphorylation and proteasomal degradation. It may also prevent
CC thiol-dependent inactivation. Interacts with AKT1; the interaction
CC phosphorylates YWHAZ and modulates dimerization (By similarity).
CC Interacts with GAB2 and SAMSN1. Binds to TLK2 (By similarity).
CC Interacts with BSPRY. Interacts with BCL2L11. Interacts with the 'Thr-
CC 369' phosphorylated form of DAPK2 (By similarity). Interacts with
CC PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with ZFP36L1
CC (via phosphorylated form); this interaction occurs in a p38 MAPK- and
CC AKT-signaling pathways (By similarity). Interacts with SLITRK1 (By
CC similarity). Interacts with AK5, LDB1, MADD, MARK3, PDE1A and SMARCB1
CC (By similarity). Interacts with YWHAZ (By similarity). Interacts with
CC MEFV (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63101,
CC ECO:0000250|UniProtKB:P63104, ECO:0000250|UniProtKB:Q9ES28,
CC ECO:0000269|PubMed:11427721, ECO:0000269|PubMed:12615066,
CC ECO:0000269|PubMed:21478148}.
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 {ECO:0000269|PubMed:12615066}.
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; D17615; BAA04534.1; -; mRNA.
DR EMBL; U37252; AAA80544.1; -; mRNA.
DR EMBL; D30740; BAA06402.1; -; mRNA.
DR EMBL; BC070941; AAH70941.2; -; mRNA.
DR EMBL; BC094305; AAH94305.1; -; mRNA.
DR EMBL; L07913; AAC37660.1; -; mRNA.
DR PIR; JC2502; JC2502.
DR PIR; JC5232; JC5232.
DR PIR; S59915; S59915.
DR RefSeq; NP_037143.2; NM_013011.3.
DR RefSeq; XP_006241591.1; XM_006241529.3.
DR AlphaFoldDB; P63102; -.
DR BMRB; P63102; -.
DR SMR; P63102; -.
DR BioGRID; 247609; 11.
DR CORUM; P63102; -.
DR DIP; DIP-36916N; -.
DR IntAct; P63102; 16.
DR MINT; P63102; -.
DR STRING; 10116.ENSRNOP00000030885; -.
DR iPTMnet; P63102; -.
DR PhosphoSitePlus; P63102; -.
DR jPOST; P63102; -.
DR PaxDb; P63102; -.
DR PRIDE; P63102; -.
DR Ensembl; ENSRNOT00000096774; ENSRNOP00000082109; ENSRNOG00000008195.
DR GeneID; 25578; -.
DR KEGG; rno:25578; -.
DR UCSC; RGD:3980; rat.
DR CTD; 7534; -.
DR RGD; 3980; Ywhaz.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; P63102; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P63102; -.
DR TreeFam; TF102003; -.
DR Reactome; R-RNO-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-RNO-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-RNO-392517; Rap1 signalling.
DR Reactome; R-RNO-430116; GP1b-IX-V activation signalling.
DR Reactome; R-RNO-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR Reactome; R-RNO-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-RNO-9013700; NOTCH4 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-RNO-9614399; Regulation of localization of FOXO transcription factors.
DR PRO; PR:P63102; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000008195; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; P63102; baseline and differential.
DR Genevisible; P63102; RN.
DR GO; GO:0031252; C:cell leading edge; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0051683; P:establishment of Golgi localization; ISO:RGD.
DR GO; GO:0090168; P:Golgi reassembly; ISO:RGD.
DR GO; GO:0002553; P:histamine secretion by mast cell; IMP:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IDA:RGD.
DR GO; GO:0010941; P:regulation of cell death; ISO:RGD.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0090128; P:regulation of synapse maturation; ISO:RGD.
DR GO; GO:0003016; P:respiratory system process; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR GO; GO:0008039; P:synaptic target recognition; ISO:RGD.
DR GO; GO:0035148; P:tube formation; ISO:RGD.
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_0000058630"
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|Ref.5"
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:0007744|PubMed:22673903"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 232
FT /note="Phosphothreonine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P63104"
FT CONFLICT 88
FT /note="T -> M (in Ref. 2; AAA80544)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="A -> R (in Ref. 8; AAC37660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 27771 MW; 2164DF3793B45B7A CRC64;
MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR
VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QPESKVFYLK
MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE
ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG
EGGEN
