1433S_BOVIN
ID 1433S_BOVIN Reviewed; 248 AA.
AC Q0VC36;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=14-3-3 protein sigma;
DE AltName: Full=Stratifin;
GN Name=SFN;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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. When bound to KRT17, regulates
CC protein synthesis and epithelial cell growth by stimulating Akt/mTOR
CC pathway. May also regulate MDM2 autoubiquitination and degradation and
CC thereby activate p53/TP53 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Found in a complex with XPO7, EIF4A1, ARHGAP1,
CC VPS26A, VPS29 and VPS35. Interacts with KRT17. Interacts with GAB2 and
CC SAMSN1 (By similarity). Interacts with SRPK2 (By similarity). Interacts
CC with COPS6 (By similarity). Interacts with COP1; this interaction leads
CC to proteasomal degradation (By similarity). Interacts with the 'Thr-
CC 369' phosphorylated form of DAPK2 (By similarity). Interacts with PI4KB
CC (By similarity). Interacts with SLITRK1 (By similarity). Interacts with
CC LRRK2; this interaction is dependent on LRRK2 phosphorylation (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:O70456,
CC ECO:0000250|UniProtKB:P31947}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Secreted {ECO:0000250}. Note=May be secreted by a non-classical
CC secretory pathway. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Ubiquitination by RFFL induces proteasomal
CC degradation and indirectly regulates p53/TP53 activation (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: 14-3-3 proteins have been shown to be PKC activators,
CC but this effect could be non-specific and only due to the acidic nature
CC of the protein.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; BC120373; AAI20374.1; -; mRNA.
DR RefSeq; NP_001069380.1; NM_001075912.1.
DR AlphaFoldDB; Q0VC36; -.
DR SMR; Q0VC36; -.
DR STRING; 9913.ENSBTAP00000012154; -.
DR PaxDb; Q0VC36; -.
DR PeptideAtlas; Q0VC36; -.
DR PRIDE; Q0VC36; -.
DR Ensembl; ENSBTAT00000012154; ENSBTAP00000012154; ENSBTAG00000009223.
DR GeneID; 528453; -.
DR KEGG; bta:528453; -.
DR CTD; 2810; -.
DR VEuPathDB; HostDB:ENSBTAG00000009223; -.
DR VGNC; VGNC:34517; SFN.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244964; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; Q0VC36; -.
DR OMA; ECRVFYL; -.
DR OrthoDB; 1176818at2759; -.
DR TreeFam; TF102003; -.
DR Reactome; R-BTA-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-BTA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-BTA-9614399; Regulation of localization of FOXO transcription factors.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000009223; Expressed in esophagus and 75 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0031424; P:keratinization; IEA:Ensembl.
DR GO; GO:0003334; P:keratinocyte development; IEA:Ensembl.
DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; ISS:UniProtKB.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0010482; P:regulation of epidermal cell division; ISS:UniProtKB.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR CDD; cd10019; 14-3-3_sigma; 1.
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 InterPro; IPR037435; 14-3-3_sigma.
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 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Secreted;
KW Ubl conjugation.
FT CHAIN 1..248
FT /note="14-3-3 protein sigma"
FT /id="PRO_0000262593"
FT SITE 56
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 129
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31947"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31947"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31947"
SQ SEQUENCE 248 AA; 27849 MW; F1166FB40B23A9B3 CRC64;
MERASLIQKA KLAEQAERYE DMAAFMKSAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR
VLSSIEQKSN EESSEEKGPE VQEYREKVET ELRGVCDTVL GLLDTHLIKE AGDAESRVFY
LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH
YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG
EAPEEPQS
