1433S_MOUSE
ID 1433S_MOUSE Reviewed; 248 AA.
AC O70456; Q3TEZ1;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=14-3-3 protein sigma;
DE AltName: Full=Stratifin;
GN Name=Sfn; Synonyms=Mkrn3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/N;
RA Karpitskiy V.V., Shaw A.S.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 1-12; 42-49; 61-68 AND 215-224, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP FUNCTION, INTERACTION WITH KRT17, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION.
RX PubMed=16710422; DOI=10.1038/nature04659;
RA Kim S., Wong P., Coulombe P.A.;
RT "A keratin cytoskeletal protein regulates protein synthesis and epithelial
RT cell growth.";
RL Nature 441:362-365(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH SAMSN1.
RX PubMed=20478393; DOI=10.1016/j.biocel.2010.05.004;
RA Brandt S., Ellwanger K., Beuter-Gunia C., Schuster M., Hausser A.,
RA Schmitz I., Beer-Hammer S.;
RT "SLy2 targets the nuclear SAP30/HDAC1 complex.";
RL Int. J. Biochem. Cell Biol. 42:1472-1481(2010).
RN [9]
RP INTERACTION WITH DAPK2.
RX PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
RA Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
RT "Suppression of death-associated protein kinase 2 by interaction with 14-3-
RT 3 proteins.";
RL Biochem. Biophys. Res. Commun. 464:70-75(2015).
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. {ECO:0000269|PubMed:16710422}.
CC -!- SUBUNIT: Homodimer. Found in a complex with XPO7, EIF4A1, ARHGAP1,
CC VPS26A, VPS29 and VPS35. Interacts with GAB2 (By similarity). Interacts
CC with KRT17. Interacts with SAMSN1. Interacts with SRPK2 (By
CC similarity). Interacts with COPS6 (By similarity). Interacts with COP1;
CC this interaction leads to proteasomal degradation (By
CC similarity).Interacts with the 'Thr-369' phosphorylated form of DAPK2
CC (PubMed:26047703). Interacts with PI4KB (By similarity). Interacts with
CC SLITRK1 (By similarity). Interacts with LRRK2; this interaction is
CC dependent on LRRK2 phosphorylation (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P31947, ECO:0000269|PubMed:26047703}.
CC -!- INTERACTION:
CC O70456; Q9QWL7: Krt17; NbExp=3; IntAct=EBI-1544118, EBI-309015;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16710422}. Nucleus
CC {ECO:0000269|PubMed:16710422}. Secreted {ECO:0000250}. Note=May be
CC secreted by a non-classical secretory pathway. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the basal layer of skin epithelium and
CC in outer root sheath of hair follicle. {ECO:0000269|PubMed:16710422}.
CC -!- INDUCTION: Induced in damaged or stressed epidermis.
CC {ECO:0000269|PubMed:16710422}.
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}.
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 EMBL; AF058798; AAC14344.1; -; mRNA.
DR EMBL; AK146490; BAE27209.1; -; mRNA.
DR EMBL; AK169358; BAE41107.1; -; mRNA.
DR EMBL; AL627228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL30056.1; -; Genomic_DNA.
DR CCDS; CCDS18754.1; -.
DR RefSeq; NP_061224.2; NM_018754.2.
DR AlphaFoldDB; O70456; -.
DR SMR; O70456; -.
DR BioGRID; 207743; 19.
DR IntAct; O70456; 6.
DR MINT; O70456; -.
DR STRING; 10090.ENSMUSP00000050374; -.
DR ChEMBL; CHEMBL1909483; -.
DR iPTMnet; O70456; -.
DR PhosphoSitePlus; O70456; -.
DR CPTAC; non-CPTAC-3758; -.
DR EPD; O70456; -.
DR jPOST; O70456; -.
DR MaxQB; O70456; -.
DR PaxDb; O70456; -.
DR PeptideAtlas; O70456; -.
DR PRIDE; O70456; -.
DR ProteomicsDB; 296416; -.
DR Antibodypedia; 1907; 779 antibodies from 45 providers.
DR DNASU; 55948; -.
DR Ensembl; ENSMUST00000057311; ENSMUSP00000050374; ENSMUSG00000047281.
DR GeneID; 55948; -.
DR KEGG; mmu:55948; -.
DR UCSC; uc008vdc.1; mouse.
DR CTD; 2810; -.
DR MGI; MGI:1891831; Sfn.
DR VEuPathDB; HostDB:ENSMUSG00000047281; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244964; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; O70456; -.
DR OMA; ECRVFYL; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; O70456; -.
DR TreeFam; TF102003; -.
DR Reactome; R-MMU-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
DR Reactome; R-MMU-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-MMU-9614399; Regulation of localization of FOXO transcription factors.
DR BioGRID-ORCS; 55948; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Sfn; mouse.
DR PRO; PR:O70456; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O70456; protein.
DR Bgee; ENSMUSG00000047281; Expressed in lip and 174 other tissues.
DR Genevisible; O70456; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
DR GO; GO:0031424; P:keratinization; IMP:MGI.
DR GO; GO:0003334; P:keratinocyte development; IGI:MGI.
DR GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR GO; GO:0043616; P:keratinocyte proliferation; IGI:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IGI:MGI.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IGI:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; IMP:UniProtKB.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:0010482; P:regulation of epidermal cell division; IMP:UniProtKB.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IGI:MGI.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Secreted; Ubl conjugation.
FT CHAIN 1..248
FT /note="14-3-3 protein sigma"
FT /id="PRO_0000058644"
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"
FT CONFLICT 244..248
FT /note="EEPQS -> DDPHI (in Ref. 1; AAC14344)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27706 MW; C1C40905824B3F48 CRC64;
MERASLIQKA KLAEQAERYE DMAAFMKSAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR
VLSSIEQKSN EEGSEEKGPE VKEYREKVET ELRGVCDTVL GLLDSHLIKG AGDAESRVFY
LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH
YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADSAGEEGG
EAPEEPQS
