ID Q5CZQ1_DANRE Unreviewed; 255 AA.
AC Q5CZQ1; B2GRG9; F6NNJ2;
DT 29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 29-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=14-3-3 protein epsilon {ECO:0000256|ARBA:ARBA00039427};
GN Name=ywhae2 {ECO:0000313|EMBL:AAI65124.1,
GN ECO:0000313|Ensembl:ENSDARP00000019829,
GN ECO:0000313|RefSeq:NP_001013359.1,
GN ECO:0000313|ZFIN:ZDB-GENE-050306-44};
GN Synonyms=zgc:113329 {ECO:0000313|RefSeq:NP_001013359.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI65124.1};
RN [1] {ECO:0000313|RefSeq:NP_001013359.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore {ECO:0000313|RefSeq:NP_001013359.1};
RX PubMed=17127101;
RA Besser J., Bagowski C.P., Salas-Vidal E., van Hemert M.J., Bussmann J.,
RA Spaink H.P.;
RT "Expression analysis of the family of 14-3-3 proteins in zebrafish
RT development.";
RL Gene Expr. Patterns 7:511-520(2007).
RN [2] {ECO:0000313|EMBL:AAI65124.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Singapore local strain {ECO:0000313|EMBL:AAH90759.1};
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH90759.1}, and PCR rescue
RC {ECO:0000313|EMBL:AAI65124.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSDARP00000019829}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000019829};
RG Ensembl;
RL Submitted (FEB-2012) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSDARP00000019829, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000019829};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [5] {ECO:0000313|RefSeq:NP_001013359.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore {ECO:0000313|RefSeq:NP_001013359.1};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [6] {ECO:0000313|RefSeq:NP_001013359.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore {ECO:0000313|RefSeq:NP_001013359.1};
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [7] {ECO:0000313|RefSeq:NP_001013359.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore {ECO:0000313|RefSeq:NP_001013359.1};
RX PubMed=29653226;
RA Cao J., Tan X.;
RT "Comparative and evolutionary analysis of the 14-3-3 family genes in eleven
RT fishes.";
RL Gene 662:76-82(2018).
RN [8] {ECO:0000313|RefSeq:NP_001013359.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Singapore {ECO:0000313|RefSeq:NP_001013359.1};
RX PubMed=31017557;
RA Teixeira C.M.M., Correa C.N., Iwai L.K., Ferro E.S., Castro L.M.;
RT "Characterization of Intracellular Peptides from Zebrafish (Danio rerio)
RT Brain.";
RL Zebrafish 16:240-251(2019).
RN [9] {ECO:0000313|RefSeq:NP_001013359.1}
RP IDENTIFICATION.
RC STRAIN=Singapore {ECO:0000313|RefSeq:NP_001013359.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBUNIT: Homodimer, and heterodimer with other family members.
CC {ECO:0000256|ARBA:ARBA00011625}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family.
CC {ECO:0000256|ARBA:ARBA00006141, ECO:0000256|RuleBase:RU003466}.
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DR EMBL; CU571069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC090759; AAH90759.1; -; mRNA.
DR EMBL; BC165124; AAI65124.1; -; mRNA.
DR RefSeq; NP_001013359.1; NM_001013341.2.
DR STRING; 7955.ENSDARP00000019829; -.
DR PaxDb; 7955-ENSDARP00000019829; -.
DR Ensembl; ENSDART00000011303; ENSDARP00000019829; ENSDARG00000017014.
DR Ensembl; ENSDART00000011303.9; ENSDARP00000019829.6; ENSDARG00000017014.9.
DR GeneID; 503763; -.
DR KEGG; dre:503763; -.
DR AGR; ZFIN:ZDB-GENE-050306-44; -.
DR CTD; 503763; -.
DR ZFIN; ZDB-GENE-050306-44; ywhae2.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_0_0_1; -.
DR OMA; ICSYRSK; -.
DR OrthoDB; 920089at2759; -.
DR TreeFam; TF102003; -.
DR Proteomes; UP000000437; Chromosome 7.
DR Bgee; ENSDARG00000017014; Expressed in somite and 34 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0050815; F:phosphoserine residue binding; IBA:GO_Central.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.190.20; 14-3-3 domain; 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; 14-3-3 PROTEIN; 1.
DR PANTHER; PTHR18860:SF17; 14-3-3 PROTEIN EPSILON; 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; 14-3-3 protein; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Monooxygenase {ECO:0000313|EMBL:AAH90759.1};
KW Oxidoreductase {ECO:0000313|EMBL:AAH90759.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q5CZQ1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT DOMAIN 4..245
FT /note="14-3-3"
FT /evidence="ECO:0000259|SMART:SM00101"
FT REGION 234..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 57
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
FT SITE 130
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000256|PIRSR:PIRSR000868-1"
SQ SEQUENCE 255 AA; 28916 MW; 1925EA14FD0E0821 CRC64;
MADREHLVYQ AKLAEQAERY DEMVESMKNV AGKDEDLSVE ERNLLSVAYK NVIGARRASW
RIISSIEQKE ESKGGADKLK MIREYRQTVE NELKSICNDI LDVLDKHLIP AANTGESKVF
YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF
YYEILNSPDR ACRLAKAAFD DAIAELDTLS EDSYKDSTLI MQLLRDNLTL WTSDIQGDGE
EQSKTAPQDA EEEKQ
//
