ID   143B1_ONCMY             Reviewed;         244 AA.
AC   Q6UFZ9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=14-3-3 protein beta/alpha-1;
DE            Short=Protein 14-3-3B1;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RX   PubMed=15326212; DOI=10.1242/jeb.01165;
RA   Koskinen H., Krasnov A., Rexroad C., Gorodilov Y., Afanasyev S.,
RA   Moelsae H.;
RT   "The 14-3-3 proteins in the teleost fish rainbow trout (Oncorhynchus
RT   mykiss).";
RL   J. Exp. Biol. 207:3361-3368(2004).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer, and heterodimer with other family members.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, gill, heart, intestine, kidney,
CC       liver, ovary, skin, spleen and testis. {ECO:0000269|PubMed:15326212}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development. Expressed in the
CC       neural crest, eyes, yolk syncytium, tail bud and caudal somites of
CC       somitic embryos. Expressed in the neural crest, gill covers and gill
CC       arches, and the pectoral fins of post-somitic embryos.
CC       {ECO:0000269|PubMed:15326212}.
CC   -!- INDUCTION: Repressed under stress conditions such as netting.
CC       {ECO:0000269|PubMed:15326212}.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR   EMBL; AY370879; AAQ72487.1; -; mRNA.
DR   RefSeq; NP_001117940.1; NM_001124468.1.
DR   AlphaFoldDB; Q6UFZ9; -.
DR   SMR; Q6UFZ9; -.
DR   Ensembl; ENSOMYT00000023898; ENSOMYP00000021796; ENSOMYG00000010450.
DR   GeneID; 100136192; -.
DR   KEGG; omy:100136192; -.
DR   CTD; 323055; -.
DR   GeneTree; ENSGT01050000244817; -.
DR   OrthoDB; 1176818at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm.
FT   CHAIN           1..244
FT                   /note="14-3-3 protein beta/alpha-1"
FT                   /id="PRO_0000058603"
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:0000250"
SQ   SEQUENCE   244 AA;  27575 MW;  5D92FAA5E242B092 CRC64;
     MDKNDLVQKA KLAEQAERYD DMAAAMKAVT EQGGELSNEE RNLLSVAYKN VVGARRSSWR
     VISSIEQKTE GNEKKQQMAR EYREKIEAEL QDICKDVLAL LDNYLIANAT QAESKVFYLK
     MKGDYYRYLS EVASGDSKKT TVENSQQAYQ EAFDISKKDM QPTHPIRLGL ALNFSVFYYE
     ILNSPEQACS LAKAAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS ENQGDEGDAG
     EGEN