ID   143B2_ONCMY             Reviewed;         244 AA.
AC   Q6UFZ8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=14-3-3 protein beta/alpha-2;
DE            Short=Protein 14-3-3B2;
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, skeletal muscle, spleen and testis.
CC       {ECO:0000269|PubMed:15326212}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development.
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; AY370880; AAQ72488.1; -; mRNA.
DR   RefSeq; NP_001117941.1; NM_001124469.1.
DR   AlphaFoldDB; Q6UFZ8; -.
DR   SMR; Q6UFZ8; -.
DR   GeneID; 100136193; -.
DR   KEGG; omy:100136193; -.
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.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm.
FT   CHAIN           1..244
FT                   /note="14-3-3 protein beta/alpha-2"
FT                   /id="PRO_0000058604"
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;  27441 MW;  69D32DFFA9DA1F09 CRC64;
     MDKNDLVQKA KLAEQAERYD DMAGAMKSVT EQGGELSNEE RNLLSVAYKN VVGARRSSWR
     VISSIEQKTE GNEKKQAMAK EYREKIETEL QDICNDVLGL LDKYLIANAT AAESKVFYLK
     MKGDYYRYLS EVAAGDAKKT TVDNSQQAYQ DAFDISKKEM QPTHPIRLGL ALNFSVFFYE
     ILNNPEKACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LKGHLTLWTS ENQGDEGETG
     EGEN