ID   TYB12_ONCMY             Reviewed;          43 AA.
AC   P26352;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Thymosin beta-12;
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   PROTEIN SEQUENCE OF 2-43, AND ACETYLATION AT SER-2.
RC   TISSUE=Spleen;
RX   PubMed=1575682; DOI=10.1042/bj2830385;
RA   Yialouris P.P., Coles B., Tsitsiloni O., Schmid B., Howell S., Aitken A.,
RA   Voelter W., Haritos A.A.;
RT   "The complete sequences of trout (Salmo gairdneri) thymosin beta 11 and its
RT   homologue thymosin beta 12.";
RL   Biochem. J. 283:385-389(1992).
RN   [2]
RP   SYNTHESIS OF 2-43.
RA   Echner H., Yialouris P.P., Haritos A.A., Gruebler G., Voelter W.;
RT   "Structure and syntheses of thymosin beta-11 and beta-12.";
RL   (In) Schneider C.H., Eberles A.N. (eds.);
RL   Peptides 1992, pp.751-752, Escom Science Publishers, Leiden (1993).
CC   -!- FUNCTION: Plays an important role in the organization of the
CC       cytoskeleton. Binds to and sequesters actin monomers (G actin) and
CC       therefore inhibits actin polymerization (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
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DR   AlphaFoldDB; P26352; -.
DR   SMR; P26352; -.
DR   iPTMnet; P26352; -.
DR   Ensembl; ENSOMYT00000066307; ENSOMYP00000060905; ENSOMYG00000028165.
DR   GeneTree; ENSGT00980000198599; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003785; F:actin monomer binding; IEA:InterPro.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR   Gene3D; 1.20.5.520; -; 1.
DR   InterPro; IPR001152; Beta-thymosin.
DR   InterPro; IPR038386; Beta-thymosin_sf.
DR   PANTHER; PTHR12021; PTHR12021; 1.
DR   Pfam; PF01290; Thymosin; 1.
DR   PIRSF; PIRSF001828; Thymosin_beta; 1.
DR   SMART; SM00152; THY; 1.
DR   PROSITE; PS00500; THYMOSIN_B4; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1575682"
FT   CHAIN           2..43
FT                   /note="Thymosin beta-12"
FT                   /id="PRO_0000045940"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:1575682"
SQ   SEQUENCE   43 AA;  4891 MW;  C290B4D4CAADCA90 CRC64;
     MSDKPDLAEV SNFDKTKLKK TETQEKNPLP TKETIEQEKQ ATA