TYB10_HORSE
ID TYB10_HORSE Reviewed; 44 AA.
AC P63314; P13472; Q547C6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Thymosin beta-10;
GN Name=TMSB10; Synonyms=PTMB10, THYB10;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Takafuji V.A., Sharova L.V., Crisman M.V., Howard R.D.;
RT "Equus caballus thymosin, beta 10 (TMSB10) mRNA.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-44.
RC TISSUE=Spleen;
RA Hoerger S., Gallert B., Kellerman J., Voelter W.;
RT "Isolation and structural identification of beta-thymosins from equine
RT tissue: development of a specific ELISA against thymosin beta-10 (TBeta-
RT 10).";
RL (In) Schneider C.H., Eberles A.N. (eds.);
RL Peptides 1992, pp.749-750, 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 EMBL; AF506973; AAM34215.1; -; mRNA.
DR RefSeq; NP_001075334.1; NM_001081865.1.
DR AlphaFoldDB; P63314; -.
DR SMR; P63314; -.
DR PeptideAtlas; P63314; -.
DR PRIDE; P63314; -.
DR GeneID; 100033928; -.
DR KEGG; ecb:100033928; -.
DR CTD; 9168; -.
DR InParanoid; P63314; -.
DR OrthoDB; 1632292at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0042989; P:sequestering of actin monomers; IBA:GO_Central.
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; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P21752, ECO:0000269|Ref.2"
FT CHAIN 2..44
FT /note="Thymosin beta-10"
FT /id="PRO_0000045930"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P21752"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZWY8"
FT MOD_RES 23
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P63312"
SQ SEQUENCE 44 AA; 5026 MW; 5485277C275A1C70 CRC64;
MADKPDMGEI ASFDKAKLKK TETQEKNTLP TKETIEQEKR SEIS
