TYB10_BOVIN
ID TYB10_BOVIN Reviewed; 42 AA.
AC P21752; Q9GMC3;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Thymosin beta-10;
DE AltName: Full=Thymosin beta-9;
DE Contains:
DE RecName: Full=Thymosin beta-8;
GN Name=TMSB10;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gutierrez-Pabello J.A., Adams L.G.;
RT "Bovine thymosin beta-10 full length cDNA sequence.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-42, AND ACETYLATION AT ALA-2.
RC TISSUE=Thymus;
RX PubMed=6952223; DOI=10.1073/pnas.79.6.1708;
RA Hannappel E., Davoust S., Horecker B.L.;
RT "Thymosins beta 8 and beta 9: two new peptides isolated from calf thymus
RT homologous to thymosin beta 4.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:1708-1711(1982).
RN [3]
RP SYNTHESIS.
RX PubMed=3818171; DOI=10.1111/j.1399-3011.1986.tb03289.x;
RA Chandramouli N., Bhargava K.K., Incefy G.S., Modak M.J., Merrifield R.B.;
RT "Solid phase synthesis of thymosin beta 9.";
RL Int. J. Pept. Protein Res. 28:536-541(1986).
RN [4]
RP STRUCTURE BY NMR.
RA Gallert B., Zarbock J., Voelter W., Holak T.A.;
RT "A nuclear magnetic resonance and simulated annealing study of thymosin
RT beta-9 in solution.";
RL (In) Schneider C.H., Eberles A.N. (eds.);
RL Peptides 1992, pp.517-518, Escom Science Publishers, Leiden (1993).
RN [5]
RP STRUCTURE BY NMR.
RC TISSUE=Thymus;
RX PubMed=9108730;
RX DOI=10.1002/(sici)1097-0282(199705)41:6<623::aid-bip3>3.0.co;2-s;
RA Stoll R., Voelter W., Holak T.A.;
RT "Conformation of thymosin beta 9 in water/fluoroalcohol solution determined
RT by NMR spectroscopy.";
RL Biopolymers 41:623-634(1997).
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 -!- TISSUE SPECIFICITY: Distributed in numerous types of tissues, including
CC thymus, spleen, lung, liver and muscle.
CC -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
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DR EMBL; AF294616; AAG03074.1; -; mRNA.
DR PIR; B19438; B19438.
DR RefSeq; NP_777048.1; NM_174623.2.
DR PDB; 1HJ0; NMR; -; A=2-42.
DR PDBsum; 1HJ0; -.
DR AlphaFoldDB; P21752; -.
DR BMRB; P21752; -.
DR SMR; P21752; -.
DR IntAct; P21752; 1.
DR STRING; 9913.ENSBTAP00000007429; -.
DR iPTMnet; P21752; -.
DR PaxDb; P21752; -.
DR PRIDE; P21752; -.
DR Ensembl; ENSBTAT00000007429; ENSBTAP00000007429; ENSBTAG00000005654.
DR GeneID; 282385; -.
DR KEGG; bta:282385; -.
DR CTD; 9168; -.
DR VEuPathDB; HostDB:ENSBTAG00000005654; -.
DR eggNOG; KOG4794; Eukaryota.
DR GeneTree; ENSGT00940000165681; -.
DR HOGENOM; CLU_208046_0_1_1; -.
DR InParanoid; P21752; -.
DR OrthoDB; 1632292at2759; -.
DR EvolutionaryTrace; P21752; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000005654; Expressed in lung and 107 other tissues.
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 3D-structure; Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6952223"
FT CHAIN 2..42
FT /note="Thymosin beta-10"
FT /id="PRO_0000034302"
FT PEPTIDE 2..40
FT /note="Thymosin beta-8"
FT /id="PRO_0000034303"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:6952223"
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 HELIX 6..28
FT /evidence="ECO:0007829|PDB:1HJ0"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1HJ0"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:1HJ0"
SQ SEQUENCE 42 AA; 4805 MW; 26D4D58BB76A8909 CRC64;
MADKPDLGEI NSFDKAKLKK TETQEKNTLP TKETIEQEKQ AK
