TYB4_BOVIN
ID TYB4_BOVIN Reviewed; 44 AA.
AC P62326; A2VDY8; P01253; P01254; Q56JV5; Q63576;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Thymosin beta-4;
DE Short=T beta-4;
DE Contains:
DE RecName: Full=Hemoregulatory peptide AcSDKP {ECO:0000305};
DE AltName: Full=Ac-Ser-Asp-Lys-Pro {ECO:0000303|PubMed:2915977};
DE AltName: Full=N-acetyl-SDKP {ECO:0000305};
DE Short=AcSDKP {ECO:0000305};
DE AltName: Full=Seraspenide {ECO:0000250|UniProtKB:P62328};
GN Name=TMSB4; Synonyms=THYB4;
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 [LARGE SCALE MRNA].
RC TISSUE=Lymphoid epithelium;
RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT "Analysis of sequences obtained from constructed full-length bovine cDNA
RT libraries.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-44, AND ACETYLATION AT SER-2.
RX PubMed=6940133; DOI=10.1073/pnas.78.2.1162;
RA Low T.L.K., Hu S.-K., Goldstein A.L.;
RT "Complete amino acid sequence of bovine thymosin beta 4: a thymic hormone
RT that induces terminal deoxynucleotidyl transferase activity in thymocyte
RT populations.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:1162-1166(1981).
RN [4]
RP FUNCTION (HEMATOPOIETIC SYSTEM REGULATORY PEPTIDE).
RX PubMed=2915977; DOI=10.1073/pnas.86.3.779;
RA Lenfant M., Wdzieczak-Bakala J., Guittet E., Prome J.-C., Sotty D.,
RA Frindel E.;
RT "Inhibitor of hematopoietic pluripotent stem cell proliferation:
RT purification and determination of its structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:779-782(1989).
RN [5]
RP FORMATION OF HEMOREGULATORY PEPTIDE ACSDKP.
RX PubMed=2253778; DOI=10.1016/0014-5793(90)81322-f;
RA Grillon C., Rieger K., Bakala J., Schott D., Morgat J.L., Hannappel E.,
RA Voelter W., Lenfant M.;
RT "Involvement of thymosin beta 4 and endoproteinase Asp-N in the
RT biosynthesis of the tetrapeptide AcSerAspLysPro a regulator of the
RT hematopoietic system.";
RL FEBS Lett. 274:30-34(1990).
RN [6]
RP INTERACTION WITH SERPINB1.
RX PubMed=1551869; DOI=10.1016/s0021-9258(19)50466-5;
RA Dubin A., Travis J., Enghild J.J., Potempa J.;
RT "Equine leukocyte elastase inhibitor. Primary structure and identification
RT as a thymosin-binding protein.";
RL J. Biol. Chem. 267:6576-6583(1992).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=2261438; DOI=10.1021/bi00486a006;
RA Zarbock J., Oschkinat H., Hannappel E., Kalbacher H., Voelter W.,
RA Holak T.A.;
RT "Solution conformation of thymosin beta 4: a nuclear magnetic resonance and
RT simulated annealing study.";
RL Biochemistry 29:7814-7821(1990).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=8269922; DOI=10.1111/j.1432-1033.1993.tb18382.x;
RA Czisch M., Schleicher M., Hoerger S., Voelter W., Holak T.A.;
RT "Conformation of thymosin beta 4 in water determined by NMR spectroscopy.";
RL Eur. J. Biochem. 218:335-344(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.
CC {ECO:0000250|UniProtKB:P62328}.
CC -!- FUNCTION: [Hemoregulatory peptide AcSDKP]: Potent inhibitor of bone
CC marrow derived stem cell differentiation (PubMed:2915977). Acts by
CC inhibits the entry of hematopoietic pluripotent stem cells into the S-
CC phase (PubMed:2915977). {ECO:0000269|PubMed:2915977}.
CC -!- SUBUNIT: Identified in a complex composed of ACTA1, COBL, GSN AND
CC TMSB4X (By similarity). Interacts with SERPINB1 (PubMed:1551869).
CC {ECO:0000250|UniProtKB:P62328, ECO:0000269|PubMed:1551869}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P62328}.
CC -!- PTM: [Hemoregulatory peptide AcSDKP]: AcSDKP is inactivated by ACE,
CC which removes the dipeptide Lys-Pro from its C-terminus.
CC {ECO:0000250|UniProtKB:P62328}.
CC -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY911377; AAW82140.1; -; mRNA.
DR EMBL; BC133478; AAI33479.1; -; mRNA.
DR PIR; A01521; TNBOB4.
DR RefSeq; NP_001106702.1; NM_001113231.1.
DR PDB; 3SJH; X-ray; 1.75 A; B=18-44.
DR PDB; 3U8X; X-ray; 2.00 A; B/D=18-44.
DR PDB; 3U9D; X-ray; 2.50 A; B/D=13-44.
DR PDBsum; 3SJH; -.
DR PDBsum; 3U8X; -.
DR PDBsum; 3U9D; -.
DR AlphaFoldDB; P62326; -.
DR BMRB; P62326; -.
DR SMR; P62326; -.
DR STRING; 9913.ENSBTAP00000024387; -.
DR iPTMnet; P62326; -.
DR PaxDb; P62326; -.
DR PeptideAtlas; P62326; -.
DR PRIDE; P62326; -.
DR GeneID; 781334; -.
DR CTD; 781334; -.
DR eggNOG; KOG4794; Eukaryota.
DR HOGENOM; CLU_208046_0_0_1; -.
DR InParanoid; P62326; -.
DR OrthoDB; 1632292at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:CAFA.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0003785; F:actin monomer binding; IDA:CAFA.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:CAFA.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; IDA:UniProtKB.
DR GO; GO:1902037; P:negative regulation of hematopoietic stem cell differentiation; IDA:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:CAFA.
DR GO; GO:0090024; P:negative regulation of neutrophil chemotaxis; IMP:CAFA.
DR GO; GO:1902624; P:positive regulation of neutrophil migration; IMP:CAFA.
DR GO; GO:0090303; P:positive regulation of wound healing; IMP:CAFA.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0042989; P:sequestering of actin monomers; IDA:CAFA.
DR DisProt; DP00795; -.
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; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6940133"
FT CHAIN 2..44
FT /note="Thymosin beta-4"
FT /evidence="ECO:0000269|PubMed:6940133"
FT /id="PRO_0000045917"
FT PEPTIDE 2..5
FT /note="Hemoregulatory peptide AcSDKP"
FT /evidence="ECO:0000305|PubMed:2253778"
FT /id="PRO_0000034292"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6940133"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 12
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 23
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 26
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 32
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT CROSSLNK 12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3U9D"
SQ SEQUENCE 44 AA; 5053 MW; 440C6158482DAAD0 CRC64;
MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES
