ID   TYB4_CHILA              Reviewed;          44 AA.
AC   Q6S9C5;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Thymosin beta-4;
DE            Short=T beta-4;
DE   Contains:
DE     RecName: Full=Hemoregulatory peptide AcSDKP {ECO:0000305};
DE     AltName: Full=N-acetyl-SDKP;
DE              Short=AcSDKP;
DE     AltName: Full=Seraspenide {ECO:0000250|UniProtKB:P62328};
GN   Name=TMSB4;
OS   Chinchilla lanigera (Long-tailed chinchilla) (Chinchilla villidera).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha;
OC   Chinchillidae; Chinchilla.
OX   NCBI_TaxID=34839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Middle ear mucosa;
RA   Erdos G., Hu F.Z., Donfack J., Ahmed A.I., Preston R.A., Hayes J.D.,
RA   Post J.C., Ehrlich G.D.;
RT   "The thymosin beta-4 gene is expressed in chinchilla middle ear mucosa.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Acts by
CC       inhibits the entry of hematopoietic pluripotent stem cells into the S-
CC       phase (By similarity). {ECO:0000250|UniProtKB:P62326,
CC       ECO:0000250|UniProtKB:P62328}.
CC   -!- SUBUNIT: Identified in a complex composed of ACTA1, COBL, GSN AND
CC       TMSB4X (By similarity). Interacts with SERPINB1 (By similarity).
CC       {ECO:0000250|UniProtKB:P62326, ECO:0000250|UniProtKB:P62328}.
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}.
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DR   EMBL; AY462140; AAR26539.1; -; mRNA.
DR   RefSeq; XP_013363643.1; XM_013508189.1.
DR   AlphaFoldDB; Q6S9C5; -.
DR   SMR; Q6S9C5; -.
DR   PRIDE; Q6S9C5; -.
DR   Ensembl; ENSCLAT00000000365; ENSCLAP00000000337; ENSCLAG00000000289.
DR   GeneID; 106147335; -.
DR   CTD; 7114; -.
DR   GeneTree; ENSGT00940000154433; -.
DR   OrthoDB; 1632292at2759; -.
DR   Proteomes; UP000694398; Unassembled WGS sequence.
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   GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR   GO; GO:1902037; P:negative regulation of hematopoietic stem cell differentiation; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62326"
FT   CHAIN           2..44
FT                   /note="Thymosin beta-4"
FT                   /id="PRO_0000045918"
FT   PEPTIDE         2..5
FT                   /note="Hemoregulatory peptide AcSDKP"
FT                   /evidence="ECO:0000250|UniProtKB:P62326"
FT                   /id="PRO_0000034293"
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:0000250|UniProtKB:P62326"
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"
SQ   SEQUENCE   44 AA;  5053 MW;  440C6158482DAAD0 CRC64;
     MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES