ID   TYB4_NOTEU              Reviewed;          44 AA.
AC   Q7YRC3;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 94.
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   Notamacropus eugenii (Tammar wallaby) (Macropus eugenii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX   NCBI_TaxID=9315;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15008146; DOI=10.1159/000076317;
RA   Waters P.D., Sankovic N., Kirby P.J., Delbridge M.L., Graves J.A.;
RT   "Assignment of the thymosin beta 4 X/Y chromosome (TMSB4X/Y) gene to tammar
RT   wallaby chromosome 5p by fluorescence in situ hybridisation.";
RL   Cytogenet. Genome Res. 103:203F-203F(2003).
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   -!- 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; AY341342; AAQ16584.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7YRC3; -.
DR   SMR; Q7YRC3; -.
DR   HOGENOM; CLU_208046_0_0_1; -.
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; 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_0000045922"
FT   PEPTIDE         2..5
FT                   /note="Hemoregulatory peptide AcSDKP"
FT                   /evidence="ECO:0000250|UniProtKB:P62326"
FT                   /id="PRO_0000034296"
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;  5037 MW;  A4F07C998DD7FFD0 CRC64;
     MSDKPDMGEI QKFNKSKLKK TETQEKNPLP SKETIEQEKQ AGES