ID   TYB4_PONAB              Reviewed;          44 AA.
AC   Q5R7H8; Q5R849;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 105.
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=TMSB4X;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, and Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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   -!- 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}.
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; CR859905; CAH92061.1; ALT_TERM; mRNA.
DR   EMBL; CR860138; CAH92282.1; -; mRNA.
DR   RefSeq; NP_001126333.1; NM_001132861.1.
DR   RefSeq; XP_009232863.1; XM_009234588.1.
DR   AlphaFoldDB; Q5R7H8; -.
DR   SMR; Q5R7H8; -.
DR   STRING; 9601.ENSPPYP00000022513; -.
DR   GeneID; 100173314; -.
DR   KEGG; pon:100173314; -.
DR   CTD; 7114; -.
DR   eggNOG; KOG4794; Eukaryota.
DR   HOGENOM; CLU_208046_0_0_1; -.
DR   InParanoid; Q5R7H8; -.
DR   OrthoDB; 1632292at2759; -.
DR   Proteomes; UP000001595; Chromosome X.
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_0000045925"
FT   PEPTIDE         2..5
FT                   /note="Hemoregulatory peptide AcSDKP"
FT                   /evidence="ECO:0000250|UniProtKB:P62326"
FT                   /id="PRO_0000034299"
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"
FT   CONFLICT        38
FT                   /note="Missing (in Ref. 1; CAH92061)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   44 AA;  5053 MW;  440C6158482DAAD0 CRC64;
     MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES