TYB4_HORSE
ID TYB4_HORSE Reviewed; 44 AA.
AC P62327; P01253; P01254; Q63576; Q6X9X4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
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; Synonyms=THYB4;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE OF 2-44.
RC TISSUE=Spleen;
RA Hoerger S., Gallert B., Kellerman J., Voelter W.;
RT "Isolation and structural identification of beta-thymosins from equine
RT tissue: development of a specific ELISA against thymosin beta-10 (TBeta-
RT 10).";
RL (In) Schneider C.H., Eberles A.N. (eds.);
RL Peptides 1992, pp.749-750, Escom Science Publishers, Leiden (1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-44.
RA Takafuji V.A., Crisman M.V., Seat K.L., Sharova L.V., Ward D.L.,
RA Howard R.D.;
RT "Expression analysis of equine interleukin-1b treated equine synovium using
RT suppression subtractive hybridization analysis (SSH-PCR).";
RL Submitted (FEB-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 -!- 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; AY246744; AAP78720.1; -; mRNA.
DR RefSeq; NP_001157420.1; NM_001163948.1.
DR AlphaFoldDB; P62327; -.
DR BMRB; P62327; -.
DR SMR; P62327; -.
DR STRING; 9796.ENSECAP00000007110; -.
DR PaxDb; P62327; -.
DR PeptideAtlas; P62327; -.
DR PRIDE; P62327; -.
DR GeneID; 100034015; -.
DR KEGG; ecb:100034015; -.
DR CTD; 7114; -.
DR HOGENOM; CLU_208046_0_0_1; -.
DR InParanoid; P62327; -.
DR OrthoDB; 1632292at2759; -.
DR Proteomes; UP000002281; Unplaced.
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: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 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 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|Ref.1"
FT CHAIN 2..44
FT /note="Thymosin beta-4"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000045919"
FT PEPTIDE 2..5
FT /note="Hemoregulatory peptide AcSDKP"
FT /evidence="ECO:0000250|UniProtKB:P62326"
FT /id="PRO_0000034294"
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
