ID   TYB4_XENLA              Reviewed;          44 AA.
AC   P18758;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Thymosin beta-4;
DE            Short=T beta 4;
DE   AltName: Full=Thymosin beta 4Xen {ECO:0000303|PubMed:3124756};
GN   Name=tmsb4;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=1567461; DOI=10.1016/0006-291x(92)91162-j;
RA   Yamamoto M., Shoda A., Minamino N., Matsuo H., Nishimatsu S., Ueno N.,
RA   Murakami K.;
RT   "Expression of thymosin beta 4 gene during Xenopus laevis embryogenesis.";
RL   Biochem. Biophys. Res. Commun. 184:93-99(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-44, AND ACETYLATION AT SER-2.
RC   TISSUE=Oocyte;
RX   PubMed=3124756; DOI=10.1016/0003-9861(88)90480-8;
RA   Hannappel E., Kalbacher H., Voelter W.;
RT   "Thymosin beta 4Xen: a new thymosin beta 4-like peptide in oocytes of
RT   Xenopus laevis.";
RL   Arch. Biochem. Biophys. 260:546-551(1988).
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P62328}.
CC   -!- TISSUE SPECIFICITY: Spleen, kidney, heart, and oocytes.
CC       {ECO:0000269|PubMed:1567461}.
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; D10692; BAA01534.1; -; mRNA.
DR   PIR; JQ1489; JQ1489.
DR   RefSeq; NP_001084321.1; NM_001090852.2.
DR   RefSeq; XP_018105220.1; XM_018249731.1.
DR   AlphaFoldDB; P18758; -.
DR   SMR; P18758; -.
DR   iPTMnet; P18758; -.
DR   GeneID; 108709680; -.
DR   GeneID; 399438; -.
DR   KEGG; xla:108709680; -.
DR   KEGG; xla:399438; -.
DR   CTD; 399438; -.
DR   Xenbase; XB-GENE-6253898; tmsb4x.L.
DR   OrthoDB; 1632292at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 108709680; Expressed in lung and 19 other tissues.
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   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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3124756"
FT   CHAIN           2..44
FT                   /note="Thymosin beta-4"
FT                   /evidence="ECO:0000269|PubMed:3124756"
FT                   /id="PRO_0000045928"
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:3124756"
FT   CONFLICT        41..42
FT                   /note="TS -> ST (in Ref. 1; BAA01534)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   44 AA;  5097 MW;  440C7C842B0C98D0 CRC64;
     MSDKPDMAEI EKFDKAKLKK TETQEKNPLP SKETIEQEKQ TSES