ID   TYB10_PIG               Reviewed;          42 AA.
AC   P21753; A1XQV2;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Thymosin beta-10;
DE   AltName: Full=Thymosin beta-9;
GN   Name=TMSB10;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Longissimus dorsi muscle;
RA   Cai G., Chen Y., Wang C., Li J., Peng G., Zhang H.;
RT   "Generation and analysis of cDNA sequences derived from a porcine skeletal
RT   muscle library.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-42.
RC   TISSUE=Spleen;
RX   PubMed=2774558; DOI=10.1016/0003-9861(89)90498-0;
RA   Hannappel E., Wartenberg F., Bustelo X.R.;
RT   "Isolation and characterization of thymosin beta 9 Met from pork spleen.";
RL   Arch. Biochem. Biophys. 273:396-402(1989).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-42.
RC   TISSUE=Thymus;
RX   PubMed=2090639; DOI=10.1111/j.1399-3011.1990.tb00986.x;
RA   Low T.L.K., Lin C.Y., Pan T.L., Chiou A.J., Tsugita A.;
RT   "Structure and immunological properties of thymosin beta 9 Met, a new
RT   analog of thymosin beta 4 isolated from porcine thymus.";
RL   Int. J. Pept. Protein Res. 36:481-488(1990).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
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DR   EMBL; DQ629174; ABK55658.1; -; mRNA.
DR   PIR; A60290; A60290.
DR   RefSeq; NP_001090951.1; NM_001097482.1.
DR   AlphaFoldDB; P21753; -.
DR   BMRB; P21753; -.
DR   SMR; P21753; -.
DR   STRING; 9823.ENSSSCP00000008804; -.
DR   PaxDb; P21753; -.
DR   PeptideAtlas; P21753; -.
DR   PRIDE; P21753; -.
DR   Ensembl; ENSSSCT00005041293; ENSSSCP00005025246; ENSSSCG00005026094.
DR   Ensembl; ENSSSCT00025094980; ENSSSCP00025041699; ENSSSCG00025069121.
DR   Ensembl; ENSSSCT00030014560; ENSSSCP00030006543; ENSSSCG00030010611.
DR   Ensembl; ENSSSCT00035002863; ENSSSCP00035000971; ENSSSCG00035002288.
DR   Ensembl; ENSSSCT00045055044; ENSSSCP00045038367; ENSSSCG00045032257.
DR   Ensembl; ENSSSCT00050035231; ENSSSCP00050014655; ENSSSCG00050026180.
DR   Ensembl; ENSSSCT00055049136; ENSSSCP00055039238; ENSSSCG00055024901.
DR   Ensembl; ENSSSCT00065065110; ENSSSCP00065028219; ENSSSCG00065047592.
DR   Ensembl; ENSSSCT00065065857; ENSSSCP00065028528; ENSSSCG00065048143.
DR   Ensembl; ENSSSCT00070058366; ENSSSCP00070049631; ENSSSCG00070029092.
DR   GeneID; 100037998; -.
DR   KEGG; ssc:100037998; -.
DR   CTD; 9168; -.
DR   eggNOG; KOG4794; Eukaryota.
DR   HOGENOM; CLU_208046_0_1_1; -.
DR   InParanoid; P21753; -.
DR   OrthoDB; 1632292at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 3.
DR   Genevisible; P21753; SS.
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: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; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P21752,
FT                   ECO:0000269|PubMed:2090639, ECO:0000269|PubMed:2774558"
FT   CHAIN           2..42
FT                   /note="Thymosin beta-10"
FT                   /id="PRO_0000045929"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P21752"
FT   MOD_RES         4
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P63313"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P63313"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P63313"
FT   MOD_RES         21
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ZWY8"
FT   MOD_RES         23
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P63313"
FT   MOD_RES         34
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P63313"
FT   MOD_RES         39
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P63313"
SQ   SEQUENCE   42 AA;  4823 MW;  26D4D58A1C703909 CRC64;
     MADKPDMGEI NSFDKAKLKK TETQEKNTLP TKETIEQEKQ AK