TYB4_RAT
ID TYB4_RAT Reviewed; 44 AA.
AC P62329; P01253; P01254; Q0P5V6; Q63576;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Thymosin beta-4;
DE Short=T beta 4;
DE Contains:
DE RecName: Full=Hematopoietic system regulatory peptide;
DE AltName: Full=Seraspenide;
GN Name=Tmsb4x; Synonyms=Thyb4, Tmsb4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2325669; DOI=10.1210/mend-4-1-69;
RA Atkinson M.J., Freeman M.W., Kronenberg H.M.;
RT "Thymosin beta 4 is expressed in ROS 17/2.8 osteosarcoma cells in a
RT regulated manner.";
RL Mol. Endocrinol. 4:69-74(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=6201851; DOI=10.1073/pnas.81.8.2295;
RA Wodnar-Filipowicz A., Gubler U., Furuichi Y., Richardson M.,
RA Nowoswiat E.F., Poonian M.S., Horecker B.L.;
RT "Cloning and sequence analysis of cDNA for rat spleen thymosin beta 4.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2295-2297(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3838131; DOI=10.1016/0003-9861(85)90646-0;
RA Goodall G.J., Richardson M., Furuichi Y., Wodnar-Filippwicz A.,
RA Horecker B.L.;
RT "Sequence of a cloned 523-bp cDNA for thymosin beta 4.";
RL Arch. Biochem. Biophys. 236:445-447(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=6954532; DOI=10.1073/pnas.79.7.2172;
RA Hannappel E., Xu G.J., Morgan J., Hempstead J., Horecker B.L.;
RT "Thymosin beta 4: a ubiquitous peptide in rat and mouse tissues.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:2172-2175(1982).
RN [6]
RP INDUCTION.
RX PubMed=3670309; DOI=10.1128/mcb.7.9.3156-3167.1987;
RA Leonard D.G., Ziff E.B., Greene L.A.;
RT "Identification and characterization of mRNAs regulated by nerve growth
RT factor in PC12 cells.";
RL Mol. Cell. Biol. 7:3156-3167(1987).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-34, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- FUNCTION: Seraspenide inhibits the entry of hematopoietic pluripotent
CC stem cells into the S-phase. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SERPINB1. Identified in a complex composed of
CC ACTA1, COBL, GSN AND TMSB4X (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Originally found in thymus but it is widely
CC distributed in many tissues. {ECO:0000269|PubMed:6954532}.
CC -!- INDUCTION: By NGF and fibroblast growth factors.
CC {ECO:0000269|PubMed:3670309}.
CC -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA42246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M34043; AAA42062.1; -; mRNA.
DR EMBL; K01334; AAA42245.1; -; mRNA.
DR EMBL; M26759; AAA42246.1; ALT_INIT; mRNA.
DR EMBL; BC058137; AAH58137.1; -; mRNA.
DR PIR; A01522; TNRTB4.
DR PIR; I52084; I52084.
DR RefSeq; NP_112398.1; NM_031136.1.
DR AlphaFoldDB; P62329; -.
DR SMR; P62329; -.
DR STRING; 10116.ENSRNOP00000066062; -.
DR iPTMnet; P62329; -.
DR PhosphoSitePlus; P62329; -.
DR PaxDb; P62329; -.
DR PRIDE; P62329; -.
DR GeneID; 81814; -.
DR KEGG; rno:81814; -.
DR CTD; 7114; -.
DR RGD; 621622; Tmsb4x.
DR VEuPathDB; HostDB:ENSRNOG00000047931; -.
DR eggNOG; KOG4794; Eukaryota.
DR HOGENOM; CLU_208046_0_0_1; -.
DR InParanoid; P62329; -.
DR OrthoDB; 1632292at2759; -.
DR PhylomeDB; P62329; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR PRO; PR:P62329; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000047931; Expressed in thymus and 20 other tissues.
DR Genevisible; P62329; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003785; F:actin monomer binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; ISO:RGD.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; ISO:RGD.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:RGD.
DR GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; IEP:RGD.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISO:RGD.
DR GO; GO:1905273; P:positive regulation of proton-transporting ATP synthase activity, rotational mechanism; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0042989; P:sequestering of actin monomers; ISO:RGD.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:RGD.
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; 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_0000045927"
FT PEPTIDE 2..5
FT /note="Hematopoietic system regulatory peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000034301"
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:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
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 8
FT /note="A -> V (in Ref. 2; AAA42245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 44 AA; 5053 MW; 440C6158482DAAD0 CRC64;
MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES
