TYB4_MOUSE
ID TYB4_MOUSE Reviewed; 50 AA.
AC P20065;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Thymosin beta-4 {ECO:0000303|PubMed:2351831};
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; Synonyms=Ptmb4, Tmsb4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND TISSUE SPECIFICITY.
RX PubMed=2351831;
RA Rudin C.M., Engler P., Storb U.;
RT "Differential splicing of thymosin beta 4 mRNA.";
RL J. Immunol. 144:4857-4862(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM SHORT).
RX PubMed=2226839; DOI=10.1016/0014-5793(90)81037-o;
RA Low T.L.K., Pan T.L., Lin Y.S.;
RT "Depression of prothymosin alpha production in murine thymus correlates
RT with staphylococcal enterotoxin-B-induced immunosuppression.";
RL FEBS Lett. 273:1-5(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT).
RC STRAIN=129/Sv;
RX PubMed=8838802; DOI=10.1006/geno.1996.0133;
RA Li X., Zimmerman A., Copeland N.G., Gilbert D.J., Jenkins N.A., Yin H.L.;
RT "The mouse thymosin beta 4 gene: structure, promoter identification, and
RT chromosome localization.";
RL Genomics 32:388-394(1996).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP DEGRADATION (HEMOREGULATORY PEPTIDE ACSDKP).
RX PubMed=11303049;
RA Junot C., Gonzales M.F., Ezan E., Cotton J., Vazeux G., Michaud A.,
RA Azizi M., Vassiliou S., Yiotakis A., Corvol P., Dive V.;
RT "RXP 407, a selective inhibitor of the N-domain of angiotensin I-converting
RT enzyme, blocks in vivo the degradation of hemoregulatory peptide acetyl-
RT Ser-Asp-Lys-Pro with no effect on angiotensin I hydrolysis.";
RL J. Pharmacol. Exp. Ther. 297:606-611(2001).
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 -!- INTERACTION:
CC P20065; Q8WWQ8: STAB2; Xeno; NbExp=3; IntAct=EBI-7946048, EBI-7945957;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P62328}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P20065-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P20065-2; Sequence=VSP_006424;
CC -!- TISSUE SPECIFICITY: Originally found in thymus but it is widely
CC distributed in many tissues. {ECO:0000269|PubMed:2351831}.
CC -!- PTM: [Hemoregulatory peptide AcSDKP]: AcSDKP is inactivated by ACE,
CC which removes the dipeptide Lys-Pro from its C-terminus.
CC {ECO:0000269|PubMed:11303049}.
CC -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
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DR EMBL; X16053; CAA34187.1; -; mRNA.
DR EMBL; X16053; CAA34188.1; -; mRNA.
DR EMBL; U38967; AAC52490.1; -; Genomic_DNA.
DR CCDS; CCDS30529.1; -. [P20065-2]
DR PIR; A37217; A37217.
DR RefSeq; NP_067253.1; NM_021278.2. [P20065-2]
DR RefSeq; XP_006528822.1; XM_006528759.1. [P20065-2]
DR PDB; 1T44; X-ray; 2.00 A; G=28-46.
DR PDB; 3M3N; X-ray; 7.00 A; W=26-50.
DR PDBsum; 1T44; -.
DR PDBsum; 3M3N; -.
DR AlphaFoldDB; P20065; -.
DR BMRB; P20065; -.
DR SMR; P20065; -.
DR BioGRID; 202471; 18.
DR CORUM; P20065; -.
DR ELM; P20065; -.
DR IntAct; P20065; 3.
DR MINT; P20065; -.
DR STRING; 10090.ENSMUSP00000107795; -.
DR iPTMnet; P20065; -.
DR PhosphoSitePlus; P20065; -.
DR EPD; P20065; -.
DR jPOST; P20065; -.
DR MaxQB; P20065; -.
DR PaxDb; P20065; -.
DR PeptideAtlas; P20065; -.
DR PRIDE; P20065; -.
DR ProteomicsDB; 297761; -. [P20065-1]
DR ProteomicsDB; 297762; -. [P20065-2]
DR Antibodypedia; 8508; 279 antibodies from 28 providers.
DR DNASU; 19241; -.
DR Ensembl; ENSMUST00000112172; ENSMUSP00000107795; ENSMUSG00000049775. [P20065-2]
DR Ensembl; ENSMUST00000112175; ENSMUSP00000107797; ENSMUSG00000049775. [P20065-1]
DR Ensembl; ENSMUST00000112176; ENSMUSP00000107798; ENSMUSG00000049775. [P20065-1]
DR GeneID; 19241; -.
DR KEGG; mmu:19241; -.
DR UCSC; uc009uwx.1; mouse. [P20065-1]
DR CTD; 7114; -.
DR MGI; MGI:99510; Tmsb4x.
DR VEuPathDB; HostDB:ENSMUSG00000049775; -.
DR eggNOG; KOG4794; Eukaryota.
DR GeneTree; ENSGT00940000154433; -.
DR HOGENOM; CLU_208046_0_0_1; -.
DR InParanoid; P20065; -.
DR OMA; WLRFPSA; -.
DR PhylomeDB; P20065; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 19241; 2 hits in 66 CRISPR screens.
DR ChiTaRS; Tmsb4x; mouse.
DR EvolutionaryTrace; P20065; -.
DR PRO; PR:P20065; -.
DR Proteomes; UP000000589; Chromosome X.
DR Bgee; ENSMUSG00000049775; Expressed in left lung lobe and 293 other tissues.
DR ExpressionAtlas; P20065; baseline and differential.
DR Genevisible; P20065; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003785; F:actin monomer binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
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:0051152; P:positive regulation of smooth muscle cell differentiation; TAS:DFLAT.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; TAS:DFLAT.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:DFLAT.
DR GO; GO:0030334; P:regulation of cell migration; IDA:MGI.
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 3D-structure; Acetylation; Actin-binding; Alternative splicing; Cytoplasm;
KW Cytoskeleton; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..50
FT /note="Thymosin beta-4"
FT /id="PRO_0000045923"
FT PEPTIDE 8..11
FT /note="Hemoregulatory peptide AcSDKP"
FT /evidence="ECO:0000305|PubMed:11303049"
FT /id="PRO_0000034297"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 18
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 29
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 32
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 38
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 40
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT MOD_RES 45
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62328"
FT VAR_SEQ 1..6
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_006424"
SQ SEQUENCE 50 AA; 5679 MW; 9A289F60EE48EB8A CRC64;
MLLPATMSDK PDMAEIEKFD KSKLKKTETQ EKNPLPSKET IEQEKQAGES
