TYB10_RAT
ID TYB10_RAT Reviewed; 44 AA.
AC P63312; P13472;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Thymosin beta-10;
GN Name=Tmsb10; Synonyms=Ptmb10, Thyb10;
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=3606131; DOI=10.1016/0003-9861(87)90461-9;
RA Goodall G.J., Horecker B.L.;
RT "Molecular cloning of the cDNA for rat spleen thymosin beta 10 and the
RT deduced amino acid sequence.";
RL Arch. Biochem. Biophys. 256:402-405(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1988550; DOI=10.1111/j.1471-4159.1991.tb08172.x;
RA Lugo D.I., Chen S.C., Hall A.K., Ziai R., Hempstead J.L., Morgan J.I.;
RT "Developmental regulation of beta-thymosins in the rat central nervous
RT system.";
RL J. Neurochem. 56:457-461(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=1744129; DOI=10.1016/s0021-9258(18)54503-8;
RA Lin S.-C., Morrison-Bogorad M.;
RT "Cloning and characterization of a testis-specific thymosin beta 10 cDNA.
RT Expression in post-meiotic male germ cells.";
RL J. Biol. Chem. 266:23347-23353(1991).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-34 AND SER-41, 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- DEVELOPMENTAL STAGE: Found to decrease dramatically after birth.
CC -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
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DR EMBL; M17698; AAA42244.1; -; mRNA.
DR EMBL; M58404; AAA42247.1; -; mRNA.
DR EMBL; M58405; AAA42248.1; -; mRNA.
DR PIR; A27266; A27266.
DR RefSeq; NP_067084.1; NM_021261.2.
DR RefSeq; XP_002726998.1; XM_002726952.5.
DR RefSeq; XP_006236754.1; XM_006236692.3.
DR RefSeq; XP_017450884.1; XM_017595395.1.
DR AlphaFoldDB; P63312; -.
DR SMR; P63312; -.
DR STRING; 10116.ENSRNOP00000051221; -.
DR iPTMnet; P63312; -.
DR PhosphoSitePlus; P63312; -.
DR PaxDb; P63312; -.
DR PRIDE; P63312; -.
DR GeneID; 100364435; -.
DR GeneID; 50665; -.
DR KEGG; rno:100364435; -.
DR KEGG; rno:50665; -.
DR UCSC; RGD:62022; rat.
DR CTD; 9168; -.
DR RGD; 62022; Tmsb10.
DR VEuPathDB; HostDB:ENSRNOG00000036921; -.
DR eggNOG; KOG4794; Eukaryota.
DR HOGENOM; CLU_208046_0_1_1; -.
DR InParanoid; P63312; -.
DR OrthoDB; 1632292at2759; -.
DR PhylomeDB; P63312; -.
DR PRO; PR:P63312; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000036921; Expressed in spleen and 5 other tissues.
DR Genevisible; P63312; RN.
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:0030036; P:actin cytoskeleton organization; TAS:RGD.
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 GO; GO:0007286; P:spermatid development; TAS:ProtInc.
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; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P21752"
FT CHAIN 2..44
FT /note="Thymosin beta-10"
FT /id="PRO_0000045933"
FT REGION 1..44
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:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63313"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 44 AA; 5026 MW; 5485277C275A1C70 CRC64;
MADKPDMGEI ASFDKAKLKK TETQEKNTLP TKETIEQEKR SEIS
