TYB4_RABIT
ID TYB4_RABIT Reviewed; 44 AA.
AC P34032;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 91.
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=TMSB4;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE OF 2-44, AND ACETYLATION AT ALA-2.
RX PubMed=6838210; DOI=10.1016/0003-9861(83)90177-7;
RA Erickson-Viitanen S., Ruggieri S., Natalini P., Horecker B.L.;
RT "Distribution of thymosin beta 4 in vertebrate classes.";
RL Arch. Biochem. Biophys. 221:570-576(1983).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Originally found in thymus but it is widely
CC distributed in many tissues.
CC -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
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DR AlphaFoldDB; P34032; -.
DR BMRB; P34032; -.
DR SMR; P34032; -.
DR iPTMnet; P34032; -.
DR InParanoid; P34032; -.
DR Proteomes; UP000001811; Unplaced.
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; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6838210"
FT CHAIN 2..44
FT /note="Thymosin beta-4"
FT /id="PRO_0000045926"
FT PEPTIDE 2..5
FT /note="Hematopoietic system regulatory peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000034300"
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:0000269|PubMed:6838210"
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:0000250|UniProtKB:P62328"
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"
SQ SEQUENCE 44 AA; 5037 MW; 440C76EE9357AAD0 CRC64;
MADKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES
