TYB4_PIG
ID TYB4_PIG Reviewed; 44 AA.
AC Q95274; Q2EN78;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Thymosin beta-4;
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=TMSB4;
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=Small intestine;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA
RT library.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Lee-Sung; TISSUE=Adipose tissue;
RX PubMed=16971568; DOI=10.2527/jas.2005-737;
RA Chen C.H., Lin E.C., Cheng W.T., Sun H.S., Mersmann H.J., Ding S.T.;
RT "Abundantly expressed genes in pig adipose tissue: an expressed sequence
RT tag approach.";
RL J. Anim. Sci. 84:2673-2683(2006).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P62328}.
CC -!- PTM: [Hemoregulatory peptide AcSDKP]: AcSDKP is inactivated by ACE,
CC which removes the dipeptide Lys-Pro from its C-terminus.
CC {ECO:0000250|UniProtKB:P62328}.
CC -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB03562.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z81195; CAB03562.1; ALT_INIT; mRNA.
DR EMBL; DQ372079; ABD18454.1; -; mRNA.
DR RefSeq; NP_001038020.1; NM_001044555.1.
DR RefSeq; NP_001135463.1; NM_001141991.1.
DR RefSeq; XP_005673463.1; XM_005673406.1.
DR AlphaFoldDB; Q95274; -.
DR SMR; Q95274; -.
DR STRING; 9823.ENSSSCP00000012901; -.
DR PaxDb; Q95274; -.
DR PeptideAtlas; Q95274; -.
DR PRIDE; Q95274; -.
DR Ensembl; ENSSSCT00000035781; ENSSSCP00000028545; ENSSSCG00000012119.
DR Ensembl; ENSSSCT00015093655; ENSSSCP00015038365; ENSSSCG00015069888.
DR Ensembl; ENSSSCT00025001905; ENSSSCP00025000601; ENSSSCG00025001517.
DR Ensembl; ENSSSCT00030087269; ENSSSCP00030040291; ENSSSCG00030062389.
DR Ensembl; ENSSSCT00035003739; ENSSSCP00035001271; ENSSSCG00035003010.
DR Ensembl; ENSSSCT00040031990; ENSSSCP00040013275; ENSSSCG00040023885.
DR Ensembl; ENSSSCT00045040755; ENSSSCP00045028337; ENSSSCG00045023876.
DR Ensembl; ENSSSCT00050023573; ENSSSCP00050009931; ENSSSCG00050017316.
DR Ensembl; ENSSSCT00055051639; ENSSSCP00055041265; ENSSSCG00055026150.
DR Ensembl; ENSSSCT00060069647; ENSSSCP00060030002; ENSSSCG00060051180.
DR Ensembl; ENSSSCT00065070249; ENSSSCP00065030615; ENSSSCG00065051287.
DR Ensembl; ENSSSCT00070010343; ENSSSCP00070008488; ENSSSCG00070005462.
DR Ensembl; ENSSSCT00070010352; ENSSSCP00070008497; ENSSSCG00070005462.
DR GeneID; 733606; -.
DR KEGG; ssc:733606; -.
DR CTD; 7114; -.
DR eggNOG; KOG4794; Eukaryota.
DR GeneTree; ENSGT00940000154433; -.
DR HOGENOM; CLU_208046_0_0_1; -.
DR InParanoid; Q95274; -.
DR OrthoDB; 1632292at2759; -.
DR Reactome; R-SSC-114608; Platelet degranulation.
DR Proteomes; UP000008227; Chromosome X.
DR Proteomes; UP000314985; Unassembled WGS sequence.
DR Bgee; ENSSSCG00000012119; Expressed in blood and 45 other tissues.
DR ExpressionAtlas; Q95274; baseline and differential.
DR Genevisible; Q95274; SS.
DR GO; GO:0005737; C:cytoplasm; IDA:CACAO.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
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: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 3: Inferred from homology;
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_0000045924"
FT PEPTIDE 2..5
FT /note="Hemoregulatory peptide AcSDKP"
FT /evidence="ECO:0000250|UniProtKB:P62326"
FT /id="PRO_0000034298"
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:0000250|UniProtKB:P62328"
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"
FT UNSURE 2
SQ SEQUENCE 44 AA; 5053 MW; 440C6158482DAAD0 CRC64;
MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES
