TYB_CAEEL
ID TYB_CAEEL Reviewed; 151 AA.
AC O17389;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Thymosin beta {ECO:0000305};
DE AltName: Full=Tetrathymosin beta {ECO:0000303|PubMed:15269284};
GN Name=tth-1 {ECO:0000312|WormBase:F08F1.8};
GN ORFNames=F08F1.8 {ECO:0000312|WormBase:F08F1.8};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH G-ACTIN AND F-ACTIN, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DOMAIN, DISRUPTION PHENOTYPE,
RP REPEAT, AND MUTAGENESIS OF 24-LEU--VAL-27; 62-LEU--THR-65; 100-LEU--THR-103
RP AND 134-LEU--VAL-137.
RX PubMed=15269284; DOI=10.1091/mbc.e04-03-0225;
RA Van Troys M., Ono K., Dewitte D., Jonckheere V., De Ruyck N.,
RA Vandekerckhove J., Ono S., Ampe C.;
RT "TetraThymosinbeta is required for actin dynamics in Caenorhabditis elegans
RT and acts via functionally different actin-binding repeats.";
RL Mol. Biol. Cell 15:4735-4748(2004).
CC -!- FUNCTION: Plays an important role in the organization of the
CC cytoskeleton by regulating actin polymerization in two ways. Firstly,
CC by binding to and sequestering actin monomers (G actin) inhibits actin
CC polymerization. Secondly, by binding directly filamentous actin (F
CC actin) promotes actin polymerization. Regulates the formation of
CC cortical actin in oocytes conferring them enough rigidity to sustain
CC the contractions during ovulation. {ECO:0000269|PubMed:15269284}.
CC -!- SUBUNIT: Interacts (via repeats 1, 2 and 4) with G-actin in a 1:3
CC ratio. Interacts (via repeats 2 and 3) with F-actin.
CC {ECO:0000269|PubMed:15269284}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:15269284}. Cytoplasm {ECO:0000269|PubMed:15269284}.
CC Cell junction {ECO:0000269|PubMed:15269284}. Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:15269284}. Note=Localizes to the cell cortex and
CC the cytoplasm in oocytes and at the inside edges of membrane cubicles
CC surrounding germ cell nuclei. Co-localizes with actin at the cell-cell
CC contact in two-cell stage embryo. {ECO:0000269|PubMed:15269284}.
CC -!- TISSUE SPECIFICITY: At the comma stage, enriched in the developing
CC nerve ring (at protein level). Ubiquitously expressed in larvae and
CC adults with enrichment in the spermatheca, the intestinal tract and the
CC posterior bulb of the pharynx (at protein level). Expressed in oocytes
CC and in the gonad (at protein level). {ECO:0000269|PubMed:15269284}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo, larvae and adults (at protein
CC level). {ECO:0000269|PubMed:15269284}.
CC -!- DOMAIN: The 4 repeats act cooperatively in the binding of G actin.
CC {ECO:0000269|PubMed:15269284}.
CC -!- DISRUPTION PHENOTYPE: Lethal at the L3/L4 larval stages or at the young
CC adult stage. Mutants are shorter and stouter, and fail to produce a
CC viable progeny. In oocytes, actin is diffused in the cytoplasm and F-
CC actin accumulation at the cell cortex is reduced resulting in deformed
CC oocytes in the spermatheca and the uterus.
CC {ECO:0000269|PubMed:15269284}.
CC -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
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DR EMBL; BX284606; CCD69031.1; -; Genomic_DNA.
DR PIR; T32473; T32473.
DR RefSeq; NP_509430.1; NM_077029.4.
DR AlphaFoldDB; O17389; -.
DR SMR; O17389; -.
DR STRING; 6239.F08F1.8; -.
DR EPD; O17389; -.
DR PaxDb; O17389; -.
DR PeptideAtlas; O17389; -.
DR EnsemblMetazoa; F08F1.8.1; F08F1.8.1; WBGene00006649.
DR EnsemblMetazoa; F08F1.8.2; F08F1.8.2; WBGene00006649.
DR GeneID; 181097; -.
DR KEGG; cel:CELE_F08F1.8; -.
DR UCSC; F08F1.8.1; c. elegans.
DR CTD; 181097; -.
DR WormBase; F08F1.8; CE27929; WBGene00006649; tth-1.
DR eggNOG; KOG4794; Eukaryota.
DR GeneTree; ENSGT00940000170493; -.
DR HOGENOM; CLU_117354_0_0_1; -.
DR InParanoid; O17389; -.
DR OMA; DQLKHAD; -.
DR OrthoDB; 1318270at2759; -.
DR PhylomeDB; O17389; -.
DR PRO; PR:O17389; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006649; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR Gene3D; 1.20.5.520; -; 3.
DR InterPro; IPR001152; Beta-thymosin.
DR InterPro; IPR038386; Beta-thymosin_sf.
DR Pfam; PF01290; Thymosin; 3.
DR SMART; SM00152; THY; 3.
PE 1: Evidence at protein level;
KW Actin-binding; Cell junction; Cytoplasm; Cytoskeleton; Reference proteome;
KW Repeat.
FT CHAIN 1..151
FT /note="Thymosin beta"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437691"
FT REPEAT 24..29
FT /note="1"
FT /evidence="ECO:0000269|PubMed:15269284"
FT REPEAT 62..67
FT /note="2"
FT /evidence="ECO:0000269|PubMed:15269284"
FT REPEAT 100..105
FT /note="3"
FT /evidence="ECO:0000269|PubMed:15269284"
FT REPEAT 134..139
FT /note="4"
FT /evidence="ECO:0000269|PubMed:15269284"
FT REGION 24..139
FT /note="4 X 6 AA repeat of L-[KH]-[KSH]-[VT]-[EP]-[TV]"
FT /evidence="ECO:0000269|PubMed:15269284"
FT MUTAGEN 24..27
FT /note="LKKV->AAAA: Moderate reduction in actin
FT polymerization inhibition. Complete loss of actin
FT sequestering activity and moderate reduction in actin
FT polymerization inhibition; when associated with 100-A--A-
FT 103 and 134-A--A-137. Complete loss of actin sequestering
FT activity and severe reduction in actin polymerization
FT inhibition; when associated with 62-A--A-65 and 134-A--A-
FT 137. Moderate loss of actin sequestering activity and
FT moderate reduction in actin polymerization inhibition; when
FT associated with 62-A--A-65 and 100-A--A-103."
FT /evidence="ECO:0000269|PubMed:15269284"
FT MUTAGEN 62..65
FT /note="LHST->AAAA: Severe reduction in actin polymerization
FT inhibition. Complete loss of actin sequestering activity
FT and severe reduction in actin polymerization inhibition;
FT when associated with 24-A--A-27 and 134-A--A-137. Severe
FT loss of actin sequestering activity and moderate reduction
FT in actin polymerization inhibition; when associated with
FT 100-A--A-103 and 134-A--A-137. Moderate loss of actin
FT sequestering activity and slight reduction in actin
FT polymerization inhibition; when associate d with 24-A--A-27
FT and 100-A--A-103."
FT /evidence="ECO:0000269|PubMed:15269284"
FT MUTAGEN 100..103
FT /note="LKKT->AAAA: Moderate reduction in actin
FT polymerization inhibition. Complete loss of actin
FT sequestering activity and severe reduction in actin
FT polymerization inhibition; when associated with 24-A--A-27
FT and 134-A--A-137. Severe loss of actin sequestering
FT activity and moderate reduction in actin polymerization
FT inhibition; when associated with 62-A--A-65 and 134-A--A-
FT 137. Moderate loss of actin sequestering activity and
FT slight reduction in actin polymerization inhibition; when
FT associated with 24-A--A-27 and 62-A--A-65."
FT /evidence="ECO:0000269|PubMed:15269284"
FT MUTAGEN 134..137
FT /note="LHHV->AAAA: Slight reduction in actin polymerization
FT inhibition. Complete loss of actin sequestering activity
FT and severe reduction in actin polymerization inhibition;
FT when associated with 24-A--A-27 and 62-A--A-65. Complete
FT loss of actin sequestering activity and moderate reduction
FT in actin polymerization inhibition; when associated with
FT 24-A--A-27 and 100-A--A-137. Severe loss of actin
FT sequestering activity and moderate reduction in actin
FT polymerization inhibition; when associated with 62-A--A-65
FT and 100-A--A-103."
FT /evidence="ECO:0000269|PubMed:15269284"
SQ SEQUENCE 151 AA; 17041 MW; 3F9583CF0F9C8095 CRC64;
MAAVTELPKM NQELAGAVRE GLELKKVETT EKNVLPTKED VAEEKQHVER IHEIEHFDST
KLHSTPVKEK IVLPSADDIK QEKQHLELTD KINNFPSENL KKTETIEKNV LPSPTDVARE
KTLQMAASFD KSALHHVETI VSTDVRVTEA Q
