ID   TYB_APLCA               Reviewed;          44 AA.
AC   Q8T697;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Thymosin beta;
DE   AltName: Full=Beta-thymosin;
OS   Aplysia californica (California sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neuron;
RX   PubMed=14561869; DOI=10.1523/jneurosci.23-28-09409.2003;
RA   Moccia R., Chen D., Lyles V., Kapuya E., Yaping E., Kalachikov S.,
RA   Spahn C.M.T., Frank J., Kandel E.R., Barad M., Martin K.C.;
RT   "An unbiased cDNA library prepared from isolated Aplysia sensory neuron
RT   processes is enriched for cytoskeletal and translational mRNAs.";
RL   J. Neurosci. 23:9409-9417(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=16237720; DOI=10.1002/jnr.20645;
RA   Colby G.P., Sung Y.J., Ambron R.T.;
RT   "mRNAs encoding the Aplysia homologues of fasciclin-I and beta-thymosin are
RT   expressed only in the second phase of nerve injury and are differentially
RT   segregated in axons regenerating in vitro and in vivo.";
RL   J. Neurosci. Res. 82:484-498(2005).
RN   [3]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, VARIANT GLN-27, AND
RP   ACETYLATION AT SER-2.
RC   TISSUE=CNS, and Hemolymph;
RX   PubMed=16924592; DOI=10.1002/jms.1060;
RA   Romanova E.V., Roth M.J., Rubakhin S.S., Jakubowski J.A., Kelley W.P.,
RA   Kirk M.D., Kelleher N.L., Sweedler J.V.;
RT   "Identification and characterization of homologues of vertebrate beta-
RT   thymosin in the marine mollusk Aplysia californica.";
RL   J. Mass Spectrom. 41:1030-1040(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 (By similarity). May be
CC       involved in the regulation of structural plasticity in the CNS.
CC       {ECO:0000250, ECO:0000269|PubMed:16924592}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in regenerating axons.
CC       {ECO:0000269|PubMed:16237720}.
CC   -!- MASS SPECTROMETRY: Mass=5009.54; Method=Electrospray; Note=Variant Gln-
CC       27.; Evidence={ECO:0000269|PubMed:16924592};
CC   -!- MASS SPECTROMETRY: Mass=5018.59; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16924592};
CC   -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF481063; AAM09681.1; -; mRNA.
DR   EMBL; AF454398; AAM22407.1; -; mRNA.
DR   RefSeq; NP_001191437.1; NM_001204508.1.
DR   AlphaFoldDB; Q8T697; -.
DR   SMR; Q8T697; -.
DR   iPTMnet; Q8T697; -.
DR   GeneID; 100533268; -.
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.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:16924592"
FT   CHAIN           2..44
FT                   /note="Thymosin beta"
FT                   /id="PRO_0000329074"
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:0000269|PubMed:16924592"
FT   VARIANT         27
FT                   /note="H -> Q"
FT                   /evidence="ECO:0000269|PubMed:16924592"
SQ   SEQUENCE   44 AA;  5111 MW;  6E68E270DAF79E5C CRC64;
     MSDKHDKPDI SEVTKFDKSK LKKTETHEKN PLPTKETIDQ EKQG