ID   TB15A_HUMAN             Reviewed;          45 AA.
AC   P0CG34; A8K614; Q99406;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   01-APR-2015, entry version 36.
DE   RecName: Full=Thymosin beta-15A;
DE   AltName: Full=NB thymosin beta;
DE   AltName: Full=Thymosin-like protein 8;
GN   Name=TMSB15A; Synonyms=TMSL8, TMSNB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=9039501; DOI=10.1093/dnares/3.5.311;
RA   Yokoyama M., Nishi Y., Yoshii J., Okubo K., Matsubara K.;
RT   "Identification and cloning of neuroblastoma-specific and nerve
RT   tissue-specific genes through compiled expression profiles.";
RL   DNA Res. 3:311-320(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-15.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [6]
RP   INDUCTION.
RX   PubMed=19296525; DOI=10.1002/gcc.20659;
RA   Banyard J., Barrows C., Zetter B.R.;
RT   "Differential regulation of human thymosin beta 15 isoforms by
RT   transforming growth factor beta 1.";
RL   Genes Chromosomes Cancer 48:502-509(2009).
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).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Neuroblastoma-specific.
CC       {ECO:0000269|PubMed:9039501}.
CC   -!- INDUCTION: Down-regulated by TGFB1. {ECO:0000269|PubMed:19296525}.
CC   -!- SIMILARITY: Belongs to the thymosin beta family. {ECO:0000305}.
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DR   EMBL; D82345; BAA11556.1; -; mRNA.
DR   EMBL; AL035609; CAC18959.1; -; Genomic_DNA.
DR   EMBL; CH471190; EAW54739.1; -; Genomic_DNA.
DR   EMBL; BC000183; AAH00183.1; -; mRNA.
DR   CCDS; CCDS14498.1; -.
DR   PIR; JC5274; JC5274.
DR   RefSeq; NP_068832.1; NM_021992.2.
DR   RefSeq; NP_919305.2; NM_194324.2.
DR   UniGene; Hs.56145; -.
DR   UniGene; Hs.675540; -.
DR   UniGene; Hs.709594; -.
DR   ProteinModelPortal; P0CG34; -.
DR   SMR; P0CG34; 2-42.
DR   DMDM; 300681171; -.
DR   MaxQB; P0CG34; -.
DR   PRIDE; P0CG34; -.
DR   Ensembl; ENST00000289373; ENSP00000289373; ENSG00000158164.
DR   GeneID; 11013; -.
DR   GeneID; 286527; -.
DR   KEGG; hsa:11013; -.
DR   KEGG; hsa:286527; -.
DR   UCSC; uc004eje.3; human.
DR   CTD; 11013; -.
DR   CTD; 286527; -.
DR   GeneCards; GC0XM101768; -.
DR   HGNC; HGNC:30744; TMSB15A.
DR   MIM; 300939; gene.
DR   neXtProt; NX_P0CG34; -.
DR   PharmGKB; PA164726584; -.
DR   InParanoid; P0CG34; -.
DR   OrthoDB; EOG761BZD; -.
DR   PhylomeDB; P0CG34; -.
DR   GeneWiki; TMSB15A; -.
DR   GeneWiki; TMSB15B; -.
DR   NextBio; 41837; -.
DR   PRO; PR:P0CG34; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; P0CG34; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR   GO; GO:0042989; P:sequestering of actin monomers; IEA:InterPro.
DR   Gene3D; 1.20.5.520; -; 1.
DR   InterPro; IPR001152; Beta-thymosin.
DR   InterPro; IPR016323; Thymosin_b4_metazoa.
DR   PANTHER; PTHR12021; PTHR12021; 1.
DR   Pfam; PF01290; Thymosin; 1.
DR   PIRSF; PIRSF001828; Thymosin_beta; 1.
DR   ProDom; PD005116; Thymosin_b4; 1.
DR   SMART; SM00152; THY; 1.
DR   PROSITE; PS00500; THYMOSIN_B4; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:12665801}.
FT   CHAIN         2     45       Thymosin beta-15A.
FT                                /FTId=PRO_0000185159.
SQ   SEQUENCE   45 AA;  5229 MW;  B1182868530D59C2 CRC64;
     MSDKPDLSEV EKFDRSKLKK TNTEEKNTLP SKETIQQEKE CVQTS
//