PLS3

Plastin 3
PDB rendering based on 1aoa.
Available structures PDB 1AOA, 1WJO
Identifiers
Symbols	PLS3; T-PLASTIN
External IDs	OMIM: 300131 MGI: 104807 HomoloGene: 68250 GeneCards: PLS3 Gene
Gene Ontology Molecular function • actin binding • calcium ion binding • protein binding Cellular component • cytoplasm Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5358	102866
Ensembl	ENSG00000102024	ENSMUSG00000016382
UniProt	P13797	Q3TUZ5
RefSeq (mRNA)	NM_001136025.3	XM_978781
RefSeq (protein)	NP_001129497.1	XP_983875
Location (UCSC)	Chr X: 114.8 – 114.89 Mb	Chr X: 73.03 – 73.12 Mb
PubMed search	[1]	[2]

Plastin-3 is a protein that in humans is encoded by the PLS3 gene.

Plastins are a family of actin-binding proteins that are conserved throughout eukaryote evolution and expressed in most tissues of higher eukaryotes. In humans, two ubiquitous plastin isoforms (L and T) have been identified. Plastin 1 (otherwise known as Fimbrin) is a third distinct plastin isoform which is specifically expressed at high levels in the small intestine. The L isoform is expressed only in hemopoietic cell lineages, while the T isoform has been found in all other normal cells of solid tissues that have replicative potential (fibroblasts, endothelial cells, epithelial cells, melanocytes, etc.). The C-terminal 570 amino acids of the T-plastin and L-plastin proteins are 83% identical. It contains a potential calcium-binding site near the N terminus.

Further reading

• Lin CS, Aebersold RH, Leavitt J (1990). "Correction of the N-terminal sequences of the human plastin isoforms by using anchored polymerase chain reaction: identification of a potential calcium-binding domain.". Mol. Cell. Biol. 10 (4): 1818–21. PMC 362293. PMID 2378651. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=362293. 
• Lin CS, Aebersold RH, Kent SB, et al. (1989). "Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts.". Mol. Cell. Biol. 8 (11): 4659–68. PMC 365555. PMID 3211125. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=365555. 
• Goldstein D, Djeu J, Latter G, et al. (1985). "Abundant synthesis of the transformation-induced protein of neoplastic human fibroblasts, plastin, in normal lymphocytes.". Cancer Res. 45 (11 Pt 2): 5643–7. PMID 4053036. 
• Arpin M, Friederich E, Algrain M, et al. (1995). "Functional differences between L- and T-plastin isoforms.". J. Cell Biol. 127 (6 Pt 2): 1995–2008. doi:10.1083/jcb.127.6.1995. PMC 2120298. PMID 7806577. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2120298. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Lin CS, Shen W, Chen ZP, et al. (1994). "Identification of I-plastin, a human fimbrin isoform expressed in intestine and kidney.". Mol. Cell. Biol. 14 (4): 2457–67. PMC 358613. PMID 8139549. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=358613. 
• Goldsmith SC, Pokala N, Shen W, et al. (1997). "The structure of an actin-crosslinking domain from human fimbrin.". Nat. Struct. Biol. 4 (9): 708–12. doi:10.1038/nsb0997-708. PMID 9302997. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Shoeman RL, Hartig R, Hauses C, Traub P (2003). "Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease.". Cell Biol. Int. 26 (6): 529–39. doi:10.1006/cbir.2002.0895. PMID 12119179. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Rao RM, Rama S, Rao AJ (2004). "Changes in T-plastin expression with human trophoblast differentiation.". Reprod. Biomed. Online 7 (2): 235–42. doi:10.1016/S1472-6483(10)61758-0. PMID 14567899. 
• Su MW, Dorocicz I, Dragowska WH, et al. (2004). "Aberrant expression of T-plastin in Sezary cells.". Cancer Res. 63 (21): 7122–7. PMID 14612505. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Giganti A, Plastino J, Janji B, et al. (2005). "Actin-filament cross-linking protein T-plastin increases Arp2/3-mediated actin-based movement.". J. Cell. Sci. 118 (Pt 6): 1255–65. doi:10.1242/jcs.01698. PMID 15741236. 
• Ralser M, Nonhoff U, Albrecht M, et al. (2005). "Ataxin-2 and huntingtin interact with endophilin-A complexes to function in plastin-associated pathways.". Hum. Mol. Genet. 14 (19): 2893–909. doi:10.1093/hmg/ddi321. PMID 16115810. 
• Ikeda H, Sasaki Y, Kobayashi T, et al. (2006). "The role of T-fimbrin in the response to DNA damage: silencing of T-fimbrin by small interfering RNA sensitizes human liver cancer cells to DNA-damaging agents.". Int. J. Oncol. 27 (4): 933–40. PMID 16142308. 
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.