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{{Infobox_gene}}
{{PBB_Controls
'''Plastin-3''' is a highly conserved [[protein]] that in humans is encoded by the ''PLS3'' [[gene]] on the X chromosome.<ref name="pmid8428952">{{cite journal | vauthors = Lin CS, Park T, Chen ZP, Leavitt J | title = Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells | journal = J Biol Chem | volume = 268 | issue = 4 | pages = 2781–92 |date=Mar 1993 | pmid = 8428952 | pmc = | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PLS3 plastin 3 (T isoform)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5358| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_PLS3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aoa.
| PDB = {{PDB2|1aoa}}, {{PDB2|1wjo}}
| Name = Plastin 3 (T isoform)
| HGNCid = 9091
| Symbol = PLS3
| AltSymbols =; T-PLASTIN
| OMIM = 300131
| ECnumber = 
| Homologene = 68250
| MGIid = 104807
| GeneAtlas_image1 = PBB_GE_PLS3_201215_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5358
    | Hs_Ensembl = ENSG00000102024
    | Hs_RefseqProtein = NP_005023
    | Hs_RefseqmRNA = NM_005032
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 114701740
    | Hs_GenLoc_end = 114791433
    | Hs_Uniprot = P13797
    | Mm_EntrezGene = 102866
    | Mm_Ensembl = ENSMUSG00000016382
    | Mm_RefseqmRNA = XM_978781
    | Mm_RefseqProtein = XP_983875
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 72038383
    | Mm_GenLoc_end = 72127258
    | Mm_Uniprot = Q3TUZ5
  }}
}}
'''Plastin 3 (T isoform)''', also known as '''PLS3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PLS3 plastin 3 (T isoform)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5358| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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 in biology|calcium]]-binding site near the [[N-terminus]].<ref name="entrez" />
{{PBB_Summary
 
| section_title =
== Clinical significance ==
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: PLS3 plastin 3 (T isoform)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5358| accessdate = }}</ref>
 
}}
Defects in PLS3 are associated with [[osteoporosis]] and bone fracture in humans and in [[gene knockout|knockout]] zebrafish.<ref name="pmid24088043">{{cite journal | vauthors = van Dijk FS, Zillikens MC, Micha D, Riessland M, Marcelis CL, de Die-Smulders CE, Milbradt J, Franken AA, Harsevoort AJ, Lichtenbelt KD| title = PLS3 Mutations in X-Linked Osteoporosis with Fractures | journal = N. Engl. J. Med. | volume = 369| issue = 16| pages = 1529–36|date=October 2013 | pmid = 24088043 | doi = 10.1056/NEJMoa1308223 |display-authors=etal}}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Lin CS, Aebersold RH, Leavitt J |title=Correction of the N-terminal sequences of the human plastin isoforms by using anchored polymerase chain reaction: identification of a potential calcium-binding domain. |journal=Mol. Cell. Biol. |volume=10 |issue= 4 |pages= 1818–21 |year= 1990 |pmid= 2378651 |doi= | pmc=362293 }}
| citations =
*{{cite journal   |vauthors=Lin CS, Aebersold RH, Kent SB, etal |title=Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts. |journal=Mol. Cell. Biol. |volume=8 |issue= 11 |pages= 4659–68 |year= 1988 |pmid= 3211125 |doi= | pmc=365555 }}
*{{cite journal  | author=Lin CS, Aebersold RH, Leavitt J |title=Correction of the N-terminal sequences of the human plastin isoforms by using anchored polymerase chain reaction: identification of a potential calcium-binding domain. |journal=Mol. Cell. Biol. |volume=10 |issue= 4 |pages= 1818-21 |year= 1990 |pmid= 2378651 |doi=  }}
*{{cite journal   |vauthors=Goldstein D, Djeu J, Latter G, etal |title=Abundant synthesis of the transformation-induced protein of neoplastic human fibroblasts, plastin, in normal lymphocytes. |journal=Cancer Res. |volume=45 |issue= 11 Pt 2 |pages= 5643–7 |year= 1985 |pmid= 4053036 |doi=  }}
*{{cite journal | author=Lin CS, Aebersold RH, Kent SB, ''et al.'' |title=Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts. |journal=Mol. Cell. Biol. |volume=8 |issue= 11 |pages= 4659-68 |year= 1989 |pmid= 3211125 |doi=  }}
*{{cite journal   |vauthors=Arpin M, Friederich E, Algrain M, etal |title=Functional differences between L- and T-plastin isoforms. |journal=J. Cell Biol. |volume=127 |issue= 6 Pt 2 |pages= 1995–2008 |year= 1995 |pmid= 7806577 |doi=10.1083/jcb.127.6.1995  | pmc=2120298 }}
*{{cite journal | author=Goldstein D, Djeu J, Latter G, ''et al.'' |title=Abundant synthesis of the transformation-induced protein of neoplastic human fibroblasts, plastin, in normal lymphocytes. |journal=Cancer Res. |volume=45 |issue= 11 Pt 2 |pages= 5643-7 |year= 1985 |pmid= 4053036 |doi=  }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Arpin M, Friederich E, Algrain M, ''et al.'' |title=Functional differences between L- and T-plastin isoforms. |journal=J. Cell Biol. |volume=127 |issue= 6 Pt 2 |pages= 1995-2008 |year= 1995 |pmid= 7806577 |doi=  }}
*{{cite journal   |vauthors=Lin CS, Shen W, Chen ZP, etal |title=Identification of I-plastin, a human fimbrin isoform expressed in intestine and kidney. |journal=Mol. Cell. Biol. |volume=14 |issue= 4 |pages= 2457–67 |year= 1994 |pmid= 8139549 |doi=  10.1128/mcb.14.4.2457| pmc=358613 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal   |vauthors=Goldsmith SC, Pokala N, Shen W, etal |title=The structure of an actin-crosslinking domain from human fimbrin. |journal=Nat. Struct. Biol. |volume=4 |issue= 9 |pages= 708–12 |year= 1997 |pmid= 9302997 |doi=10.1038/nsb0997-708 }}
*{{cite journal | author=Lin CS, Shen W, Chen ZP, ''et al.'' |title=Identification of I-plastin, a human fimbrin isoform expressed in intestine and kidney. |journal=Mol. Cell. Biol. |volume=14 |issue= 4 |pages= 2457-67 |year= 1994 |pmid= 8139549 |doi=  }}
*{{cite journal  | vauthors=Shoeman RL, Hartig R, Hauses C, Traub P |title=Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease. |journal=Cell Biol. Int. |volume=26 |issue= 6 |pages= 529–39 |year= 2003 |pmid= 12119179 |doi=10.1006/cbir.2002.0895  }}
*{{cite journal  | author=Lin CS, Park T, Chen ZP, Leavitt J |title=Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells. |journal=J. Biol. Chem. |volume=268 |issue= 4 |pages= 2781-92 |year= 1993 |pmid= 8428952 |doi=  }}
*{{cite journal  | vauthors=Rao RM, Rama S, Rao AJ |title=Changes in T-plastin expression with human trophoblast differentiation. |journal=Reprod. Biomed. Online |volume=7 |issue= 2 |pages= 235–42 |year= 2004 |pmid= 14567899 |doi=10.1016/S1472-6483(10)61758-0 }}
*{{cite journal | author=Goldsmith SC, Pokala N, Shen W, ''et al.'' |title=The structure of an actin-crosslinking domain from human fimbrin. |journal=Nat. Struct. Biol. |volume=4 |issue= 9 |pages= 708-12 |year= 1997 |pmid= 9302997 |doi= }}
*{{cite journal   |vauthors=Su MW, Dorocicz I, Dragowska WH, etal |title=Aberrant expression of T-plastin in Sezary cells. |journal=Cancer Res. |volume=63 |issue= 21 |pages= 7122–7 |year= 2004 |pmid= 14612505 |doi=  }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal   |vauthors=Giganti A, Plastino J, Janji B, etal |title=Actin-filament cross-linking protein T-plastin increases Arp2/3-mediated actin-based movement. |journal=J. Cell Sci. |volume=118 |issue= Pt 6 |pages= 1255–65 |year= 2005 |pmid= 15741236 |doi= 10.1242/jcs.01698 }}
*{{cite journal  | author=Shoeman RL, Hartig R, Hauses C, Traub P |title=Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease. |journal=Cell Biol. Int. |volume=26 |issue= 6 |pages= 529-39 |year= 2003 |pmid= 12119179 |doi=  }}
*{{cite journal   |vauthors=Ralser M, Nonhoff U, Albrecht M, etal |title=Ataxin-2 and huntingtin interact with endophilin-A complexes to function in plastin-associated pathways. |journal=Hum. Mol. Genet. |volume=14 |issue= 19 |pages= 2893–909 |year= 2005 |pmid= 16115810 |doi= 10.1093/hmg/ddi321 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Ikeda H, Sasaki Y, Kobayashi T, etal |title=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. |journal=Int. J. Oncol. |volume=27 |issue= 4 |pages= 933–40 |year= 2006 |pmid= 16142308 |doi=  10.3892/ijo.27.4.933}}
*{{cite journal  | author=Rao RM, Rama S, Rao AJ |title=Changes in T-plastin expression with human trophoblast differentiation. |journal=Reprod. Biomed. Online |volume=7 |issue= 2 |pages= 235-42 |year= 2004 |pmid= 14567899 |doi=  }}
*{{cite journal | author=Su MW, Dorocicz I, Dragowska WH, ''et al.'' |title=Aberrant expression of T-plastin in Sezary cells. |journal=Cancer Res. |volume=63 |issue= 21 |pages= 7122-7 |year= 2004 |pmid= 14612505 |doi=  }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Giganti A, Plastino J, Janji B, ''et al.'' |title=Actin-filament cross-linking protein T-plastin increases Arp2/3-mediated actin-based movement. |journal=J. Cell. Sci. |volume=118 |issue= Pt 6 |pages= 1255-65 |year= 2005 |pmid= 15741236 |doi= 10.1242/jcs.01698 }}
*{{cite journal | author=Ralser M, Nonhoff U, Albrecht M, ''et al.'' |title=Ataxin-2 and huntingtin interact with endophilin-A complexes to function in plastin-associated pathways. |journal=Hum. Mol. Genet. |volume=14 |issue= 19 |pages= 2893-909 |year= 2005 |pmid= 16115810 |doi= 10.1093/hmg/ddi321 }}
*{{cite journal | author=Ikeda H, Sasaki Y, Kobayashi T, ''et al.'' |title=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. |journal=Int. J. Oncol. |volume=27 |issue= 4 |pages= 933-40 |year= 2006 |pmid= 16142308 |doi=  }}
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=5358}}
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[[Category:EF-hand-containing proteins]]
 
 
{{gene-X-stub}}

Revision as of 01:36, 10 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

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Ensembl

n/a

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UniProt

n/a

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Plastin-3 is a highly conserved protein that in humans is encoded by the PLS3 gene on the X chromosome.[1][2]

Function

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.[2]

Clinical significance

Defects in PLS3 are associated with osteoporosis and bone fracture in humans and in knockout zebrafish.[3]

References

  1. ↑ Lin CS, Park T, Chen ZP, Leavitt J (Mar 1993). "Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells". J Biol Chem. 268 (4): 2781–92. PMID 8428952.
  2. ↑ 2.0 2.1 "Entrez Gene: PLS3 plastin 3 (T isoform)".
  3. ↑ van Dijk FS, Zillikens MC, Micha D, Riessland M, Marcelis CL, de Die-Smulders CE, Milbradt J, Franken AA, Harsevoort AJ, Lichtenbelt KD, et al. (October 2013). "PLS3 Mutations in X-Linked Osteoporosis with Fractures". N. Engl. J. Med. 369 (16): 1529–36. doi:10.1056/NEJMoa1308223. PMID 24088043.

Further reading


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