Plastin-1 (PLS1)

The protein contains 629 amino acids for an estimated molecular weight of 70253 Da.

 

Actin-bundling protein. In the inner ear, it is required for stereocilia formation. Mediates liquid packing of actin filaments that is necessary for stereocilia to grow to their proper dimensions. (updated: Oct. 7, 2020)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

Interpro domains
Total structural coverage: 84%
Model score: 45
MODL_MODELLER-9.18

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VariantDescription
dbSNP:rs35710125
dbSNP:rs35435507
DFNA76
DFNA76
DFNA76
DFNA76

No binding partner found

The reference OMIM entry for this protein is 602734

Plastin 1; pls1
Intestine-specific plastin
I-plastin
Fimbrin

CLONING

Fimbrin is an actin-bundling protein that was originally discovered in chicken intestinal brush border microvilli. By screening a human small intestine cDNA library with a chicken fimbrin cDNA, Lin et al. (1994) identified a cDNA encoding I-plastin. Northern blot analysis revealed that I-plastin was expressed as a 3.7-kb mRNA in human colon and small intestine. A survey of rat tissues detected I-plastin expression primarily in the intestine, with a lower level in the kidneys. By immunofluorescence, Lin et al. (1994) localized I-plastin to the brush border of the human small intestine and colon. The predicted 629-amino acid protein is 86%, 75%, and 73% identical to chicken fimbrin, human T-plastin (PLS3; 300131), and L-plastin (LCP1; 153430), respectively. I-plastin migrated as a 68-kD protein on Western blots of human small intestine and colon extracts. Lin et al. (1994) concluded that I-plastin is the human homolog of chicken intestine fimbrin.

GENE FUNCTION

Lin et al. (1994) found that recombinant I-plastin crosslinked actin filaments into bundles in the absence of calcium but not in its presence.

MAPPING

Lin et al. (1994) mapped the I-plastin gene to chromosome 3 by PCR of somatic cell hybrids.

ANIMAL MODEL

Grimm-Gunter et al. (2009) created Pls1-knockout mice on a C57BL/6 background. The Pls1-null mice were fertile and displayed a normal reproductive rate. Sex distribution of pups and life span were not significantly altered. Microscopic examination of HE-stained intestinal epithelium showed no obvious changes in the organization of villi or crypts. However, transmission electron microscopic analysis of intestinal sections showed that the microvilli were shorter, constricted at their base, and lacked rootlets. The morphologic changes resulted in increased fragility of the epithelium, demonstrated by increased sensitivity of the brush border to biochemical manipulations, decreased transepithelial resistance, and increased sensitivity to dextran sodium sulfate-induced colitis. Taylor et al. (2015) determined that Pls1-null mice have a moderate and progressive form of hearing loss across all frequencies. The auditory hair cells of the knockout mice developed normally, but the stereocilia of inner hair cells were reduced in width and length. The outer hair cell stereocilia were comparatively less affected, but showed signs of degeneration in aging mice. Taylor et al. (2015) noted that C57BL/6 mice are known for increased susceptibility to age-related hearing loss; however, the Pls1-null mice exhibited a more significant hearing loss phenotype starting at an earlier age. ... More on the omim web site

Subscribe to this protein entry history

Oct. 20, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

June 20, 2017: Protein entry updated
Automatic update: comparative model was added.

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 602734 was added.