Nexilin (NEXN)

The protein contains 675 amino acids for an estimated molecular weight of 80658 Da.

 

Involved in regulating cell migration through association with the actin cytoskeleton. Has an essential role in the maintenance of Z line and sarcomere integrity. (updated: Sept. 12, 2018)

Protein identification was indicated in the following studies:

  1. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.

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.

This protein is annotated as membranous in Gene Ontology.


Interpro domains
Total structural coverage: 29%
Model score: 0
No model available.

(right-click above to access to more options from the contextual menu)

VariantDescription
CMH20
dbSNP:rs1166698
CMH20
dbSNP:rs9660322
CMD1CC
CMD1CC

The reference OMIM entry for this protein is 613121

Nexilin, rat, homolog of; nexn
Nexilin-like protein; nelin

DESCRIPTION

NEXN is a filamentous actin (F-actin; see 102560)-binding protein that localizes to focal contacts and may be involved in cell adhesion and migration (Ohtsuka et al., 1998; Wang et al., 2005).

CLONING

Ohtsuka et al. (1998) cloned 2 splice variants of rat nexilin, which they called b-nexilin and s-nexilin, from brain and cultured fibroblasts, respectively. The name nexilin came from the Latin word nexilis, meaning 'bound together.' Full-length b-nexilin contains an N-terminal F-actin-binding domain (ABD), followed by a spacer, a coiled-coil region, a second ABD, and a long C-terminal tail. In comparison, s-nexilin lacks the N-terminal ABD and has an insertion in the C-terminal tail. Immunofluorescence microscopy revealed that both b-nexilin and s-nexilin colocalized with F-actin at focal contacts at the ends of stress fibers. The nexilins did not localize to cell-cell junctions. Western blot analysis detected nexilin proteins with apparent molecular masses above 90 kD in rat brain, testis, and spleen and in cultured rodent fibroblasts. Neither protein was detected in liver, kidney, or epithelial cell lines. Wang et al. (2010) stated that the full-length nexilin protein contains 675 amino acids. By sequencing clones obtained from a heart cDNA library and by EST database analysis, Zhao et al. (2001) cloned human nexilin, which they called NELIN. The deduced 493-amino acid protein contains an N-terminal FERIN-like domain, followed by an ABD and a C-terminal immunoglobulin domain. It also has 2 nuclear localization signals. Northern blot analysis detected a major 4.0-kb transcript in adult and fetal heart and skeletal muscle only. A minor 2.7-kb transcript, representing the NELIN cDNA cloned by Zhao et al. (2001), was detected in adult and fetal heart only. Using RT-PCR, Wang et al. (2005) cloned NELIN from umbilical vein wall mRNA. The deduced protein contains 447 amino acids. Northern blot analysis detected a major transcript of about 3.0 kb in heart and skeletal muscle. Fluorescence-tagged NELIN localized predominantly to the cytoplasm of transfected HeLa cells, with some perinuclear concentration. NELIN colocalized with F-actin. Using whole-mount antisense RNA in situ hybridization, Hassel et al. (2009) found that NEXN expression first became detectable in the developing somite and zebrafish heart tube and remained restricted to the heart and skeletal muscle throughout embryogenesis.

GENE STRUCTURE

Wang et al. (2010) noted that the NEXN gene contains 13 exons.

MAPPING

By genomic sequence analysis, Zhao et al. (2001) mapped the NEXN gene to chromosome 1p32-p31. Hassel et al. (2009) noted that the NEXN gene maps to chromosome 1p31.1.

GENE FUNCTION

Using F-actin and deletion constructs of recombinant rat nexilins in cosedimentation assays, Ohtsuka et al. (1998) showed that b-nexilin has 2 ABDs and that s-nexilin has a single ABD. The coiled-coil region and the second ABD were required for localization of b-nexilin and s-nexilin at focal contacts. Pretreatment of F-actin with myosin (see 160730) subfragment-1, which binds along the sides of F-actin, inhibited F-actin binding by b-nexilin. This inhibition was reversed by MgATP, which dissociates the actin-myosin complex. B-nexilin, but not s-nexilin, increased the viscosity of the nexilin-F-actin complex, and electron microscopy showed that the increased viscosity was due to F-actin crosslink formation by b-nexilin. The stoich ... More on the omim web site

Subscribe to this protein entry history

Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 613121 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).