Plexin-A1 (PLXNA1)
The protein contains 1896 amino acids for an estimated molecular weight of 211067 Da.
Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm (By similarity). (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- 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.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
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.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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Biological Process
Branchiomotor neuron axon guidance
Dichotomous subdivision of terminal units involved in salivary gland branching
Multicellular organism development
Negative regulation of cell adhesion
Neuron projection extension
Positive regulation of axonogenesis
Regulation of axon extension involved in axon guidance
Regulation of cell migration
Regulation of cell shape
Regulation of GTPase activity
Regulation of smooth muscle cell migration
Semaphorin-plexin signaling pathway involved in axon guidance
The reference OMIM entry for this protein is 601055
Plexin a1; plxna1
Plexin 1; plxn1
Transmembrane protein nov; nov
CLONING
Maestrini et al. (1996) identified a novel family of transmembrane proteins with homology to the MET-hepatocyte growth factor receptor family. The first of these, which they termed SEX (300022), mapped to Xq28 and was found in the course of search for previously unknown genes on the human X chromosome. The transmembrane protein they called NOV was identified by a cDNA found in a skeletal muscle cDNA library and shares 72% identity with SEX. The proteins of this family contain large cytoplasmic domains characterized by a distinctive highly conserved sequence, which they termed the SEX domain. Like the SEX and OCT (601054) genes, NOV is expressed in fetal tissues, predominantly in the brain. See also 601053.GENE FUNCTION
Takahashi et al. (1999) found that the 2 semaphorin-binding proteins, plexin-1 (PLXN1) and neuropilin-1 (NRP1; 602069), form a stable complex. PLXN1 alone did not bind semaphorin-3A (SEMA3A; 603961), but the NRP1/PLXN1 complex had a higher affinity for SEMA3A than did NRP1 alone. While SEMA3A binding to NRP1 did not alter nonneuronal cell morphology, SEMA3A interaction with NRP1/PLXN1 complexes induced adherent cells to round up. Expression of a dominant-negative PLXN1 in sensory neurons blocked SEMA3A-induced growth cone collapse. SEMA3A treatment led to the redistribution of growth cone NRP1 and PLXN1 into clusters. Thus, the authors concluded that physiologic SEMA3A receptors consist of NRP1/PLXN1 complexes. Using microarray and RNA interference analyses in mice deficient in major histocompatibility complex (MHC) class II and MHC class II transactivator (CIITA; 600005), Wong et al. (2003) found that Pxna1 was expressed in dendritic cells (DCs), but not in other immune cells, and was strongly induced by Ciita, which regulates Plxna1 promoter function. Plxna1 was not required for peptide binding to MHC, indicating that Plxna1 is involved in T cell-DC interactions, but not in antigen processing.MAPPING
Maestrini et al. (1996) localized the NOV gene to 3q21-qter by screening a panel of hamster/human somatic cell hybrids.NOMENCLATURE
This gene is unrelated to NOV, the nephroblastoma overexpressed gene (164958). Tamagnone et al. (1999) proposed a novel nomenclature for the genes of the plexin family, which they grouped into the A, B, C, and D subfamilies; the PLXN1 gene was renamed plexin A1 by them. ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 601055 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).