Spermine synthase (SMS)
The protein contains 366 amino acids for an estimated molecular weight of 41268 Da.
Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM). (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- 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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- 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.
| 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.
The reference OMIM entry for this protein is 300105
Spermine synthase; sms
DESCRIPTION
Spermine synthase (EC 2.5.1.22) is 1 of 4 enzymes involved in the synthesis of polyamines from arginine and methionine. The others are ornithine decarboxylase (165640), S-adenosyl-L-methionine decarboxylase (180980), and spermidine synthase (182891).CLONING
Korhonen et al. (1995) isolated and sequenced cDNA clones encoding human spermine synthase. The open reading frame encodes a 368-amino acid protein with little sequence similarity to proteins from bacterial and mammalian sources catalyzing almost identical reactions.GENE STRUCTURE
Grieff et al. (1997) determined that the SMS gene (which they symbolized SpS) contains 11 exons spanning 54 kb.MAPPING
Grieff et al. (1997) mapped the SMS gene 38 kb telomeric to the PHEX gene (300550) on Xp22.1.BIOCHEMICAL FEATURES
- Crystal Structure Wu et al. (2008) determined the crystal structure of human SMS, which is a dimer of 2 identical subunits. Each monomer has 3 domains: a C-terminal domain, which contains the active site and is similar in structure to spermidine synthase; a central domain made up of 4 beta-strands; and an N-terminal domain with structural similarity to S-adenosylmethionine decarboxylase (AMD1; 180980), the enzyme that forms the aminopropyl donor substrate. Dimerization occurs mainly through interactions between the N-terminal domains. Deletion of the N-terminal domain led to a complete loss of spermine synthase activity, suggesting that dimerization may be required for activity.MOLECULAR GENETICS
In affected members of a family with Snyder-Robinson mental retardation syndrome (MRXSSR; 309583) originally reported by Snyder and Robinson (1969), Cason et al. (2003) identified a splice site mutation in the SMS gene (300105.0001). In 2 Mexican brothers with MRXSSR, Becerra-Solano et al. (2009) identified a mutation in the SMS gene (V132G; 300105.0003). In 2 affected males from a Belgian family with a relatively mild form of Snyder-Robinson mental retardation syndrome, Zhang et al. (2013) identified a missense mutation in the SMS gene (Y328C; 300105.0004). In a boy from Italy with Snyder-Robinson syndrome, Peron et al. (2013) identified a missense mutation in the SMS gene (G67E; 300105.0005).ANIMAL MODEL
First identified as a mouse model for X-linked hypophosphatemia, the 'Gyro' or 'Gy' mouse (see 300550) also exhibits neurologic abnormalities, including deafness, hyperactivity, circling behavior, and inner ear abnormalities (Lyon et al., 1986). Meyer et al. (1998) found that the Gyro mouse has a partial deletion of both the Sms gene and the Phex gene, making it a contiguous gene syndrome in that species. However, as mutation in the Phex gene alone results in a hypophosphatemic phenotype in the mouse (Hyp) without neurologic manifestations, Meyer et al. (1998) suggested that a deficiency of spermine may explain the additional neurologic findings in the Gy mouse. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 300105 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed