RMND5B

RMND5B
Identifiers
AliasesRMND5B, GID2, GID2B, required for meiotic nuclear division 5 homolog B
External IDsMGI: 1913339 HomoloGene: 100777 GeneCards: RMND5B
Gene location (Human)
Chr.Chromosome 5 (human)[1]
Band5q35.3Start178,130,996 bp[1]
End178,150,565 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

64777

66089

Ensembl

ENSG00000145916

ENSMUSG00000001054

UniProt

Q96G75

Q91YQ7

RefSeq (mRNA)

NM_001288794
NM_001288795
NM_022762

NM_025346

RefSeq (protein)

NP_001275723
NP_001275724
NP_073599

NP_079622

Location (UCSC)Chr 5: 178.13 – 178.15 MbChr 11: 51.62 – 51.64 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Required for meiotic nuclear division 5 homolog B (S. cerevisiae), also known as RMND5B, is a protein which in humans is encoded by the RMND5B gene.[5] It has a zinc finger domain and is highly conserved throughout many eukaryotic organisms.

Protein sequence

This protein is rich in leucine (14.0%) and might belong to the protein family of leucine-rich repeats

        1 meqcacvere ldkvlqkflt ygqhcersle ellhyvgqlr aelasaalqg tplsatlslv
       61 msqccrkikd tvqklasdhk dihssvsrvg kaidrnfdse icgvvsdavw dareqqqqil
      121 qmaivehlyq qgmlsvaeel cqestlnvdl dfkqpfleln rilealheqd lgpalewavs
      181 hrqrllelns slefklhrlh firllaggpa kqlealsyar hfqpfarlhq reiqvmmgsl
      241 vylrlgleks pychlldssh waeicetftr dacsllglsv esplsvsfas gcvalpvlmn
      301 ikavieqrqc tgvwnhkdel pieielgmkc wyhsvfacpi lrqqtsdsnp piklicghvi
      361 srdalnklin ggklkcpycp meqnpadgkr iif

Homology

text shaded multiple sequence alignment of CAD28476; the shaded amino acids are conserved

CAD28476 is highly conserved in many eukaryotic organism. Its high conservation suggests that it plays a primary role in meiosis.

Orthologs

taxonomic name common name NCBI entry Percentage of sequence similarity Length (AAs) comments
Homo sapiensHuman100%393hypothetical Protein for Meiosis
Pan troglodytesChimpanzee99.7%393required for meiotic nuclear division 5 homolog B isoform 6
Macaca mulattaRhesus macaque98.5%393Similar to CG3295-PA isoform 11
Rattus norvegicusNorway rat98.2%393Similar to RIKEN cDNA 0610039K22
Mus musculusHouse mouse97.7%393Required for meiotic nuclear division 5 homolog B
Equus caballusHorse97.7%273PREDICTED: similar required for meiotic nuclear division 5 homolog B
Bos taurusCattle95.4%393required for meiotic nuclear division 5 homolog B
Danio rerioZebrafish72.8%391required for meiotic nuclear division 5 homolog B
Xenopus laevisAfrican clawed frog70%391MGC84431 protein
Canis lupus familiarisDog70%391PREDICTED: similar to CG3295-PA isoform A
Tetraodon nigroviridisSpotted green pufferfish68.5%417unnamed protein product
Ornithorhynchus anatinusPlatypus64.5%389
Branchiostoma floridaeFlorida lancelet57%491hypothetical protein BRAFLDRAFT_126901
Nematostella vectensisSea anemone50.1%389
Culex quinquefasciatusSouthern house mosquito48.5%392conserved hypothetical protein
Aedes aegyptiYellow fever mosquito48.2%392hypothetical protein AaeL_AAEL009407
Strongylocentrotus purpuratusPurple urchin48.2405PREDICTED: Similar to MGC88921 protein
Drosophila virilisFruit fly41.5%437GJ20343
Drosophila melanogasterFruit fly40.3%431CG3295
Acyrthosiphon pisum Acrythosiphon39.5%366PREDICTED: required for meiothic nuclear division 5 homolg A
Oryza sativaRice32.2%386membrane protein-like

Zinc finger domain

This depiction shows the location of the two predicted protein domains.
Result of local sequence alignment- the amino acids found in the zinc finger domain are highlighted in different color
The three amino acids which are coordinated to the zinc ion.

Two domains were predicted by the program BLIMPS[6] to exist in the protein of which one of the domains contains a zinc finger domain.

Zinc finger domains assist the binding of the protein to nucleic acids. This points to a direct interaction of CAD28476 with DNA during meiosis. By comparing CAD28476 with a related zinc finger protein[7] in a local sequence alignment using LALIGN,[8] the amino acids His359, Cys381 and Cys384 could be attributed to the zinc finger domain. This zinc finger structure is uncommon in the way that it involves one histidine instead of two.

Expression

Microarray data show that CAD28476 is highly expressed in tissue where meiosis occurs like in testis and ovaries. Moreover it is also highly expressed in the brain around the hypothalamus.

Transcriptional regulation

Listed binding sites for different transcription factors, the bold transcription factors are very likely to be involved in regulation.

The analysis of the promoter region (tools on the page rVista .[9] were used) shows that there are several transcription factor binding sites localized in conserved regions . It is very likely that the transcription factor Ets-1 which belongs to the ETS transcription factor family and its core binding factor CBF are involved in regulation of transcription since they both have independent binding sites.

Interacting proteins

There were two proteins predicted[10] which interact with CAD28476.

name of the protein Uniprot entry information about the gene
Ewing sarcoma breakpoint region 1, isoform CRA_a gene encodes a putative RNA binding protein. Mutations in this gene, specifically a t(11;22)(q24;q12) translocation, are known to cause Ewing sarcoma as well as neuroectodermal and various other tumors.
Mothers against decapentaplegic homolog 4 SMAD4

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000145916 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000001054 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ "Entrez Gene: RMND5B required for meiotic nuclear division 5 homolog B (S. cerevisiae)".
  6. ↑ Jorja Henikoff, Fred Hutchinson Cancer Research Center, 1100 Fairview AV N, A1-162, PO Box 19024 Seattle, WA 98109-1024 FAX: 206-667-5889
  7. ↑ "PDB entry of 2ct2". Retrieved 12 May 2009.
  8. ↑ © 1997 by William R. Pearson and the University of Virginia (This is from distribution "fasta20u66", version 2.0u66, Sep., 1998, sale or incorporation into a commercial product expressly forbidden without permission)
  9. ↑ "rvista Home Page". Retrieved 12 May 2009.
  10. ↑ "homepage of Genecard". Retrieved 12 May 2009.

Further reading

  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Pope SN, Lee IR (2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin". J. Steroid Biochem. Mol. Biol. 94 (1–3): 203–8. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
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