Biology:RMND5B

Generic protein structure example

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. 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 sapiens	Human	[1]	100%	393	hypothetical Protein for Meiosis
Pan troglodytes	Chimpanzee	[2]	99.7%	393	required for meiotic nuclear division 5 homolog B isoform 6
Macaca mulatta	Rhesus macaque	[3]	98.5%	393	Similar to CG3295-PA isoform 11
Rattus norvegicus	Norway rat	[4]	98.2%	393	Similar to RIKEN cDNA 0610039K22
Mus musculus	House mouse	[5]	97.7%	393	Required for meiotic nuclear division 5 homolog B
Equus caballus	Horse	[6]	97.7%	273	PREDICTED: similar required for meiotic nuclear division 5 homolog B
Bos taurus	Cattle	[7]	95.4%	393	required for meiotic nuclear division 5 homolog B
Danio rerio	Zebrafish	[8]	72.8%	391	required for meiotic nuclear division 5 homolog B
Xenopus laevis	African clawed frog	[9]	70%	391	MGC84431 protein
Canis lupus familiaris	Dog	[10]	70%	391	PREDICTED: similar to CG3295-PA isoform A
Tetraodon nigroviridis	Spotted green pufferfish	[11]	68.5%	417	unnamed protein product
Ornithorhynchus anatinus	Platypus	[12]	64.5%	389
Branchiostoma floridae	Florida lancelet	[13]	57%	491	hypothetical protein BRAFLDRAFT_126901
Nematostella vectensis	Sea anemone	[14]	50.1%	389
Culex quinquefasciatus	Southern house mosquito	[15]	48.5%	392	conserved hypothetical protein
Aedes aegypti	Yellow fever mosquito	[16]	48.2%	392	hypothetical protein AaeL_AAEL009407
Strongylocentrotus purpuratus	Purple urchin	[17]	48.2	405	PREDICTED: Similar to MGC88921 protein
Drosophila virilis	Fruit fly	[18]	41.5%	437	GJ20343
Drosophila melanogaster	Fruit fly	[19]	40.3%	431	CG3295
Acyrthosiphon pisum	Acrythosiphon	[20]	39.5%	366	PREDICTED: required for meiothic nuclear division 5 homolg A
Oryza sativa	Rice	[21]	32.2%	386	membrane 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 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 in a local sequence alignment using LALIGN, 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 . 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 which interact with CAD28476.

name of the protein	Uniprot entry	information about the gene
Ewing sarcoma breakpoint region 1, isoform CRA_a	[22]	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	[23]	SMAD4

Further reading

• "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. 
• "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. 2003. doi:10.1101/gr.1293003. PMID 12975309. 
• "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. 2004. doi:10.1038/ng1285. PMID 14702039. 
• "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324–32. 2004. doi:10.1101/gr.2334104. PMID 15231748. 
• "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334. 
• "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin.". J. Steroid Biochem. Mol. Biol. 94 (1–3): 203–8. 2005. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967. 
• "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514.