Venom Protein Card


Accession: Pre05209    Major royal jelly protein 1 precursor   [Apis mellifera]

Basic info
Organism Apis mellifera
Taxonomy Insecta > Hymenoptera > Apidae > Apis > Apis mellifera
Protein Description Major royal jelly protein 1 precursor
Mass Weight 48885.54 Da
Isoelectric Point 5.1
Expression Highly expressed in venom gland
Annotation
Function [Major royal jelly protein 1]: Induces the differentiation of honeybee larvae into queens through an Egfr-mediated signaling pathway. Promotes body size increase by activating p70 S6 kinase, stimulates ovary development by augmenting the titer of vitellogenin (Vg) and juvenile hormone, and reduces developmental time by increasing the activity of mitogen-activated protein kinase and inducing the 20- hydroxyecdysone protein (20E). Most abundant protein found in the royal jelly which is the food of the queen honey bee larva. The royal jelly determines the development of the young larvae and is responsible for the high reproductive ability of the honeybee queen.
Pfam
PF03022 MRJP
Features
Feature key Position Length
Signal Peptide 1..19 19
Chain 20..432 413
Peptide 424..432 9
Peptide 424..431 8
Peptide 425..432 8
Cross-Reference
NCBI Nucleotide NM_001011579.1
NCBI Protein NP_001011579.1
UniProt O18330
Sequence
ATGACAAGATTGTTTATGCTGGTATGCCTTGGCATAGTTTGTCAAGGTACGACAGGCAACATTCTTCGAGGAGAGTCTTTAAACAAATCATTACCCATCCTTCACGAATGGAAATTCTTTGATTATGATTTCGGTAGCGATGAAAGAAGACAAGATGCAATTCTATCTGGCGAATACGACTACAAGAATAATTATCCATCCGACATTGACCAATGGCATGATAAGATTTTTGTCACCATGCTGAGATACAATGGCGTACCTTCCTCTTTGAACGTGATATCTAAAAAGGTCGGTGATGGTGGTCCTCTTCTACAACCTTATCCCGATTGGTCGTTTGCTAAATATGACGATTGCTCTGGAATCGTGAGCGCCTCAAAACTTGCGATCGACAAATGCGACAGATTGTGGGTTCTGGACTCAGGTCTTGTCAATAATACTCAACCCATGTGTTCTCCAAAACTGCTCACCTTTGATCTGACTACCTCGCAATTGCTCAAGCAAGTTGAAATACCACATGATGTTGCCGTAAATGCCACTACAGGAAAGGGAAGATTATCATCTCTAGCTGTTCAATCTTTAGATTGCAATACAAATAGCGATACTATGGTGTACATAGCAGACGAGAAAGGTGAAGGTTTAATCGTGTATCATAATTCTGATGATTCCTTCCATCGATTGACTTCCAACACTTTCGATTACGATCCTAAATTTACCAAAATGACGATCGATGGAGAAAGTTACACAGCCCAAGATGGAATTTCTGGAATGGCTCTTAGTCCCATGACTAACAATCTCTATTACAGTCCTGTAGCTTCCACCAGTTTGTATTATGTTAACACGGAACAATTCAGAACATCCGATTATCAACAGAATGACATACATTACGAAGGAGTCCAAAATATTTTGGATACCCAATCGTCCGCTAAAGTAGTATCAAAGAGTGGCGTTCTCTTCTTCGGATTGGTGGGCGATTCAGCTCTTGGCTGCTGGAACGAACATCGAACACTTGAAAGACACAATATCCGTACCGTCGCTCAAAGTGATGAGACTCTTCAAATGATCGCTAGCATGAAGATTAAGGAAGCTCTNCCACACGTGCCTATATTCGATAGGTATATAAACCGTGAATACATATTGGTTTTAAGTAACAAAATGCAAAAAATGGTGAATAATGACTTCAACTTCGACGATGTTAACTTCAGAATTATGAACGCGAATGTAAACGAATTGATATTGAACACTCGTTGCGAAAATCCCGATAATGATCGAACACCTTTCAAAATTTCAATCCATTTGTAA
MTRLFMLVCLGIVCQGTTGNILRGESLNKSLPILHEWKFFDYDFGSDERRQDAILSGEYDYKNNYPSDIDQWHDKIFVTMLRYNGVPSSLNVISKKVGDGGPLLQPYPDWSFAKYDDCSGIVSASKLAIDKCDRLWVLDSGLVNNTQPMCSPKLLTFDLTTSQLLKQVEIPHDVAVNATTGKGRLSSLAVQSLDCNTNSDTMVYIADEKGEGLIVYHNSDDSFHRLTSNTFDYDPKFTKMTIDGESYTAQDGISGMALSPMTNNLYYSPVASTSLYYVNTEQFRTSDYQQNDIHYEGVQNILDTQSSAKVVSKSGVLFFGLVGDSALGCWNEHRTLERHNIRTVAQSDETLQMIASMKIKEALPHVPIFDRYINREYILVLSNKMQKMVNNDFNFDDVNFRIMNANVNELILNTRCENPDNDRTPFKISIHL

3D Structure
Not available now!
Publication
1. Ohashi K., Natori S., Kubo T.;
"Change in the mode of gene expression of the hypopharyngeal gland cells with an age-dependent role change of the worker honeybee Apis mellifera L.";
Eur. J. Biochem. 249:797-802(1997).
2. Schmitzova J., Klaudiny J., Albert S., Schroeder W., Schreckengost W., Hanes J., Judova J., Simuth J.;
"A family of major royal jelly proteins of the honeybee Apis mellifera L.";
Cell. Mol. Life Sci. 54:1020-1030(1998).
3. Malecova B., Ramser J., O'Brien J.K., Janitz M., Judova J., Lehrach H., Simuth J.;
"Honeybee (Apis mellifera L.) mrjp gene family: computational analysis of putative promoters and genomic structure of mrjp1, the gene coding for the most abundant protein of larval food.";
Gene 303:165-175(2003).
4. Yoon B.S., Nguyen K.T.;
"Cloning, expression and monoclonal antibody generation of major royal jelly protein 1 (MJRP1) from Apis mellifera."; Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
5. Kamakura M., Fukuda T., Fukushima M., Yonekura M.;
"Storage-dependent degradation of 57-kDa protein in royal jelly: a possible marker for freshness.";
Biosci. Biotechnol. Biochem. 65:277-284(2001).
6. Fontana R., Mendes M.A., de Souza B.M., Konno K., Cesar L.M., Malaspina O., Palma M.S.;
"Jelleines: a family of antimicrobial peptides from the royal jelly of honeybees (Apis mellifera).";
Peptides 25:919-928(2004).
7. Simuth J.;
"Some properties of the main protein of honeybee (Apis mellifera) royal jelly."; Apidologie 32:69-80(2001).
8. Kamakura M., Sakaki T.;
"A hypopharyngeal gland protein of the worker honeybee Apis mellifera L. enhances proliferation of primary-cultured rat hepatocytes and suppresses apoptosis in the absence of serum.";
Protein Expr. Purif. 45:307-314(2006).
9. Kamakura M.;
"Royalactin induces queen differentiation in honeybees.";
Nature 473:478-483(2011).
10. Furusawa T., Arai Y., Kato K., Ichihara K.;
"Quantitative analysis of apisin, a major protein unique to royal jelly.";
Evid. Based Complement Alternat. Med. 2016:5040528-5040528(2016).