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O18330 (MRJP1_APIME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Major royal jelly protein 1

Short name=MRJP-1
Alternative name(s):
56-kDa protein 4
Short name=p56kP-4
Bee-milk protein
Royalactin

Cleaved into the following 3 chains:

  1. Jellein-1
    Alternative name(s):
    Jelleine-I
  2. Jellein-2
    Alternative name(s):
    Jelleine-II
  3. Jellein-4
    Alternative name(s):
    Jelleine-IV
Gene names
Name:MRJP1
OrganismApis mellifera (Honeybee) [Reference proteome]
Taxonomic identifier7460 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataApoideaApidaeApis

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.5 Ref.7

Jellein-1: has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans. Lack cytolytic activity and does not induce rat peritoneal mast cell degranulation. Ref.1 Ref.5 Ref.7

Jellein-2: has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans. Lack cytolytic activity and does not induce rat peritoneal mast cell degranulation. Ref.1 Ref.5 Ref.7

Jellein-4: lacks antibacterial and antifungal activity. Lacks cytolytic activity and does not induce rat peritoneal mast cell degranulation. Ref.1 Ref.5 Ref.7

Subcellular location

Secreted Ref.1 Ref.5.

Tissue specificity

Found in the hypopharyngeal glands of the worker honeybee. Ref.1 Ref.5

Developmental stage

Produced in the cephalic glands of both the nurse bee and the forager bee. This bee milk protein changes to alpha-glucosidase in accordance with the age-dependent role change of the worker bee. Ref.1

Post-translational modification

Glycosylated. Ref.1

Jellein-2 is probably processed to yield jellein-1 and jellein-4.

Miscellaneous

Exhibits a growth factor-like action on primary-cultured rat hepatocytes by stimulating DNA synthesis and protecting cells from apoptosis induced by serum deprivation. Also activates mitogen-activated protein kinase, as well as protein kinase B, a key regulator of cell survival (Ref.6).

Degraded proportionally to the period of storage, and is completely lost during storage at 40 degrees Celsius for 30 days (Ref.7).

Sequence similarities

Belongs to the major royal jelly protein family.

Caution

Neither His-431 nor Leu-432 is followed in the nucleotide sequence by the expected Gly residue that would be required to produce amidation.

Mass spectrometry

Molecular mass is 953.24±0.17 Da from positions 425 - 432. Determined by ESI. Jellein-1. Ref.5

Molecular mass is 1054.30±0.18 Da from positions 424 - 432. Determined by ESI. Jellein-2. Ref.5

Molecular mass is 942.13±0.17 Da from positions 424 - 431. Determined by ESI. Jellein-4. Ref.5

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.2 Ref.4
Chain20 – 432413Major royal jelly protein 1
PRO_0000031043
Peptide424 – 4329Jellein-2 Ref.5
PRO_0000224649
Peptide424 – 4318Jellein-4
PRO_0000224650
Peptide425 – 4328Jellein-1
PRO_0000224648

Amino acid modifications

Modified residue4311Histidine amide; atypical Ref.5
Modified residue4321Leucine amide; atypical Ref.5
Glycosylation281N-linked (GlcNAc...) Potential
Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict281N → L AA sequence Ref.4
Sequence conflict301S → K AA sequence Ref.4

Sequences

Sequence LengthMass (Da)Tools
O18330 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 9F42BF08D34A1A7B

FASTA43248,886
        10         20         30         40         50         60 
MTRLFMLVCL GIVCQGTTGN ILRGESLNKS LPILHEWKFF DYDFGSDERR QDAILSGEYD 

        70         80         90        100        110        120 
YKNNYPSDID QWHDKIFVTM LRYNGVPSSL NVISKKVGDG GPLLQPYPDW SFAKYDDCSG 

       130        140        150        160        170        180 
IVSASKLAID KCDRLWVLDS GLVNNTQPMC SPKLLTFDLT TSQLLKQVEI PHDVAVNATT 

       190        200        210        220        230        240 
GKGRLSSLAV QSLDCNTNSD TMVYIADEKG EGLIVYHNSD DSFHRLTSNT FDYDPKFTKM 

       250        260        270        280        290        300 
TIDGESYTAQ DGISGMALSP MTNNLYYSPV ASTSLYYVNT EQFRTSDYQQ NDIHYEGVQN 

       310        320        330        340        350        360 
ILDTQSSAKV VSKSGVLFFG LVGDSALGCW NEHRTLERHN IRTVAQSDET LQMIASMKIK 

       370        380        390        400        410        420 
EALPHVPIFD RYINREYILV LSNKMQKMVN NDFNFDDVNF RIMNANVNEL ILNTRCENPD 

       430 
NDRTPFKISI HL 

« Hide

References

[1]"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."
Ohashi K., Natori S., Kubo T.
Eur. J. Biochem. 249:797-802(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-48; 63-71 AND 361-380, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION.
Tissue: Hypopharyngeal gland.
[2]"A family of major royal jelly proteins of the honeybee Apis mellifera L."
Schmitzova J., Klaudiny J., Albert S., Schroeder W., Schreckengost W., Hanes J., Judova J., Simuth J.
Cell. Mol. Life Sci. 54:1020-1030(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-30.
Tissue: Head.
[3]"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."
Malecova B., Ramser J., O'Brien J.K., Janitz M., Judova J., Lehrach H., Simuth J.
Gene 303:165-175(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Storage-dependent degradation of 57-kDa protein in royal jelly: a possible marker for freshness."
Kamakura M., Fukuda T., Fukushima M., Yonekura M.
Biosci. Biotechnol. Biochem. 65:277-284(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-34.
[5]"Jelleines: a family of antimicrobial peptides from the royal jelly of honeybees (Apis mellifera)."
Fontana R., Mendes M.A., de Souza B.M., Konno K., Cesar L.M., Malaspina O., Palma M.S.
Peptides 25:919-928(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 424-432, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AMIDATION AT HIS-431 AND LEU-432.
[6]"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."
Kamakura M., Sakaki T.
Protein Expr. Purif. 45:307-314(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[7]"Royalactin induces queen differentiation in honeybees."
Kamakura M.
Nature 473:478-483(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Web resources

Protein Spotlight

A queen's dinner - Issue 130 of August 2011

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D79207 mRNA. Translation: BAA23639.1.
AF000633 mRNA. Translation: AAC61895.1.
AF388203 Genomic DNA. Translation: AAM73637.1.
RefSeqNP_001011579.1. NM_001011579.1.
UniGeneAme.208.

3D structure databases

ProteinModelPortalO18330.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome7627. Api m Apalbumin 1.

Proteomic databases

PaxDbO18330.
PRIDEO18330.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaGB14888-RA; GB14888-PA; GB14888.
GeneID406090.
KEGGame:406090.

Organism-specific databases

CTD406090.

Phylogenomic databases

eggNOGCOG3386.
HOGENOMHOG000136640.
InParanoidO18330.
OMAERHNIRT.
PhylomeDBO18330.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR017996. Royal_jelly.
[Graphical view]
PANTHERPTHR10009. PTHR10009. 1 hit.
PfamPF03022. MRJP. 1 hit.
[Graphical view]
PRINTSPR01366. ROYALJELLY.
ProtoNetSearch...

Entry information

Entry nameMRJP1_APIME
AccessionPrimary (citable) accession number: O18330
Secondary accession number(s): Q548D6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries