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Protein

Major royal jelly protein 1

Gene

MRJP1

Organism
Apis mellifera (Honeybee)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

  1. caste determination, influence by environmental factors Source: UniProtKB
  2. defense response to fungus Source: UniProtKB
  3. defense response to Gram-negative bacterium Source: UniProtKB
  4. defense response to Gram-positive bacterium Source: UniProtKB
  5. killing of cells of other organism Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Developmental protein, Fungicide

Names & Taxonomyi

Protein namesi
Recommended 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:
Alternative name(s):
Jelleine-I
Alternative name(s):
Jelleine-II
Alternative name(s):
Jelleine-IV
Gene namesi
Name:MRJP1
OrganismiApis mellifera (Honeybee)
Taxonomic identifieri7460 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaHymenopteraApocritaAculeataApoideaApidaeApis
ProteomesiUP000005203: Unassembled WGS sequence, UP000005203: Unplaced

Subcellular locationi

Secreted 2 Publications

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei7627. Api m Apalbumin 1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19192 PublicationsAdd
BLAST
Chaini20 – 432413Major royal jelly protein 1PRO_0000031043Add
BLAST
Peptidei424 – 4329Jellein-2PRO_0000224649
Peptidei424 – 4318Jellein-4PRO_0000224650
Peptidei425 – 4328Jellein-1PRO_0000224648

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi28 – 281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence Analysis
Modified residuei431 – 4311Histidine amide; atypical1 Publication
Modified residuei432 – 4321Leucine amide; atypical1 Publication

Post-translational modificationi

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

Keywords - PTMi

Amidation, Glycoprotein

Proteomic databases

PaxDbiO18330.
PRIDEiO18330.

Expressioni

Tissue specificityi

Found in the hypopharyngeal glands of the worker honeybee.2 Publications

Developmental stagei

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.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO18330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the major royal jelly protein family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3386.
HOGENOMiHOG000136640.
InParanoidiO18330.
PhylomeDBiO18330.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR017996. Royal_jelly/Protein_yellow.
[Graphical view]
PANTHERiPTHR10009. PTHR10009. 1 hit.
PfamiPF03022. MRJP. 1 hit.
[Graphical view]
PRINTSiPR01366. ROYALJELLY.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O18330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRLFMLVCL GIVCQGTTGN ILRGESLNKS LPILHEWKFF DYDFGSDERR
60 70 80 90 100
QDAILSGEYD YKNNYPSDID QWHDKIFVTM LRYNGVPSSL NVISKKVGDG
110 120 130 140 150
GPLLQPYPDW SFAKYDDCSG IVSASKLAID KCDRLWVLDS GLVNNTQPMC
160 170 180 190 200
SPKLLTFDLT TSQLLKQVEI PHDVAVNATT GKGRLSSLAV QSLDCNTNSD
210 220 230 240 250
TMVYIADEKG EGLIVYHNSD DSFHRLTSNT FDYDPKFTKM TIDGESYTAQ
260 270 280 290 300
DGISGMALSP MTNNLYYSPV ASTSLYYVNT EQFRTSDYQQ NDIHYEGVQN
310 320 330 340 350
ILDTQSSAKV VSKSGVLFFG LVGDSALGCW NEHRTLERHN IRTVAQSDET
360 370 380 390 400
LQMIASMKIK EALPHVPIFD RYINREYILV LSNKMQKMVN NDFNFDDVNF
410 420 430
RIMNANVNEL ILNTRCENPD NDRTPFKISI HL
Length:432
Mass (Da):48,886
Last modified:January 1, 1998 - v1
Checksum:i9F42BF08D34A1A7B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281N → L AA sequence (PubMed:11302159).Curated
Sequence conflicti30 – 301S → K AA sequence (PubMed:11302159).Curated

Mass spectrometryi

Molecular mass is 953.24±0.17 Da from positions 425 - 432. Determined by ESI. Jellein-1.1 Publication
Molecular mass is 1054.30±0.18 Da from positions 424 - 432. Determined by ESI. Jellein-2.1 Publication
Molecular mass is 942.13±0.17 Da from positions 424 - 431. Determined by ESI. Jellein-4.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D79207 mRNA. Translation: BAA23639.1.
AF000633 mRNA. Translation: AAC61895.1.
AF388203 Genomic DNA. Translation: AAM73637.1.
RefSeqiNP_001011579.1. NM_001011579.1.
UniGeneiAme.208.

Genome annotation databases

EnsemblMetazoaiGB55205-RA; GB55205-PA; GB55205.
GeneIDi406090.
KEGGiame:406090.

Cross-referencesi

Web resourcesi

Protein Spotlight

A queen's dinner - Issue 130 of August 2011

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D79207 mRNA. Translation: BAA23639.1.
AF000633 mRNA. Translation: AAC61895.1.
AF388203 Genomic DNA. Translation: AAM73637.1.
RefSeqiNP_001011579.1. NM_001011579.1.
UniGeneiAme.208.

3D structure databases

ProteinModelPortaliO18330.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei7627. Api m Apalbumin 1.

Proteomic databases

PaxDbiO18330.
PRIDEiO18330.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiGB55205-RA; GB55205-PA; GB55205.
GeneIDi406090.
KEGGiame:406090.

Organism-specific databases

CTDi406090.

Phylogenomic databases

eggNOGiCOG3386.
HOGENOMiHOG000136640.
InParanoidiO18330.
PhylomeDBiO18330.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR017996. Royal_jelly/Protein_yellow.
[Graphical view]
PANTHERiPTHR10009. PTHR10009. 1 hit.
PfamiPF03022. MRJP. 1 hit.
[Graphical view]
PRINTSiPR01366. ROYALJELLY.
ProtoNetiSearch...

Publicationsi

  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. 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.

Entry informationi

Entry nameiMRJP1_APIME
AccessioniPrimary (citable) accession number: O18330
Secondary accession number(s): Q548D6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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 (PubMed:16290177).1 Publication
Degraded proportionally to the period of storage, and is completely lost during storage at 40 degrees Celsius for 30 days.1 Publication

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.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.