Major royal jelly protein 1 precursor - Apis mellifera (Honeybee)

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O18330 (MRJP1_APIME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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:

Jellein-1
Alternative name(s):
Jelleine-I
Jellein-2
Alternative name(s):
Jelleine-II
Jellein-4
Alternative name(s):
Jelleine-IV

Gene names

Name:

MRJP1

Organism

Apis mellifera (Honeybee) [Reference proteome]

Taxonomic identifier

7460 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Hymenoptera › Apocrita › Aculeata › Apoidea › Apidae › Apis

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Antibiotic Antimicrobial Developmental protein Fungicide
PTM	Amidation Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	caste determination, influence by environmental factors Inferred from direct assay Ref.7. Source: UniProtKB defense response to Gram-negative bacterium Inferred from direct assay Ref.5. Source: UniProtKB defense response to Gram-positive bacterium Inferred from direct assay Ref.5. Source: UniProtKB defense response to fungus Inferred from direct assay Ref.5. Source: UniProtKB killing of cells of other organism Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Ref.2 Ref.4

Chain

20 – 432

413

Major royal jelly protein 1

PRO_0000031043

Peptide

424 – 432

Jellein-2 Ref.5

PRO_0000224649

Peptide

424 – 431

Jellein-4

PRO_0000224650

Peptide

425 – 432

Jellein-1

PRO_0000224648

Amino acid modifications

Modified residue

431

Histidine amide; atypical Ref.5

Modified residue

432

Leucine amide; atypical Ref.5

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

144

N-linked (GlcNAc...) Potential

Glycosylation

177

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

N → L AA sequence Ref.4

Sequence conflict

S → K AA sequence Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

O18330 [UniParc].

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

432

48,886

        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

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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.
RefSeq	NP_001011579.1. NM_001011579.1.
UniGene	Ame.208.
3D structure databases
ProteinModelPortal	O18330.
ModBase	Search...
Protein family/group databases
Allergome	7627. Api m Apalbumin 1.
Proteomic databases
PaxDb	O18330.
PRIDE	O18330.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	GB14888-RA; GB14888-PA; GB14888.
GeneID	406090.
KEGG	ame:406090.
Organism-specific databases
CTD	406090.
Phylogenomic databases
eggNOG	COG3386.
HOGENOM	HOG000136640.
InParanoid	O18330.
OrthoDB	EOG49ZW6G.
PhylomeDB	O18330.
Family and domain databases
Gene3D	2.120.10.30. 1 hit.
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR017996. Royal_jelly. IPR003534. Royal_jelly-related. [Graphical view]
PANTHER	PTHR10009. PTHR10009. 1 hit.
Pfam	PF03022. MRJP. 1 hit. [Graphical view]
PRINTS	PR01366. ROYALJELLY.
ProtoNet	Search...

Entry information

Entry name

MRJP1_APIME

Accession

Primary (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:	April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 3 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents