MRJP1_APIME
ID MRJP1_APIME Reviewed; 432 AA.
AC O18330; C6K481; Q548D6;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Major royal jelly protein 1 {ECO:0000303|PubMed:9791542};
DE Short=MRJP-1;
DE Short=MRJP1 {ECO:0000303|PubMed:12559578, ECO:0000303|PubMed:9791542};
DE AltName: Full=56-kDa protein 4 {ECO:0000303|PubMed:9395329};
DE Short=p56kP-4 {ECO:0000303|PubMed:9395329};
DE AltName: Full=Apalbumin 1 {ECO:0000305};
DE AltName: Full=Apisin subunit MRJP1 {ECO:0000303|PubMed:27721892};
DE AltName: Full=Bee-milk protein {ECO:0000303|PubMed:9395329};
DE AltName: Full=Royalactin {ECO:0000303|PubMed:21516106};
DE Contains:
DE RecName: Full=Jellein-1 {ECO:0000305};
DE AltName: Full=Jelleine-I {ECO:0000303|PubMed:15203237};
DE Contains:
DE RecName: Full=Jellein-2 {ECO:0000305};
DE AltName: Full=Jelleine-II {ECO:0000303|PubMed:15203237};
DE Contains:
DE RecName: Full=Jellein-4 {ECO:0000305};
DE AltName: Full=Jelleine-IV {ECO:0000303|PubMed:15203237};
DE Flags: Precursor;
GN Name=MRJP1;
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7460;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-48; 63-71 AND 361-380,
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND GLYCOSYLATION.
RC TISSUE=Hypopharyngeal gland;
RX PubMed=9395329; DOI=10.1111/j.1432-1033.1997.t01-1-00797.x;
RA Ohashi K., Natori S., Kubo T.;
RT "Change in the mode of gene expression of the hypopharyngeal gland cells
RT with an age-dependent role change of the worker honeybee Apis mellifera
RT L.";
RL Eur. J. Biochem. 249:797-802(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-30.
RC TISSUE=Head;
RX PubMed=9791542; DOI=10.1007/s000180050229;
RA Schmitzova J., Klaudiny J., Albert S., Schroeder W., Schreckengost W.,
RA Hanes J., Judova J., Simuth J.;
RT "A family of major royal jelly proteins of the honeybee Apis mellifera L.";
RL Cell. Mol. Life Sci. 54:1020-1030(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12559578; DOI=10.1016/s0378-1119(02)01174-5;
RA Malecova B., Ramser J., O'Brien J.K., Janitz M., Judova J., Lehrach H.,
RA Simuth J.;
RT "Honeybee (Apis mellifera L.) mrjp gene family: computational analysis of
RT putative promoters and genomic structure of mrjp1, the gene coding for the
RT most abundant protein of larval food.";
RL Gene 303:165-175(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yoon B.S., Nguyen K.T.;
RT "Cloning, expression and monoclonal antibody generation of major royal
RT jelly protein 1 (MJRP1) from Apis mellifera.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 20-34.
RX PubMed=11302159; DOI=10.1271/bbb.65.277;
RA Kamakura M., Fukuda T., Fukushima M., Yonekura M.;
RT "Storage-dependent degradation of 57-kDa protein in royal jelly: a possible
RT marker for freshness.";
RL Biosci. Biotechnol. Biochem. 65:277-284(2001).
RN [6]
RP PROTEIN SEQUENCE OF 424-432, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, AND AMIDATION AT HIS-431 AND LEU-432.
RX PubMed=15203237; DOI=10.1016/j.peptides.2004.03.016;
RA Fontana R., Mendes M.A., de Souza B.M., Konno K., Cesar L.M., Malaspina O.,
RA Palma M.S.;
RT "Jelleines: a family of antimicrobial peptides from the royal jelly of
RT honeybees (Apis mellifera).";
RL Peptides 25:919-928(2004).
RN [7]
RP SUBUNIT.
RA Simuth J.;
RT "Some properties of the main protein of honeybee (Apis mellifera) royal
RT jelly.";
RL Apidologie 32:69-80(2001).
RN [8]
RP IDENTIFICATION.
RX PubMed=16290177; DOI=10.1016/j.pep.2005.08.004;
RA Kamakura M., Sakaki T.;
RT "A hypopharyngeal gland protein of the worker honeybee Apis mellifera L.
RT enhances proliferation of primary-cultured rat hepatocytes and suppresses
RT apoptosis in the absence of serum.";
RL Protein Expr. Purif. 45:307-314(2006).
RN [9]
RP FUNCTION.
RX PubMed=21516106; DOI=10.1038/nature10093;
RA Kamakura M.;
RT "Royalactin induces queen differentiation in honeybees.";
RL Nature 473:478-483(2011).
RN [10]
RP SUBUNIT.
RX PubMed=27721892; DOI=10.1155/2016/5040528;
RA Furusawa T., Arai Y., Kato K., Ichihara K.;
RT "Quantitative analysis of apisin, a major protein unique to royal jelly.";
RL Evid. Based Complement Alternat. Med. 2016:5040528-5040528(2016).
CC -!- FUNCTION: [Major royal jelly protein 1]: Induces the differentiation of
CC honeybee larvae into queens through an Egfr-mediated signaling pathway.
CC Promotes body size increase by activating p70 S6 kinase, stimulates
CC ovary development by augmenting the titer of vitellogenin (Vg) and
CC juvenile hormone, and reduces developmental time by increasing the
CC activity of mitogen-activated protein kinase and inducing the 20-
CC hydroxyecdysone protein (20E). Most abundant protein found in the royal
CC jelly which is the food of the queen honey bee larva. The royal jelly
CC determines the development of the young larvae and is responsible for
CC the high reproductive ability of the honeybee queen.
CC {ECO:0000269|PubMed:21516106}.
CC -!- FUNCTION: [Jellein-1]: Has antibacterial activity against the Gram-
CC positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis
CC CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC
CC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and
CC antifungal activity against C.albicans. Lack cytolytic activity and
CC does not induce rat peritoneal mast cell degranulation.
CC {ECO:0000269|PubMed:15203237}.
CC -!- FUNCTION: [Jellein-2]: Has antibacterial activity against the Gram-
CC positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis
CC CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC
CC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and
CC antifungal activity against C.albicans. Lack cytolytic activity and
CC does not induce rat peritoneal mast cell degranulation.
CC {ECO:0000269|PubMed:15203237}.
CC -!- FUNCTION: [Jellein-4]: Lacks antibacterial and antifungal activity.
CC Lacks cytolytic activity and does not induce rat peritoneal mast cell
CC degranulation. {ECO:0000269|PubMed:15203237}.
CC -!- SUBUNIT: Is present in royal jelly in different forms: monomer (55
CC kDa), oligomeric subunit (ca. 420 kDa), and water-insoluble aggregates
CC in sediment after interaction with fatty acids (Ref.7). Interacts with
CC apisimin to form the heterooligomer apisin (350 kDa) (PubMed:27721892).
CC {ECO:0000269|PubMed:27721892, ECO:0000269|Ref.7}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15203237,
CC ECO:0000269|PubMed:9395329}. Note=Royal jelly.
CC {ECO:0000269|PubMed:9395329}.
CC -!- TISSUE SPECIFICITY: Found in the hypopharyngeal glands of the worker
CC honeybee. {ECO:0000269|PubMed:15203237, ECO:0000269|PubMed:9395329}.
CC -!- DEVELOPMENTAL STAGE: Produced in the cephalic glands of both the nurse
CC bee and the forager bee. This bee milk protein changes to alpha-
CC glucosidase in accordance with the age-dependent role change of the
CC worker bee. {ECO:0000269|PubMed:9395329}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:9395329}.
CC -!- PTM: Jellein-2 is probably processed to yield jellein-1 and jellein-4.
CC -!- MASS SPECTROMETRY: [Jellein-1]: Mass=953.24; Mass_error=0.17;
CC Method=Electrospray; Note=Jellein-1.;
CC Evidence={ECO:0000269|PubMed:15203237};
CC -!- MASS SPECTROMETRY: [Jellein-2]: Mass=1054.30; Mass_error=0.18;
CC Method=Electrospray; Note=Jellein-2.;
CC Evidence={ECO:0000269|PubMed:15203237};
CC -!- MASS SPECTROMETRY: [Jellein-4]: Mass=942.13; Mass_error=0.17;
CC Method=Electrospray; Note=Jellein-4.;
CC Evidence={ECO:0000269|PubMed:15203237};
CC -!- MISCELLANEOUS: Exhibits a growth factor-like action on primary-cultured
CC rat hepatocytes by stimulating DNA synthesis and protecting cells from
CC apoptosis induced by serum deprivation. Also activates mitogen-
CC activated protein kinase, as well as protein kinase B, a key regulator
CC of cell survival (PubMed:16290177). {ECO:0000305|PubMed:16290177}.
CC -!- MISCELLANEOUS: Degraded proportionally to the period of storage, and is
CC completely lost during storage at 40 degrees Celsius for 30 days.
CC {ECO:0000305|PubMed:21516106}.
CC -!- SIMILARITY: Belongs to the major royal jelly protein family.
CC {ECO:0000305}.
CC -!- CAUTION: Neither His-431 nor Leu-432 is followed in the nucleotide
CC sequence by the expected Gly residue that would be required to produce
CC amidation. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A queen's dinner - Issue 130
CC of August 2011;
CC URL="https://web.expasy.org/spotlight/back_issues/130";
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DR EMBL; D79207; BAA23639.1; -; mRNA.
DR EMBL; AF000633; AAC61895.1; -; mRNA.
DR EMBL; AF388203; AAM73637.1; -; Genomic_DNA.
DR EMBL; GQ160518; ACS66836.1; -; mRNA.
DR RefSeq; NP_001011579.1; NM_001011579.1.
DR PDB; 5YYL; X-ray; 2.65 A; A/B=1-432.
DR PDB; 7ASD; EM; 3.50 A; AA/BA/CA/DA/EA/FA/GA/HA=1-432.
DR PDBsum; 5YYL; -.
DR PDBsum; 7ASD; -.
DR AlphaFoldDB; O18330; -.
DR SMR; O18330; -.
DR STRING; 7460.GB55205-PA; -.
DR Allergome; 7627; Api m Apalbumin 1.
DR GlyConnect; 2; 4 N-Linked glycans.
DR PaxDb; O18330; -.
DR EnsemblMetazoa; NM_001011579; NP_001011579; GeneID_406090.
DR GeneID; 406090; -.
DR KEGG; ame:406090; -.
DR CTD; 406090; -.
DR eggNOG; ENOG502SCJK; Eukaryota.
DR HOGENOM; CLU_031076_2_1_1; -.
DR InParanoid; O18330; -.
DR OMA; SIMCADA; -.
DR OrthoDB; 940689at2759; -.
DR PhylomeDB; O18330; -.
DR Proteomes; UP000005203; Unplaced.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0048650; P:caste determination, influence by environmental factors; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR017996; Royal_jelly/protein_yellow.
DR PANTHER; PTHR10009; PTHR10009; 1.
DR Pfam; PF03022; MRJP; 1.
DR PRINTS; PR01366; ROYALJELLY.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Antibiotic; Antimicrobial; Developmental protein;
KW Direct protein sequencing; Fungicide; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:11302159,
FT ECO:0000269|PubMed:9791542"
FT CHAIN 20..432
FT /note="Major royal jelly protein 1"
FT /evidence="ECO:0000305|PubMed:9395329,
FT ECO:0000305|PubMed:9791542"
FT /id="PRO_0000031043"
FT PEPTIDE 424..432
FT /note="Jellein-2"
FT /evidence="ECO:0000269|PubMed:15203237"
FT /id="PRO_0000224649"
FT PEPTIDE 424..431
FT /note="Jellein-4"
FT /evidence="ECO:0000269|PubMed:15203237"
FT /id="PRO_0000224650"
FT PEPTIDE 425..432
FT /note="Jellein-1"
FT /evidence="ECO:0000269|PubMed:15203237"
FT /id="PRO_0000224648"
FT MOD_RES 431
FT /note="Histidine amide; atypical"
FT /evidence="ECO:0000269|PubMed:15203237"
FT MOD_RES 432
FT /note="Leucine amide; atypical"
FT /evidence="ECO:0000269|PubMed:15203237"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 28
FT /note="N -> L (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="S -> K (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:5YYL"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:5YYL"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 99..108
FT /evidence="ECO:0007829|PDB:5YYL"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:5YYL"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:5YYL"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:5YYL"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:5YYL"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:5YYL"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:5YYL"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:5YYL"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:5YYL"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:5YYL"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:5YYL"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:5YYL"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:5YYL"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:5YYL"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 352..361
FT /evidence="ECO:0007829|PDB:5YYL"
FT HELIX 367..372
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 376..383
FT /evidence="ECO:0007829|PDB:5YYL"
FT HELIX 385..389
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 400..406
FT /evidence="ECO:0007829|PDB:5YYL"
FT HELIX 407..411
FT /evidence="ECO:0007829|PDB:5YYL"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:5YYL"
SQ SEQUENCE 432 AA; 48886 MW; 9F42BF08D34A1A7B CRC64;
MTRLFMLVCL GIVCQGTTGN ILRGESLNKS LPILHEWKFF DYDFGSDERR QDAILSGEYD
YKNNYPSDID QWHDKIFVTM LRYNGVPSSL NVISKKVGDG GPLLQPYPDW SFAKYDDCSG
IVSASKLAID KCDRLWVLDS GLVNNTQPMC SPKLLTFDLT TSQLLKQVEI PHDVAVNATT
GKGRLSSLAV QSLDCNTNSD TMVYIADEKG EGLIVYHNSD DSFHRLTSNT FDYDPKFTKM
TIDGESYTAQ DGISGMALSP MTNNLYYSPV ASTSLYYVNT EQFRTSDYQQ NDIHYEGVQN
ILDTQSSAKV VSKSGVLFFG LVGDSALGCW NEHRTLERHN IRTVAQSDET LQMIASMKIK
EALPHVPIFD RYINREYILV LSNKMQKMVN NDFNFDDVNF RIMNANVNEL ILNTRCENPD
NDRTPFKISI HL
