MRJP3_APIME
ID MRJP3_APIME Reviewed; 544 AA.
AC Q17060;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Major royal jelly protein 3 {ECO:0000303|PubMed:9791542};
DE Short=MRJP-3 {ECO:0000303|PubMed:9791542};
DE AltName: Full=Bee-milk protein {ECO:0000303|PubMed:9395329};
DE AltName: Full=Royal jelly protein RJP57-1 {ECO:0000303|Ref.1, ECO:0000303|Ref.2};
DE Flags: Precursor;
GN Name=MRJP3 {ECO:0000303|PubMed:9791542};
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].
RC TISSUE=Head;
RX AGRICOLA=IND20437271;
RA Klaudiny J., Hanes J., Kulifajova J., Albert S., Simuth J.;
RT "Molecular cloning of two cDNAs from the head of the nurse honey bee (Apis
RT mellifera L.) for coding related proteins of royal jelly.";
RL J. Apic. Res. 33:105-111(1994).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RX AGRICOLA=IND20554548;
RA Albert S., Klaudiny J., Simuth J.;
RT "Newly discovered features of the updated sequence of royal jelly protein
RT RJP571; longer repetitive region on C-terminus and homology to Drosophila
RT melanogaster yellow protein.";
RL J. Apic. Res. 35:63-68(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-36, AND SUBCELLULAR
RP LOCATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 45-59; 70-77; 106-120;
RP 214-224 AND 243-253.
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 [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=31051140; DOI=10.1016/j.molcel.2019.03.010;
RA Maori E., Navarro I.C., Boncristiani H., Seilly D.J., Rudolph K.L.M.,
RA Sapetschnig A., Lin C.C., Ladbury J.E., Evans J.D., Heeney J.L.,
RA Miska E.A.;
RT "A secreted RNA binding protein forms RNA-stabilizing granules in the
RT honeybee royal jelly.";
RL Mol. Cell 74:598-608(2019).
CC -!- FUNCTION: Secreted RNA-binding protein required to concentrate,
CC stabilize and enhance environmental RNA bioavailability in the honeybee
CC royal jelly (PubMed:31051140). Acts as a RNA-aggregating protein: binds
CC 18 nucleotides and longer single- and double-stranded RNA (ssRNA and
CC dsRNA, respectively) in a non-specific manner (PubMed:31051140). RNA-
CC binding drives super-order assembly of oligomers into extracellular
CC ribonucleoprotein granules that concentrate, protect and enhance RNA
CC uptake granules, facilitating RNA transfer among bees
CC (PubMed:31051140). {ECO:0000269|PubMed:31051140}.
CC -!- SUBUNIT: Homoligomer; in the absence of RNA, assembles into a higher-
CC order oligomeric form, composed of around 20 monomer units.
CC {ECO:0000269|PubMed:31051140}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9791542}.
CC -!- TISSUE SPECIFICITY: Hypopharyngeal glands of nurse honey bees.
CC {ECO:0000269|PubMed:9791542}.
CC -!- DEVELOPMENTAL STAGE: Produced by the cephalic glandular system of the
CC nurse honey bee. {ECO:0000269|PubMed:9791542}.
CC -!- SIMILARITY: Belongs to the major royal jelly protein family.
CC {ECO:0000305}.
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DR EMBL; Z26318; CAA81227.1; -; mRNA.
DR PIR; S39193; S39193.
DR RefSeq; NP_001011601.1; NM_001011601.1.
DR AlphaFoldDB; Q17060; -.
DR SMR; Q17060; -.
DR STRING; 7460.GB55204-PA; -.
DR PaxDb; Q17060; -.
DR PRIDE; Q17060; -.
DR EnsemblMetazoa; NM_001011601; NP_001011601; GeneID_406121.
DR GeneID; 406121; -.
DR KEGG; ame:406121; -.
DR CTD; 406121; -.
DR eggNOG; ENOG502SCJK; Eukaryota.
DR InParanoid; Q17060; -.
DR OrthoDB; 940689at2759; -.
DR PhylomeDB; Q17060; -.
DR Proteomes; UP000005203; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
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 Direct protein sequencing; Glycoprotein; Reference proteome; Repeat;
KW RNA-binding; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:9791542"
FT CHAIN 21..544
FT /note="Major royal jelly protein 3"
FT /id="PRO_0000031045"
FT REPEAT 424..428
FT /note="1"
FT REPEAT 429..433
FT /note="2"
FT REPEAT 434..438
FT /note="3"
FT REPEAT 439..443
FT /note="4"
FT REPEAT 444..448
FT /note="5"
FT REPEAT 449..453
FT /note="6"
FT REPEAT 454..458
FT /note="7"
FT REPEAT 459..463
FT /note="8"
FT REPEAT 464..468
FT /note="9"
FT REPEAT 469..473
FT /note="10"
FT REPEAT 474..478
FT /note="11"
FT REPEAT 479..483
FT /note="12"
FT REPEAT 484..488
FT /note="13"
FT REPEAT 489..493
FT /note="14"
FT REPEAT 494..498
FT /note="15"
FT REPEAT 499..503
FT /note="16"
FT REPEAT 504..508
FT /note="17"
FT REPEAT 509..513
FT /note="18"
FT REPEAT 514..518
FT /note="19"
FT REPEAT 519..523
FT /note="20"
FT REGION 421..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..523
FT /note="20 X 5 AA tandem repeats of [NKR]-Q-N-[AGD]-[DNG]"
FT COMPBIAS 421..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 544 AA; 61662 MW; 4C8FFFC8A2759F52 CRC64;
MTKWLLLVVC LGIACQDVTS AAVNHQRKSA NNLAHSMKVI YEWKHIDFDF GSDERRDAAI
KSGEFDHTKN YPFDVDRWRD KTFVTIERNN GVPSSLNVVT NKKGKGGPLL RPYPDWSFAK
YEDCSGIVSA FKIAVDKFDR LWVLDSGLVN NNQPMCSPKL LTFDLKTSKL VKQVEIPHNI
AVNATTGMGE LVSLAVQAID RTNTMVYIAD EKGEGLIMYQ NSDDSFHRLT SNTFDYDPRY
TKLTVAGESF TVKNGIYGIA LSPVTNNLYY SPLLSHGLYY VDTEQFSNPQ YEENNVQYEG
SQDILNTQSF GKVVSKNGVL FLGLVGNSGI ACVNEHQVLQ RESFDVVAQN EETLQMIVSM
KIMENLPQSG RINDPEGNEY MLALSNRMQK IINNDFNFND VNFRILGANV DDLMRNTRCG
RYHNQNAGNQ NADNQNADNQ NANNQNADNQ NANKQNGNRQ NDNRQNDNKQ NGNRQNDNKQ
NGNRQNDNKQ NGNRQNGNKQ NDNKQNGNRQ NDNKRNGNRQ NDNQNNQNDN NRNDNQVHHS
SKLH
