MRJP2_APIME
ID MRJP2_APIME Reviewed; 452 AA.
AC O77061; C6K482;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Major royal jelly protein 2;
DE Short=MRJP-2;
DE AltName: Full=55 kDa RJGP {ECO:0000303|PubMed:8988648};
DE AltName: Full=Apalbumin 2 {ECO:0000305};
DE AltName: Full=Bee-milk protein;
DE Flags: Precursor;
GN Name=MRJP2;
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 18-30, 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yoon B.S., Nguyen K.T.;
RT "Cloning whole encoding region of major royal jelly protein 2 (MRJP2) from
RT Apis mellifera.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=8988648; DOI=10.1271/bbb.60.2099;
RA Kimura Y., Kajiyama S., Kanaeda J., Izukawa T., Yonekura M.;
RT "N-linked sugar chain of 55-kDa royal jelly glycoprotein.";
RL Biosci. Biotechnol. Biochem. 60:2099-2102(1996).
CC -!- FUNCTION: May play an important role in honeybee nutrition. It is found
CC in the royal jelly which is the food of the queen honey bee larva. The
CC royal jelly determines the development of the young larvae and is
CC responsible for the high reproductive ability of the honeybee queen.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9791542}. Note=Royal
CC jelly. {ECO:0000269|PubMed:9791542}.
CC -!- TISSUE SPECIFICITY: Found in the hypopharyngeal glands.
CC -!- DEVELOPMENTAL STAGE: Produced in the cephalic glands of the nurse
CC honeybee.
CC -!- PTM: N-linked core structure contains mannose (which consists of 8-
CC alpha-mannosyl residues, one beta-mannosyl residue, and chitobiose).
CC {ECO:0000305|PubMed:8988648}.
CC -!- SIMILARITY: Belongs to the major royal jelly protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF000632; AAC61894.1; -; mRNA.
DR EMBL; GQ160519; ACS66837.1; -; mRNA.
DR RefSeq; NP_001011580.1; NM_001011580.1.
DR AlphaFoldDB; O77061; -.
DR SMR; O77061; -.
DR STRING; 7460.GB55212-PA; -.
DR Allergome; 7628; Api m Apalbumin 2.
DR PaxDb; O77061; -.
DR EnsemblMetazoa; NM_001011580; NP_001011580; GeneID_406091.
DR GeneID; 406091; -.
DR KEGG; ame:406091; -.
DR CTD; 406091; -.
DR eggNOG; ENOG502SCJK; Eukaryota.
DR InParanoid; O77061; -.
DR PhylomeDB; O77061; -.
DR Proteomes; UP000005203; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Secreted;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:9791542"
FT CHAIN 18..452
FT /note="Major royal jelly protein 2"
FT /id="PRO_0000031044"
FT REGION 416..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 452 AA; 51074 MW; 25E5B621288FE189 CRC64;
MTRWLFMVAC LGIACQGAIV RENSPRNLEK SLNVIHEWKY FDYDFGSEER RQAAIQSGEY
DHTKNYPFDV DQWRDKTFVT ILRYDGVPST LNVISGKTGK GGRLLKPYPD WSFAEFKDCS
KIVSAFKIAI DKFDRLWVLD SGLVNRTVPV CAPKLHVFDL KTSNHLKQIE IPHDIAVNAT
TGKGGLVSLA VQAIDLANTL VYMADHKGDA LIVYQNADDS FHRLTSNTFD YDPRYAKMTI
DGESFTLKNG ICGMALSPVT NNLYYSPLAS HGLYYVNTAP FMKSQFGENN VQYQGSEDIL
NTQSLAKAVS KNGVLFVGLV GNSAVGCWNE HQSLQRQNLE MVAQNDRTLQ MIAGMKIKEE
LPHFVGSNKP VKDEYMLVLS NRMQKIVNDD FNFDDVNFRI LGANVKELIR NTHCVNNNQN
DNIQNTNNQN DNNQKNNKKN ANNQKNNNQN DN