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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}.
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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
 
 
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