YELL_DROGU
ID YELL_DROGU Reviewed; 568 AA.
AC Q9GP81;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Protein yellow;
DE Flags: Precursor;
GN Name=y;
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A;
RX PubMed=11110911; DOI=10.1093/oxfordjournals.molbev.a026296;
RA Munte A., Aguade M., Segarra C.;
RT "Nucleotide variation at the yellow gene region is not reduced in
RT Drosophila subobscura: a study in relation to chromosomal polymorphism.";
RL Mol. Biol. Evol. 17:1942-1955(2000).
CC -!- FUNCTION: Controls the pigmentation pattern of the adult cuticle and
CC larval mouth parts. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
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; AJ289813; CAC16215.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9GP81; -.
DR SMR; Q9GP81; -.
DR FlyBase; FBgn0043413; Dgua\y.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0060179; P:male mating behavior; IEA:InterPro.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:InterPro.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR017996; Royal_jelly/protein_yellow.
DR InterPro; IPR029846; Yellow.
DR PANTHER; PTHR10009; PTHR10009; 1.
DR PANTHER; PTHR10009:SF14; PTHR10009:SF14; 1.
DR Pfam; PF03022; MRJP; 1.
DR PRINTS; PR01366; ROYALJELLY.
PE 3: Inferred from homology;
KW Developmental protein; Glycoprotein; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..568
FT /note="Protein yellow"
FT /id="PRO_0000031049"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 568 AA; 62624 MW; 4FDB9AC2B3B846D1 CRC64;
MHAQDKGGVL PGLSLLLIAV AMVCPSQAAY KLQERYSWNQ LDFAFPSARL KEQALASGDY
IPTNALPVGV EHFGNRLFVT VPRWRDGIPA TLTYINMDHS VTGSPELIPY PDWRANTAGD
CSNSITTAYR IKVDECGRLW VLDTGTVGIG NTTTNPCPYA INIFDLTTNT RIRRYELPAA
DTNPNTFIAN IAVDIGKNCD DAFAYFADEL GYGLISYSWE LNKSWRFSAH SYFFPDPLRG
DFNVAGINFQ WGEEGIFGMS LTPIRSDGYR TLYFSPLASH RQFAVSTRIL RDETRTEDSY
HDFVALDERG PNAHTTSRVM SDDGVELFNL IDQNAVGCWH SSMPYSPQFH GIVDRDDVGL
VFPADVKIDE NKNVWVLSDR MPVFLLSDLD YSDTNFRIYT APLATLIENT VCDLRNNAYG
PPNTVSIPKQ AAPGHSAVGP PLYTTTNQYR PVLSQKPQTS WGPSPPSRNY LPALNGNPGI
PGSLSKLNNL GAPGQVVSSV SVSTNTVGPS GIEVPKAYVF NQHNGLNYET SGPHLFPTLQ
PAPSQLGGGL KTYVNARQSG WWHHQQQG