ID   RBP_DRONO               Reviewed;         238 AA.
AC   P86009; B9A1T1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Riboflavin-binding protein {ECO:0000303|PubMed:19416692, ECO:0000312|EMBL:BAH22358.1};
DE            Short=RBP {ECO:0000250|UniProtKB:P02752};
DE   Flags: Precursor;
OS   Dromaius novaehollandiae (Emu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Casuariiformes; Dromaiidae; Dromaius.
OX   NCBI_TaxID=8790;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 18-44, TISSUE
RP   SPECIFICITY, AND GLYCOSYLATION.
RC   TISSUE=Egg yolk, and Oviduct;
RX   PubMed=19416692; DOI=10.1016/j.cbpb.2009.02.004;
RA   Maehashi K., Matano M., Uchino M., Yamamoto Y., Takano K., Watanabe T.;
RT   "The primary structure of a novel riboflavin-binding protein of emu
RT   (Dromaius novaehollandiae).";
RL   Comp. Biochem. Physiol. 153:95-100(2009).
CC   -!- FUNCTION: Required for the transport of riboflavin to the developing
CC       oocyte. {ECO:0000250|UniProtKB:P02752}.
CC   -!- TISSUE SPECIFICITY: Expressed in egg yolk and egg white (at protein
CC       level). {ECO:0000269|PubMed:19416692}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19416692}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined MW is: 47 kDa.
CC       {ECO:0000269|PubMed:19416692}.
CC   -!- SIMILARITY: Belongs to the folate receptor family. {ECO:0000255}.
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DR   EMBL; AB440148; BAH22358.1; -; mRNA.
DR   EMBL; AB469328; BAH22359.1; -; Genomic_DNA.
DR   AlphaFoldDB; P86009; -.
DR   SMR; P86009; -.
DR   Ensembl; ENSDNVT00000015924; ENSDNVP00000013216; ENSDNVG00000009354.
DR   GO; GO:0032217; F:riboflavin transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0032218; P:riboflavin transport; ISS:UniProtKB.
DR   InterPro; IPR004269; Folate_rcpt.
DR   InterPro; IPR018143; Folate_rcpt-like.
DR   PANTHER; PTHR10517; PTHR10517; 1.
DR   Pfam; PF03024; Folate_rec; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Phosphoprotein;
KW   Signal; Transport.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:19416692"
FT   CHAIN           18..238
FT                   /note="Riboflavin-binding protein"
FT                   /evidence="ECO:0000269|PubMed:19416692"
FT                   /id="PRO_5000434275"
FT   MOD_RES         204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   MOD_RES         209
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   MOD_RES         212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        22..49
FT                   /note="Or C-22 with C-50"
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   DISULFID        41..90
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   DISULFID        50..94
FT                   /note="Or C-49 with C-94"
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   DISULFID        74..155
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   DISULFID        81..127
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   DISULFID        116..186
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   DISULFID        120..169
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   DISULFID        133..151
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
FT   DISULFID        184..219
FT                   /evidence="ECO:0000250|UniProtKB:P02752"
SQ   SEQUENCE   238 AA;  27344 MW;  CF182BA48B89DFDA CRC64;
     MLRFAVTLFA VITSSTCKKY SCLEGETHKL KPSPEPNMQE CTLYSESSCC YANFTEQLAH
     SPVIKINNSY WNRCGQLSKS CEDFTKKIEC FYRCSPHAAH WIHPNYTAGI QSVPLCQSFC
     DDWYEACKDD SACVRNWLMD WEWDESGVNH CKNECIPYSE MYVNGTDMCQ SMWGESFKVS
     ESSCLCLQMN KKDMMAIKYL LSESSEESSS VSSSEERACQ KKLLKFEKLK EEEGGETR