RBP_CHICK
ID RBP_CHICK Reviewed; 238 AA.
AC P02752; Q7T3Y1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Riboflavin-binding protein;
DE Short=RBP;
DE Contains:
DE RecName: Full=Riboflavin-binding protein, plasma form;
DE Contains:
DE RecName: Full=Riboflavin-binding protein, yolk major form;
DE Contains:
DE RecName: Full=Riboflavin-binding protein, yolk minor form;
DE Flags: Precursor;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3403518; DOI=10.1016/s0021-9258(18)37931-6;
RA Zheng D.B., Lim H.M., Pene J.J., White H.B. III;
RT "Chicken riboflavin-binding protein. cDNA sequence and homology with milk
RT folate-binding protein.";
RL J. Biol. Chem. 263:11126-11129(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8226844; DOI=10.1016/s0021-9258(19)49452-0;
RA MacLachlan I., Nimpf J., White H.B. III, Schneider W.J.;
RT "Riboflavinuria in the rd chicken. 5'-splice site mutation in the gene for
RT riboflavin-binding protein.";
RL J. Biol. Chem. 268:23222-23226(1993).
RN [3]
RP PROTEIN SEQUENCE OF 18-236, PYROGLUTAMATE FORMATION AT GLN-18, AND
RP PHOSPHORYLATION AT SER-212; SER-213 AND SER-214.
RC STRAIN=White leghorn; TISSUE=Egg white;
RX PubMed=6469943; DOI=10.1093/oxfordjournals.jbchem.a134776;
RA Hamazume Y., Mega T., Ikenaka T.;
RT "Characterization of hen egg white- and yolk-riboflavin binding proteins
RT and amino acid sequence of egg white-riboflavin binding protein.";
RL J. Biochem. 95:1633-1644(1984).
RN [4]
RP PROTEIN SEQUENCE.
RC STRAIN=White leghorn; TISSUE=Yolk;
RX PubMed=3997791; DOI=10.1093/oxfordjournals.jbchem.a135044;
RA Norioka N., Okada T., Hamazume Y., Mega T., Ikenaka T.;
RT "Comparison of the amino acid sequences of hen plasma-, yolk-, and white-
RT riboflavin binding proteins.";
RL J. Biochem. 97:19-28(1985).
RN [5]
RP DISULFIDE BONDS.
RC TISSUE=Egg white;
RX PubMed=3571203; DOI=10.1093/oxfordjournals.jbchem.a121894;
RA Hamazume Y., Mega T., Ikenaka T.;
RT "Positions of disulfide bonds in riboflavin-binding protein of hen egg
RT white.";
RL J. Biochem. 101:217-223(1987).
RN [6]
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=1637312; DOI=10.1042/bj2850275;
RA Rohrer J.S., White H.B. III;
RT "Separation and characterization of the two Asn-linked glycosylation sites
RT of chicken serum riboflavin-binding protein. Glycosylation differences
RT despite similarity of primary structure.";
RL Biochem. J. 285:275-280(1992).
RN [7]
RP PHOSPHORYLATION AT SER-204; SER-205; SER-208; SER-209 AND SER-210.
RX PubMed=4091257; DOI=10.1016/0003-2697(85)90515-9;
RA Fenselau C., Heller D.N., Miller M.S., White H.B. III;
RT "Phosphorylation sites in riboflavin-binding protein characterized by fast
RT atom bombardment mass spectrometry.";
RL Anal. Biochem. 150:309-314(1985).
CC -!- FUNCTION: Required for the transport of riboflavin to the developing
CC oocyte.
CC -!- TISSUE SPECIFICITY: Yolk RBP is synthesized in the liver; egg-white RBP
CC is synthesized in the oviduct.
CC -!- PTM: Plasma and yolk RBPS have the same carbohydrate components,
CC whereas egg-white RBP has a different, ovomucoid-type carbohydrate
CC chain.
CC -!- PTM: Plasma RBP has the same C-terminal sequence as the egg-white RBP,
CC which suggests that the C-terminal residues are cleaved off upon
CC incorporation into the oocyte.
CC -!- SIMILARITY: Belongs to the folate receptor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD44564.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J03922; AAA49056.1; -; mRNA.
DR EMBL; X74247; CAD44564.1; ALT_INIT; mRNA.
DR PIR; A29228; VOCH.
DR RefSeq; NP_990794.1; NM_205463.2.
DR RefSeq; XP_015146458.1; XM_015290972.1.
DR PDB; 6HCE; X-ray; 2.50 A; A=1-238.
DR PDBsum; 6HCE; -.
DR AlphaFoldDB; P02752; -.
DR SMR; P02752; -.
DR STRING; 9031.ENSGALP00000037592; -.
DR BindingDB; P02752; -.
DR ChEMBL; CHEMBL1944489; -.
DR DrugCentral; P02752; -.
DR Allergome; 10114; Gal d RfBP.
DR GlyConnect; 527; 42 N-Linked glycans (2 sites).
DR iPTMnet; P02752; -.
DR PaxDb; P02752; -.
DR GeneID; 396449; -.
DR KEGG; gga:396449; -.
DR CTD; 41880; -.
DR VEuPathDB; HostDB:geneid_396449; -.
DR eggNOG; ENOG502RYYP; Eukaryota.
DR HOGENOM; CLU_070826_2_0_1; -.
DR InParanoid; P02752; -.
DR OrthoDB; 1534387at2759; -.
DR PhylomeDB; P02752; -.
DR TreeFam; TF328532; -.
DR PRO; PR:P02752; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IBA:GO_Central.
DR GO; GO:1902444; F:riboflavin binding; IDA:AgBase.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:1904661; P:negative regulation of sensory perception of bitter taste; IMP:AgBase.
DR GO; GO:1904657; P:negative regulation of sensory perception of sweet taste; IMP:AgBase.
DR GO; GO:0032218; P:riboflavin transport; IDA: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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:6469943"
FT CHAIN 18..238
FT /note="Riboflavin-binding protein, plasma form"
FT /id="PRO_0000008811"
FT CHAIN 18..225
FT /note="Riboflavin-binding protein, yolk minor form"
FT /id="PRO_0000008812"
FT CHAIN 18..223
FT /note="Riboflavin-binding protein, yolk major form"
FT /id="PRO_0000008813"
FT MOD_RES 18
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:6469943"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:4091257"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:4091257"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:4091257"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:4091257"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:4091257"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:6469943"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:6469943"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:6469943"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /id="CAR_000059"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /id="CAR_000060"
FT DISULFID 22..49
FT /note="Or C-22 with C-50"
FT /evidence="ECO:0000269|PubMed:3571203"
FT DISULFID 41..90
FT /evidence="ECO:0000269|PubMed:3571203"
FT DISULFID 50..94
FT /note="Or C-49 with C-94"
FT /evidence="ECO:0000269|PubMed:3571203"
FT DISULFID 74..155
FT /evidence="ECO:0000269|PubMed:3571203"
FT DISULFID 81..127
FT /evidence="ECO:0000269|PubMed:3571203"
FT DISULFID 116..186
FT /evidence="ECO:0000269|PubMed:3571203"
FT DISULFID 120..169
FT /evidence="ECO:0000269|PubMed:3571203"
FT DISULFID 133..151
FT /evidence="ECO:0000269|PubMed:3571203"
FT DISULFID 184..219
FT /evidence="ECO:0000269|PubMed:3571203"
FT VARIANT 31
FT /note="N -> K (in 30% of egg-white and yolk)"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6HCE"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6HCE"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:6HCE"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:6HCE"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:6HCE"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6HCE"
FT HELIX 79..94
FT /evidence="ECO:0007829|PDB:6HCE"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:6HCE"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6HCE"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6HCE"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:6HCE"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6HCE"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:6HCE"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:6HCE"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6HCE"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:6HCE"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:6HCE"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6HCE"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6HCE"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:6HCE"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:6HCE"
FT HELIX 214..229
FT /evidence="ECO:0007829|PDB:6HCE"
SQ SEQUENCE 238 AA; 27211 MW; ACCC43F172116A08 CRC64;
MLRFAITLFA VITSSTCQQY GCLEGDTHKA NPSPEPNMHE CTLYSESSCC YANFTEQLAH
SPIIKVSNSY WNRCGQLSKS CEDFTKKIEC FYRCSPHAAR WIDPRYTAAI QSVPLCQSFC
DDWYEACKDD SICAHNWLTD WERDESGENH CKSKCVPYSE MYANGTDMCQ SMWGESFKVS
ESSCLCLQMN KKDMVAIKHL LSESSEESSS MSSSEEHACQ KKLLKFEALQ QEEGEERR
