RET4_BOVIN
ID RET4_BOVIN Reviewed; 183 AA.
AC P18902;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Retinol-binding protein 4;
DE AltName: Full=Plasma retinol-binding protein;
DE Short=PRBP;
DE Short=RBP {ECO:0000303|PubMed:17255476};
GN Name=RBP4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE, CRYSTALLIZATION, INTERACTION WITH TTR, FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=2209607; DOI=10.1111/j.1432-1033.1990.tb19254.x;
RA Berni R., Stoppini M., Zapponi M.C., Meloni M.L., Monaco H.L., Zanotti G.;
RT "The bovine plasma retinol-binding protein. Amino acid sequence,
RT interaction with transthyretin, crystallization and preliminary X-ray
RT data.";
RL Eur. J. Biochem. 192:507-513(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-183.
RX PubMed=8373966; DOI=10.1095/biolreprod49.2.393;
RA Liu K.H., Dore J.J. Jr., Roberts M.P., Krishnan R., Hopkins F.M.,
RA Godkin J.D.;
RT "Expression and cellular localization of retinol-binding protein messenger
RT ribonucleic acid in bovine blastocysts and extraembryonic membranes.";
RL Biol. Reprod. 49:393-400(1993).
RN [3]
RP INTERACTION WITH STRA6, AND FUNCTION.
RX PubMed=17255476; DOI=10.1126/science.1136244;
RA Kawaguchi R., Yu J., Honda J., Hu J., Whitelegge J., Ping P., Wiita P.,
RA Bok D., Sun H.;
RT "A membrane receptor for retinol binding protein mediates cellular uptake
RT of vitamin A.";
RL Science 315:820-825(2007).
RN [4]
RP INTERACTION WITH STRA6, AND FUNCTION.
RX PubMed=18419130; DOI=10.1021/bi8002082;
RA Kawaguchi R., Yu J., Wiita P., Ter-Stepanian M., Sun H.;
RT "Mapping the membrane topology and extracellular ligand binding domains of
RT the retinol binding protein receptor.";
RL Biochemistry 47:5387-5395(2008).
RN [5]
RP COMPARISON OF X-RAY STRUCTURES.
RX PubMed=1623143; DOI=10.1002/bip.360320425;
RA Monaco H.L., Zanotti G.;
RT "Three-dimensional structure and active site of three hydrophobic molecule-
RT binding proteins with significant amino acid sequence similarity.";
RL Biopolymers 32:457-465(1992).
RN [6] {ECO:0007744|PDB:1HBP, ECO:0007744|PDB:1HBQ}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), SUBCELLULAR LOCATION, AND DISULFIDE
RP BONDS.
RX PubMed=8496140; DOI=10.1016/s0021-9258(18)82046-4;
RA Zanotti G., Berni R., Monaco H.L.;
RT "Crystal structure of liganded and unliganded forms of bovine plasma
RT retinol-binding protein.";
RL J. Biol. Chem. 268:10728-10738(1993).
RN [7] {ECO:0007744|PDB:1KT3, ECO:0007744|PDB:1KT4, ECO:0007744|PDB:1KT5, ECO:0007744|PDB:1KT6, ECO:0007744|PDB:1KT7}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH RETINOL, SUBCELLULAR
RP LOCATION, AND DISULFIDE BONDS.
RX PubMed=12787682; DOI=10.1016/s0022-2836(03)00468-6;
RA Calderone V., Berni R., Zanotti G.;
RT "High-resolution structures of retinol-binding protein in complex with
RT retinol: pH-induced protein structural changes in the crystal state.";
RL J. Mol. Biol. 329:841-850(2003).
CC -!- FUNCTION: Retinol-binding protein that mediates retinol transport in
CC blood plasma. Delivers retinol from the liver stores to the peripheral
CC tissues. Transfers the bound all-trans retinol to STRA6, that then
CC facilitates retinol transport across the cell membrane.
CC {ECO:0000269|PubMed:17255476, ECO:0000269|PubMed:18419130,
CC ECO:0000305|PubMed:2209607}.
CC -!- SUBUNIT: Interacts with TTR (PubMed:2209607). Interaction with TTR
CC prevents its loss by filtration through the kidney glomeruli
CC (Probable). Interacts with STRA6 (PubMed:17255476, PubMed:18419130).
CC {ECO:0000269|PubMed:17255476, ECO:0000269|PubMed:18419130,
CC ECO:0000269|PubMed:2209607, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12787682,
CC ECO:0000269|PubMed:2209607, ECO:0000269|PubMed:8496140}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level).
CC {ECO:0000269|PubMed:2209607}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; S65585; AAB28336.1; -; mRNA.
DR PIR; I46955; I46955.
DR PIR; S13186; S13186.
DR PDB; 1ERB; X-ray; 1.90 A; A=1-183.
DR PDB; 1FEL; X-ray; 1.80 A; A=1-183.
DR PDB; 1FEM; X-ray; 1.90 A; A=1-183.
DR PDB; 1FEN; X-ray; 1.90 A; A=1-183.
DR PDB; 1HBP; X-ray; 1.90 A; A=1-183.
DR PDB; 1HBQ; X-ray; 1.70 A; A=1-183.
DR PDB; 1KT3; X-ray; 1.40 A; A=1-183.
DR PDB; 1KT4; X-ray; 1.46 A; A=1-183.
DR PDB; 1KT5; X-ray; 1.46 A; A=1-175.
DR PDB; 1KT6; X-ray; 1.10 A; A=1-183.
DR PDB; 1KT7; X-ray; 1.27 A; A=1-183.
DR PDBsum; 1ERB; -.
DR PDBsum; 1FEL; -.
DR PDBsum; 1FEM; -.
DR PDBsum; 1FEN; -.
DR PDBsum; 1HBP; -.
DR PDBsum; 1HBQ; -.
DR PDBsum; 1KT3; -.
DR PDBsum; 1KT4; -.
DR PDBsum; 1KT5; -.
DR PDBsum; 1KT6; -.
DR PDBsum; 1KT7; -.
DR AlphaFoldDB; P18902; -.
DR SMR; P18902; -.
DR STRING; 9913.ENSBTAP00000000566; -.
DR PaxDb; P18902; -.
DR PeptideAtlas; P18902; -.
DR PRIDE; P18902; -.
DR eggNOG; ENOG502RXEW; Eukaryota.
DR HOGENOM; CLU_094618_0_0_1; -.
DR InParanoid; P18902; -.
DR EvolutionaryTrace; P18902; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
DR GO; GO:0019841; F:retinol binding; IDA:UniProtKB.
DR GO; GO:0034632; F:retinol transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0034633; P:retinol transport; IBA:GO_Central.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR022271; Lipocalin_ApoD.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR002449; Retinol-bd/Purpurin.
DR PANTHER; PTHR11873; PTHR11873; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR PIRSF; PIRSF500204; RBP_purpurin; 1.
DR PRINTS; PR01174; RETINOLBNDNG.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Methylation;
KW Reference proteome; Retinol-binding; Secreted; Transport; Vitamin A.
FT CHAIN 1..183
FT /note="Retinol-binding protein 4"
FT /id="PRO_0000201028"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12787682,
FT ECO:0007744|PDB:1KT3, ECO:0007744|PDB:1KT4,
FT ECO:0007744|PDB:1KT5, ECO:0007744|PDB:1KT6,
FT ECO:0007744|PDB:1KT7"
FT MOD_RES 121
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q00724"
FT DISULFID 4..160
FT /evidence="ECO:0000269|PubMed:12787682,
FT ECO:0000269|PubMed:8496140, ECO:0007744|PDB:1HBP,
FT ECO:0007744|PDB:1HBQ, ECO:0007744|PDB:1KT3,
FT ECO:0007744|PDB:1KT4, ECO:0007744|PDB:1KT5,
FT ECO:0007744|PDB:1KT6, ECO:0007744|PDB:1KT7"
FT DISULFID 70..174
FT /evidence="ECO:0000269|PubMed:12787682,
FT ECO:0000269|PubMed:8496140, ECO:0007744|PDB:1HBP,
FT ECO:0007744|PDB:1HBQ, ECO:0007744|PDB:1KT3,
FT ECO:0007744|PDB:1KT4, ECO:0007744|PDB:1KT5,
FT ECO:0007744|PDB:1KT6, ECO:0007744|PDB:1KT7"
FT DISULFID 120..129
FT /evidence="ECO:0000269|PubMed:12787682,
FT ECO:0000269|PubMed:8496140, ECO:0007744|PDB:1HBP,
FT ECO:0007744|PDB:1HBQ, ECO:0007744|PDB:1KT3,
FT ECO:0007744|PDB:1KT4, ECO:0007744|PDB:1KT5,
FT ECO:0007744|PDB:1KT6, ECO:0007744|PDB:1KT7"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1KT6"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:1KT6"
FT STRAND 22..30
FT /evidence="ECO:0007829|PDB:1KT6"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1KT6"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:1KT6"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:1KT6"
FT STRAND 68..79
FT /evidence="ECO:0007829|PDB:1KT6"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:1KT6"
FT STRAND 100..109
FT /evidence="ECO:0007829|PDB:1KT6"
FT STRAND 111..123
FT /evidence="ECO:0007829|PDB:1KT6"
FT STRAND 127..142
FT /evidence="ECO:0007829|PDB:1KT6"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:1KT6"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:1HBQ"
SQ SEQUENCE 183 AA; 21069 MW; D6BA064CB9E67C09 CRC64;
ERDCRVSSFR VKENFDKARF AGTWYAMAKK DPEGLFLQDN IVAEFSVDEN GHMSATAKGR
VRLLNNWDVC ADMVGTFTDT EDPAKFKMKY WGVASFLQKG NDDHWIIDTD YETFAVQYSC
RLLNLDGTCA DSYSFVFARD PSGFSPEVQK IVRQRQEELC LARQYRLIPH NGYCDGKSER
NIL
