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   24-JAN-2024, entry version 149.
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.ENSBTAP00000057660; -.
DR   PaxDb; 9913-ENSBTAP00000000566; -.
DR   PeptideAtlas; 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   CDD; cd00743; lipocalin_RBP_like; 1.
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; RETINOL-BINDING PROTEIN 4; 1.
DR   PANTHER; PTHR11873:SF2; RETINOL-BINDING PROTEIN 4; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR   PIRSF; PIRSF500204; RBP_purpurin; 1.
DR   PRINTS; PR00179; LIPOCALIN.
DR   PRINTS; PR01174; RETINOLBNDNG.
DR   SUPFAM; SSF50814; Lipocalins; 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
//