ID   RET4_RABIT              Reviewed;         201 AA.
AC   P06912;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Retinol-binding protein 4;
DE   AltName: Full=Plasma retinol-binding protein;
DE            Short=PRBP;
DE            Short=RBP;
DE   Flags: Precursor;
GN   Name=RBP4;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1339354; DOI=10.1016/0014-4835(92)90104-z;
RA   Lee S.Y., Ubels J.L., Soprano D.R.;
RT   "The lacrimal gland synthesizes retinol-binding protein.";
RL   Exp. Eye Res. 55:163-171(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 19-201, AND SUBCELLULAR LOCATION.
RX   PubMed=3838985; DOI=10.1016/s0021-9258(18)88996-7;
RA   Sundelin J., Laurent B.C., Anundi H., Traegaardh L., Larhammar D.,
RA   Bjoerck L., Eriksson U., Aakerstroem B., Jones A., Newcomer M.,
RA   Peterson P.A., Rask L.;
RT   "Amino acid sequence homologies between rabbit, rat, and human serum
RT   retinol-binding proteins.";
RL   J. Biol. Chem. 260:6472-6480(1985).
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:0000250|UniProtKB:P02753}.
CC   -!- SUBUNIT: Interacts with TTR. Interaction with TTR prevents its loss by
CC       filtration through the kidney glomeruli. Interacts with STRA6.
CC       {ECO:0000250|UniProtKB:P02753}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3838985}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   EMBL; S45958; AAB23582.1; -; mRNA.
DR   PIR; A49178; VARB.
DR   RefSeq; NP_001075790.1; NM_001082321.1.
DR   AlphaFoldDB; P06912; -.
DR   SMR; P06912; -.
DR   STRING; 9986.ENSOCUP00000009070; -.
DR   GeneID; 100009161; -.
DR   KEGG; ocu:100009161; -.
DR   CTD; 5950; -.
DR   eggNOG; ENOG502RXEW; Eukaryota.
DR   InParanoid; P06912; -.
DR   OrthoDB; 1631943at2759; -.
DR   Proteomes; UP000001811; 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; IEA:UniProtKB-KW.
DR   GO; GO:0034632; F:retinol transmembrane transporter activity; IEA:InterPro.
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   Direct protein sequencing; Disulfide bond; Methylation; Reference proteome;
KW   Retinol-binding; Secreted; Signal; Transport; Vitamin A.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:3838985"
FT   CHAIN           19..201
FT                   /note="Retinol-binding protein 4"
FT                   /id="PRO_0000017969"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P27485"
FT   MOD_RES         139
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00724"
FT   DISULFID        22..178
FT                   /evidence="ECO:0000250|UniProtKB:P02753"
FT   DISULFID        88..192
FT                   /evidence="ECO:0000250|UniProtKB:P02753"
FT   DISULFID        138..147
FT                   /evidence="ECO:0000250|UniProtKB:P02753"
SQ   SEQUENCE   201 AA;  23102 MW;  4153FCF050184136 CRC64;
     MEWVWALVLL AALGSGRGER DCRVSSFRVK ENFDKARFAG TWYAMAKKDP EGLFLQDNIV
     AEFSVDENGH MSATAKGRVR LLNNWDVCAD MVGTFTDTED PAKFKMKYWG VASFLQRGND
     DHWIIDTDYD TFAVQYSCRL LNFDGTCADS YSFVFSRDPH GLPPDVQKLV RQRQEELCLS
     RQYRLIVHNG YCDDKSVRNL L